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Conserved domains on  [gi|575501534|ref|NP_001276452|]
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multifunctional protein CAD isoform 3 [Mus musculus]

Protein Classification

carbamoyl-phosphate synthase (glutamine-hydrolyzing) large subunit; carbamoyl-phosphate synthase small subunit( domain architecture ID 12849522)

carbamoyl-phosphate synthase (glutamine-hydrolyzing) large subunit is a component of carbamoylphosphate synthetase (CPS), which catalyzes the formation of carbamoylphosphate from C02, ATP, and ammonia or glutamine, for pyrimidine biosynthesis, arginine biosynthesis, or the urea cycle; small subunit of carbamoyl phosphate synthetase (CPS) which plays a key role in both arginine and pyrimidine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 391-1440 0e+00

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


:

Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 1775.31  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   391 PPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITLHYVTQVIRNERPD 470
Cdd:TIGR01369    4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   471 GVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGY 550
Cdd:TIGR01369   84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   551 PVLVRAAFALGGLGSGFASTKEELSALVAPAFAHT--SQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHT 628
Cdd:TIGR01369  164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   629 GESIVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAK 708
Cdd:TIGR01369  244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   709 LALGIPLPELRNSVTGGT-AAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENC 787
Cdd:TIGR01369  324 LAVGYTLDELKNPVTGTTpASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   788 VGFDHT---VKPVSD--MELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHRGQALPQDL 862
Cdd:TIGR01369  404 TGFDLPdreVEPDEDlwRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPEL 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   863 LHQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDF-RAPHVLVLGSG 941
Cdd:TIGR01369  484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKKVLVLGSG 563

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   942 VYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPN 1021
Cdd:TIGR01369  564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1022 NMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVA 1101
Cdd:TIGR01369  644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1102 YTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVACDGIVSAIAISEHVENAGVHSGDATLVTPPQDITPKTLER 1181
Cdd:TIGR01369  724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1182 IKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVEPVG--LMTGSGVV 1259
Cdd:TIGR01369  804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1260 GVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPEKNILLTIGSYKNKSELLPTVRLLESLG 1339
Cdd:TIGR01369  884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1340 YSLYASLGTADFYTEHGVKVTAVDWHFEEAvdgecppqRSILDQLAENHFELVINLSMRGAGgrrlssFVTKGYRTRRLA 1419
Cdd:TIGR01369  964 YKLYATEGTAKFLGEAGIKPELVLKVSEGR--------PNILDLIKNGEIELVINTTSKGAG------TATDGYKIRREA 1029

                         1050      1060
                   ....*....|....*....|.
gi 575501534  1420 ADFSVPLIIDIKCTKLFVEAL 1440
Cdd:TIGR01369 1030 LDYGVPLITTLNTAEAFAEAL 1050
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1460-1806 0e+00

The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.


:

Pssm-ID: 238641 [Multi-domain]  Cd Length: 344  Bit Score: 592.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1460 KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASS 1539
Cdd:cd01316     1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1540 ENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPAHLPIVAHAERQSVAAVLMVAQLTQRPVHICHVARKE 1619
Cdd:cd01316    81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1620 EILLIKTAKAQGLPVTCEVAPHHLFLNREDLERlgpGKGEVRPELGSREDMEALWENMAVIDCFASDHAPHTLEEKCGPK 1699
Cdd:cd01316   161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPR---GQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1700 PPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVEVDLEHEWTVPSHMPFSKARWTPFEGQKV 1779
Cdd:cd01316   238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317

                         330       340
                  ....*....|....*....|....*..
gi 575501534 1780 KGTVRRVVLRGEVAYIDGQVLVPPGYG 1806
Cdd:cd01316   318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-355 6.92e-159

carbamoyl-phosphate synthase small subunit;


:

Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 493.44  E-value: 6.92e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534    1 MAALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDeedefglskWFESSE 80
Cdd:PRK12564    4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESDR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   81 IHVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALP-----FVDPNA 155
Cdd:PRK12564   75 PHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLLG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  156 RPLAPEVSIKTPRVFNAGGA---PRICALDCGLKYNQIRCLCQLGAEVTVVPWD---HELDSQKYDGLFLSNGPGDPASY 229
Cdd:PRK12564  155 LDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPAAL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  230 PGVVSTLSRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWA 309
Cdd:PRK12564  235 DYAIEMIRELLEKK--IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLE 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 575501534  310 PLFTNANDCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDVFLE 355
Cdd:PRK12564  313 VTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1919-2163 1.06e-96

Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis


:

Pssm-ID: 440306 [Multi-domain]  Cd Length: 306  Bit Score: 314.68  E-value: 1.06e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1919 HSLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYE--------------------------- 1971
Cdd:COG0540     1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEpstrtrlsfelaakrlgadvinfsast 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1972 -----------------------------------LAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2016
Cdd:COG0540    81 ssvskgesladtirtleaygadaivirhpqegaarLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2017 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPSVRDFVAsrgtkqEEFESIEEALPDTDVLYMTRIQKERF--GSV 2094
Cdd:COG0540   161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEIEELGV------EVTTDLDEALPDADVVYMLRIQKERFtdGLF 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501534 2095 QEYEACFGQFILTPHIMTRAKKKMVVMH--PMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2163
Cdd:COG0540   234 PSYREYKRSYGLTAERLALAKPDAIVMHpgPRNRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1842-1921 8.79e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.76  E-value: 8.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1842 PGLPDGRFHLPPRIHRASDPgLPAEEPKEKPPRKVVE------PELMGTPDGPCYPA--PPVPRQASPQNLgSSGLLHPQ 1913
Cdd:pfam03154  197 AGPTPSAPSVPPQGSPATSQ-PPNQTQSTAAPHTLIQqtptlhPQRLPSPHPPLQPMtqPPPPSQVSPQPL-PQPSLHGQ 274


                   ....*...
gi 575501534  1914 MSPLLHSL 1921
Cdd:pfam03154  275 MPPMPHSL 282
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 391-1440 0e+00

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 1775.31  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   391 PPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITLHYVTQVIRNERPD 470
Cdd:TIGR01369    4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   471 GVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGY 550
Cdd:TIGR01369   84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   551 PVLVRAAFALGGLGSGFASTKEELSALVAPAFAHT--SQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHT 628
Cdd:TIGR01369  164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   629 GESIVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAK 708
Cdd:TIGR01369  244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   709 LALGIPLPELRNSVTGGT-AAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENC 787
Cdd:TIGR01369  324 LAVGYTLDELKNPVTGTTpASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   788 VGFDHT---VKPVSD--MELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHRGQALPQDL 862
Cdd:TIGR01369  404 TGFDLPdreVEPDEDlwRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPEL 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   863 LHQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDF-RAPHVLVLGSG 941
Cdd:TIGR01369  484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKKVLVLGSG 563

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   942 VYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPN 1021
Cdd:TIGR01369  564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1022 NMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVA 1101
Cdd:TIGR01369  644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1102 YTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVACDGIVSAIAISEHVENAGVHSGDATLVTPPQDITPKTLER 1181
Cdd:TIGR01369  724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1182 IKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVEPVG--LMTGSGVV 1259
Cdd:TIGR01369  804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1260 GVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPEKNILLTIGSYKNKSELLPTVRLLESLG 1339
Cdd:TIGR01369  884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1340 YSLYASLGTADFYTEHGVKVTAVDWHFEEAvdgecppqRSILDQLAENHFELVINLSMRGAGgrrlssFVTKGYRTRRLA 1419
Cdd:TIGR01369  964 YKLYATEGTAKFLGEAGIKPELVLKVSEGR--------PNILDLIKNGEIELVINTTSKGAG------TATDGYKIRREA 1029

                         1050      1060
                   ....*....|....*....|.
gi 575501534  1420 ADFSVPLIIDIKCTKLFVEAL 1440
Cdd:TIGR01369 1030 LDYGVPLITTLNTAEAFAEAL 1050
carB PRK05294
carbamoyl-phosphate synthase large subunit;
394-1440 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1428.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITLHYVTQVIRNERPDGVL 473
Cdd:PRK05294    8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVL 553
Cdd:PRK05294   88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  554 VRAAFALGGLGSGFASTKEELSALVAPAFAH--TSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGES 631
Cdd:PRK05294  168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  632 IVVAPSQTLNDREYQLLRRTAIKVTQHLGIV-GECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLA 710
Cdd:PRK05294  248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  711 LGIPLPELRNSVTGGT-AAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVG 789
Cdd:PRK05294  328 VGYTLDEIKNDITGKTpASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  790 FDHTVKPVSDME-----LETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHrGQALPQDLLH 864
Cdd:PRK05294  408 LDEDLFEEESLEelreeLKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEN-GLPLDAELLR 486

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  865 QAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRAPHVLVLGSGVYR 944
Cdd:PRK05294  487 EAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNR 566

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  945 IGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMA 1024
Cdd:PRK05294  567 IGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLA 646

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1025 MALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVAYTD 1104
Cdd:PRK05294  647 KALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDE 726

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1105 GDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaCDGIVSAIA-ISEHVENAGVHSGDATLVTPPQDITPKTLERIK 1183
Cdd:PRK05294  727 EELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEDVLIGgIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIR 805

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1184 AIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVEPVGLMTG--SGVVGV 1261
Cdd:PRK05294  806 EYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGliPPYVAV 885

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1262 KVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPEK-NILLTIgSYKNKSELLPTVRLLESLGY 1340
Cdd:PRK05294  886 KEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLELGF 964

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1341 SLYASLGTADFYTEHGVKVTAVDWHFEEAVDgecppqrsILDQLAENHFELVINlSMRGAGGRRlssfvtKGYRTRRLAA 1420
Cdd:PRK05294  965 KILATSGTAKFLREAGIPVELVNKVHEGRPH--------IVDLIKNGEIDLVIN-TPTGRQAIR------DGFSIRRAAL 1029

                        1050      1060
                  ....*....|....*....|
gi 575501534 1421 DFSVPLIIDIKCTKLFVEAL 1440
Cdd:PRK05294 1030 EYKVPYITTLAGARAAVKAI 1049
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 399-940 0e+00

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 649.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  399 LGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITLHYVTQVIRNERPDGVLLTFGG 478
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  479 QTALNCGVELTKAGVLAryGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAF 558
Cdd:COG0458    81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  559 ALGGLGSGFASTKEELSALVAPAFAH--TSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAP 636
Cdd:COG0458   159 VLGGRGMGIVYNEEELEEYLERALKVspDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  637 SQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNpeSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:COG0458   239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  717 ELRNSvTGgtaaFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDencVGFDHTV-- 794
Cdd:COG0458   317 ELGND-TG----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLE---IGLPGTVll 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  795 KPVSD-----MELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHRgqaLPQDLLHQAKCL 869
Cdd:COG0458   389 SLVADddkeeALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEII---LVINTLLGAKSL 465

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501534  870 GFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRAPHVLVLGS 940
Cdd:COG0458   466 GDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1460-1806 0e+00

The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.


Pssm-ID: 238641 [Multi-domain]  Cd Length: 344  Bit Score: 592.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1460 KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASS 1539
Cdd:cd01316     1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1540 ENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPAHLPIVAHAERQSVAAVLMVAQLTQRPVHICHVARKE 1619
Cdd:cd01316    81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1620 EILLIKTAKAQGLPVTCEVAPHHLFLNREDLERlgpGKGEVRPELGSREDMEALWENMAVIDCFASDHAPHTLEEKCGPK 1699
Cdd:cd01316   161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPR---GQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1700 PPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVEVDLEHEWTVPSHMPFSKARWTPFEGQKV 1779
Cdd:cd01316   238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317

                         330       340
                  ....*....|....*....|....*..
gi 575501534 1780 KGTVRRVVLRGEVAYIDGQVLVPPGYG 1806
Cdd:cd01316   318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-355 6.92e-159

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 493.44  E-value: 6.92e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534    1 MAALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDeedefglskWFESSE 80
Cdd:PRK12564    4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESDR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   81 IHVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALP-----FVDPNA 155
Cdd:PRK12564   75 PHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLLG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  156 RPLAPEVSIKTPRVFNAGGA---PRICALDCGLKYNQIRCLCQLGAEVTVVPWD---HELDSQKYDGLFLSNGPGDPASY 229
Cdd:PRK12564  155 LDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPAAL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  230 PGVVSTLSRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWA 309
Cdd:PRK12564  235 DYAIEMIRELLEKK--IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLE 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 575501534  310 PLFTNANDCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDVFLE 355
Cdd:PRK12564  313 VTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 2-359 1.63e-154

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 481.36  E-value: 1.63e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534     2 AALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDeedefglskWFESSEI 81
Cdd:TIGR01368    1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDE---------DAESKGI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534    82 HVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVqkgTEPSALPF------VDPNA 155
Cdd:TIGR01368   72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVIS---TEDSNDEElvekarVSPDI 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   156 RP--LAPEVSIKTPRVFNA--GGAPRICALDCGLKYNQIRCLCQLGAEVTVVPWDHELDS-QKY--DGLFLSNGPGDPAS 228
Cdd:TIGR01368  149 TGinLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEiKKYnpDGIFLSNGPGDPAA 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   229 YPGVVSTLSRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAG- 307
Cdd:TIGR01368  229 VEPAIETIRKLLEK---IPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGd 305

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 575501534   308 WAPLFTNANDCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDVFLETVRE 359
Cdd:TIGR01368  306 LEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 2-358 4.52e-154

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 480.29  E-value: 4.52e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534    2 AALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDeedefglskWFESSEI 81
Cdd:COG0505     5 ALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDE---------DFESDRP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   82 HVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALP-----FVDPNAR 156
Cdd:COG0505    76 WVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLekaraAPGMEGL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  157 PLAPEVSIKTPRVFNAGGAP--RICALDCGLKYNQIRCLCQLGAEVTVVPWD---HELDSQKYDGLFLSNGPGDPASYPG 231
Cdd:COG0505   156 DLVKEVSTKEPYEWTEAPGAgfHVVALDFGVKRNILRELAERGCRVTVVPATtsaEEILALNPDGVFLSNGPGDPAALDY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  232 VVSTLSRVLSEpnPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPA-GWAP 310
Cdd:COG0505   236 AIETIRELLGK--GIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEV 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 575501534  311 LFTNANDCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDVFLETVR 358
Cdd:COG0505   314 THVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 514-716 1.48e-102

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 327.34  E-value: 1.48e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   514 DRRAFAARMAEIGEHVAPSEAA--NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELSALVAPAFAHT------ 585
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   586 SQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLgiHTGESIVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGEC 665
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 575501534   666 NVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:pfam02786  159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 1437-1810 5.59e-101

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 332.44  E-value: 5.59e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1437 VEALGQIGPAPPLKVHVDCmtSQKLVrLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPAL 1516
Cdd:COG0044    25 IAAIGPDLAAPEAAEVIDA--TGLLV-LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEAL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1517 ALAQKLAEAGARCDFTLFLGAS---SENAGTLGAVAGS-AAGLKLYLNETFSELRLDS----------------VAQWME 1576
Cdd:COG0044   102 EFKLARAEEKALVDVGPHGALTkglGENLAELGALAEAgAVAFKVFMGSDDGNPVLDDgllrraleyaaefgalVAVHAE 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1577 HFET------------WPAHLPIV-AHAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHL 1643
Cdd:COG0044   182 DPDLirggvmnegktsPRLGLKGRpAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHL 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1644 FLNREDLERLGPgKGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPG--FPGLETMLPLLLT-AV 1718
Cdd:COG0044   262 TLTDEDLERYGT-NFKVNPPLRTEEDREALWEGLAdgTIDVIATDHAPHTLEEKELPFAEAPngIPGLETALPLLLTeLV 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1719 SEGRLSLDDLLQRLHHNPRRIFHLP----LQEDTY---VEVDLEHEWTV-PSHMpFSKARWTPFEGQKVKGTVRRVVLRG 1790
Cdd:COG0044   341 HKGRLSLERLVELLSTNPARIFGLPrkgrIAVGADadlVLFDPDAEWTVtAEDL-HSKSKNTPFEGRELTGRVVATIVRG 419

                         410       420
                  ....*....|....*....|
gi 575501534 1791 EVAYIDGQVLVPPgYGQDVR 1810
Cdd:COG0044   420 RVVYEDGEVVGEP-RGRFLR 438
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 178-354 1.95e-97

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 311.35  E-value: 1.95e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  178 ICALDCGLKYNQIRCLCQLGAEVTVVPWDH---ELDSQKYDGLFLSNGPGDPASYPGVVSTLSRVLSEPnpRPVFGICLG 254
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTdaeEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK--IPIFGICLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  255 HQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDSLPFFSVQ 334
Cdd:cd01744    79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158

                         170       180
                  ....*....|....*....|
gi 575501534  335 FHPEHRAGPSDMELLFDVFL 354
Cdd:cd01744   159 FHPEASPGPHDTEYLFDEFL 178
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1919-2163 1.06e-96

Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440306 [Multi-domain]  Cd Length: 306  Bit Score: 314.68  E-value: 1.06e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1919 HSLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYE--------------------------- 1971
Cdd:COG0540     1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEpstrtrlsfelaakrlgadvinfsast 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1972 -----------------------------------LAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2016
Cdd:COG0540    81 ssvskgesladtirtleaygadaivirhpqegaarLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2017 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPSVRDFVAsrgtkqEEFESIEEALPDTDVLYMTRIQKERF--GSV 2094
Cdd:COG0540   161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEIEELGV------EVTTDLDEALPDADVVYMLRIQKERFtdGLF 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501534 2095 QEYEACFGQFILTPHIMTRAKKKMVVMH--PMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2163
Cdd:COG0540   234 PSYREYKRSYGLTAERLALAKPDAIVMHpgPRNRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
PLN02527 PLN02527
aspartate carbamoyltransferase
 1924-2162 2.06e-90

aspartate carbamoyltransferase


Pssm-ID: 178142 [Multi-domain]  Cd Length: 306  Bit Score: 296.66  E-value: 2.06e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1924 QHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYE-------------------------------- 1971
Cdd:PLN02527    1 SDVIEAQQFDREMLELLFEVAREMEKVERGSPGSQMLKGYLMATLFYEpstrtrlsfesamkrlggevlttenagefssa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1972 -------------------------------LAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDL 2020
Cdd:PLN02527   81 akgetledtirtvegysdiivlrhfesgaarRAAATAEIPVINAGDGPGQHPTQALLDVYTIQREIGRLDGIKVGLVGDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2021 KHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPPSVRDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFG-SVQEYE 2098
Cdd:PLN02527  161 ANGRTVRSLAYLLAKYEdVKIYFVAPDVVKMKDDIKDYLTSKGVEWEESSDLMEVASKCDVLYQTRIQRERFGeRIDLYE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575501534 2099 ACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2162
Cdd:PLN02527  241 AARGKYIVDKKVMDVLPKHAVVMHPLPRLDEITTDVDSDPRAAYFRQAKNGLFIRMALLKLLLG 304
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 1461-1796 1.11e-88

dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273302 [Multi-domain]  Cd Length: 411  Bit Score: 295.89  E-value: 1.11e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSE 1540
Cdd:TIGR00857   35 LLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQG 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1541 NAGTLGAVAGS--AAGL--KLYLNETFSELRLDSVAQWME-----------HFE---------------TWPAHLPIVA- 1589
Cdd:TIGR00857  115 NQGKELTEAYElkEAGAvgRMFTDDGSEVQDILSMRRALEyaaiagvpialHAEdpdliyggvmhegpsAAQLGLPARPp 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1590 HAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGpGKGEVRPELGSRED 1669
Cdd:TIGR00857  195 EAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLD-GNGKVNPPLREKED 273

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1670 MEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPG--FPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP-- 1743
Cdd:TIGR00857  274 RLALIEGLKdgIIDIIATDHAPHTLEEKTKEFAAAPpgIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPdk 353

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 575501534  1744 --LQEDTYVE---VDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAYID 1796
Cdd:TIGR00857  354 gtLEEGNPADitvFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
pyrC PRK09357
dihydroorotase; Validated
 1461-1796 6.49e-83

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 279.77  E-value: 6.49e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIiDAPA-----LALAQK-------------- 1521
Cdd:PRK09357   49 LVVAPGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVI-DTPEvveyvLDRAKEaglvdvlpvgaitk 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1522 ------------LAEAGARC---DftlflGASSENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWME-------HFE 1579
Cdd:PRK09357  128 glageeltefgaLKEAGVVAfsdD-----GIPVQDARLMRRALEYAKALDLLIAQHCEDPSLTEGGVMNEgevsarlGLP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1580 TWPAHlpivahAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPgKGE 1659
Cdd:PRK09357  203 GIPAV------AEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDP-NYK 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1660 VRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPGF--PGLETMLPLLLTA-VSEGRLSLDDLLQRLHH 1734
Cdd:PRK09357  276 VNPPLRTEEDREALIEGLKdgTIDAIATDHAPHAREEKECEFEAAPFgiTGLETALSLLYTTlVKTGLLDLEQLLEKMTI 355

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575501534 1735 NPRRIFHLP---LQE---DTYVEVDLEHEWTV-PSHMpFSKARWTPFEGQKVKGTVRRVVLRGEVAYID 1796
Cdd:PRK09357  356 NPARILGLPagpLAEgepADLVIFDPEAEWTVdGEDF-ASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
asp_carb_tr TIGR00670
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ...
 1925-2162 1.59e-75

aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273209 [Multi-domain]  Cd Length: 301  Bit Score: 253.82  E-value: 1.59e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1925 HILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYE--------------------------------- 1971
Cdd:TIGR00670    2 HLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEpstrtrlsfetamkrlggsvvnfsdsetssvak 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1972 -----------------------------LAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKH 2022
Cdd:TIGR00670   82 getladtiktlsgyvdaivirhplegaarLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDLKY 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  2023 GRTVHSLACLLTQYRVSLRYVAPPSLRMPPSVRDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSVQEYEACFG 2102
Cdd:TIGR00670  162 GRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEYEKVKG 241

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  2103 QFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2162
Cdd:TIGR00670  242 SYGITLERLEAAKKGVIIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 4-138 2.76e-74

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.


Pssm-ID: 460017 [Multi-domain]  Cd Length: 126  Bit Score: 243.00  E-value: 2.76e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534     4 LVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEedefglskwFESSEIHV 83
Cdd:pfam00988    1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPED---------FESDKIHV 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 575501534    84 AGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:pfam00988   72 AGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 2-138 6.46e-70

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.


Pssm-ID: 198165 [Multi-domain]  Cd Length: 130  Bit Score: 230.72  E-value: 6.46e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534      2 AALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDeedefglskWFESSEI 81
Cdd:smart01097    3 AYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDE---------DFESDKI 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 575501534     82 HVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:smart01097   74 QVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 799-921 1.68e-54

Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 198164 [Multi-domain]  Cd Length: 124  Bit Score: 186.12  E-value: 1.68e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534    799 DMELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHRGQALPQDLLHQAKCLGFSDKQIAL 878
Cdd:smart01096    2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 575501534    879 AVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTY 921
Cdd:smart01096   82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
MGS_CPS_I_III cd01423
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ...
 1313-1438 1.08e-41

Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.


Pssm-ID: 238711 [Multi-domain]  Cd Length: 116  Bit Score: 149.37  E-value: 1.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1313 KNILLTIGSYkNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGEcppqRSILDQLAENHFELV 1392
Cdd:cd01423     1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK----PSLRELLAEGKIDLV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 575501534 1393 INLSMRGAGGRRLSsfvtkGYRTRRLAADFSVPLIIDIKCTKLFVE 1438
Cdd:cd01423    76 INLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
OTCace pfam00185
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;
2013-2160 1.29e-38

Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;


Pssm-ID: 425511 [Multi-domain]  Cd Length: 154  Bit Score: 141.98  E-value: 1.29e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  2013 TITMVGDlKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPSV----RDFVASRGTKQEEFESIEEALPDTDVLYMTRIQ- 2087
Cdd:pfam00185    1 KIAYVGD-GHNNVAHSLIIAAAKLGMDVRLATPKGYPPDPEVldkaKKIAEKSGGSIEITDDPAEAVKGADVVYTDVWQs 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575501534  2088 ----KERFgsvQEYEAcFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATV 2160
Cdd:pfam00185   80 mgqeKERE---ERLKA-FKPYQVNEELMKLAKKDAIFMHCLPahRGEEVTDDVFDGPRSVVFDQAENRLHAQKALLALL 154
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 1464-1792 5.46e-07

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 54.04  E-value: 5.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1464 LPGLIDVHVHLR--------EPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDApalalaqkLAEAgarcdftlfl 1535
Cdd:pfam01979    3 LPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEA--------LLEA---------- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1536 gASSENAGtLGAVAGSAAGLKLYLNETFSELRLDSVAQWM-EHFETWPAHLPIVAHAERQSV-----AAVLMVAQLTQRP 1609
Cdd:pfam01979   65 -AEELPLG-LRFLGPGCSLDTDGELEGRKALREKLKAGAEfIKGMADGVVFVGLAPHGAPTFsddelKAALEEAKKYGLP 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1610 VHIcHVARKEEILLIKTAKAQG----------------LPVTCEVAPHHLFLNREDLERLGPGKGEVR------PELGSR 1667
Cdd:pfam01979  143 VAI-HALETKGEVEDAIAAFGGgiehgthlevaesgglLDIIKLILAHGVHLSPTEANLLAEHLKGAGvahcpfSNSKLR 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1668 EDMEALWE--NMAVIDCFASDHAPHTleekcgpkpPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQ 1745
Cdd:pfam01979  222 SGRIALRKalEDGVKVGLGTDGAGSG---------NSLNMLEELRLALELQFDPEGGLSPLEALRMATINPAKALGLDDK 292

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 575501534  1746 EDTyVEV----DLehewtvpshMPFSKARWTPFEGQKVKGTVRRVVLRGEV 1792
Cdd:pfam01979  293 VGS-IEVgkdaDL---------VVVDLDPLAAFFGLKPDGNVKKVIVKGKI 333
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1842-1921 8.79e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.76  E-value: 8.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1842 PGLPDGRFHLPPRIHRASDPgLPAEEPKEKPPRKVVE------PELMGTPDGPCYPA--PPVPRQASPQNLgSSGLLHPQ 1913
Cdd:pfam03154  197 AGPTPSAPSVPPQGSPATSQ-PPNQTQSTAAPHTLIQqtptlhPQRLPSPHPPLQPMtqPPPPSQVSPQPL-PQPSLHGQ 274


                   ....*...
gi 575501534  1914 MSPLLHSL 1921
Cdd:pfam03154  275 MPPMPHSL 282
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 391-1440 0e+00

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 1775.31  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   391 PPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITLHYVTQVIRNERPD 470
Cdd:TIGR01369    4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   471 GVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGY 550
Cdd:TIGR01369   84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   551 PVLVRAAFALGGLGSGFASTKEELSALVAPAFAHT--SQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHT 628
Cdd:TIGR01369  164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   629 GESIVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAK 708
Cdd:TIGR01369  244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   709 LALGIPLPELRNSVTGGT-AAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENC 787
Cdd:TIGR01369  324 LAVGYTLDELKNPVTGTTpASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   788 VGFDHT---VKPVSD--MELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHRGQALPQDL 862
Cdd:TIGR01369  404 TGFDLPdreVEPDEDlwRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPEL 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   863 LHQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDF-RAPHVLVLGSG 941
Cdd:TIGR01369  484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKKVLVLGSG 563

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   942 VYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPN 1021
Cdd:TIGR01369  564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1022 NMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVA 1101
Cdd:TIGR01369  644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1102 YTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVACDGIVSAIAISEHVENAGVHSGDATLVTPPQDITPKTLER 1181
Cdd:TIGR01369  724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1182 IKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVEPVG--LMTGSGVV 1259
Cdd:TIGR01369  804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1260 GVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPEKNILLTIGSYKNKSELLPTVRLLESLG 1339
Cdd:TIGR01369  884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1340 YSLYASLGTADFYTEHGVKVTAVDWHFEEAvdgecppqRSILDQLAENHFELVINLSMRGAGgrrlssFVTKGYRTRRLA 1419
Cdd:TIGR01369  964 YKLYATEGTAKFLGEAGIKPELVLKVSEGR--------PNILDLIKNGEIELVINTTSKGAG------TATDGYKIRREA 1029

                         1050      1060
                   ....*....|....*....|.
gi 575501534  1420 ADFSVPLIIDIKCTKLFVEAL 1440
Cdd:TIGR01369 1030 LDYGVPLITTLNTAEAFAEAL 1050
carB PRK05294
carbamoyl-phosphate synthase large subunit;
394-1440 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1428.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITLHYVTQVIRNERPDGVL 473
Cdd:PRK05294    8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVL 553
Cdd:PRK05294   88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  554 VRAAFALGGLGSGFASTKEELSALVAPAFAH--TSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGES 631
Cdd:PRK05294  168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  632 IVVAPSQTLNDREYQLLRRTAIKVTQHLGIV-GECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLA 710
Cdd:PRK05294  248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  711 LGIPLPELRNSVTGGT-AAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVG 789
Cdd:PRK05294  328 VGYTLDEIKNDITGKTpASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  790 FDHTVKPVSDME-----LETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHrGQALPQDLLH 864
Cdd:PRK05294  408 LDEDLFEEESLEelreeLKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEN-GLPLDAELLR 486

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  865 QAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRAPHVLVLGSGVYR 944
Cdd:PRK05294  487 EAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNR 566

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  945 IGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMA 1024
Cdd:PRK05294  567 IGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLA 646

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1025 MALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVAYTD 1104
Cdd:PRK05294  647 KALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDE 726

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1105 GDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaCDGIVSAIA-ISEHVENAGVHSGDATLVTPPQDITPKTLERIK 1183
Cdd:PRK05294  727 EELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEDVLIGgIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIR 805

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1184 AIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVEPVGLMTG--SGVVGV 1261
Cdd:PRK05294  806 EYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGliPPYVAV 885

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1262 KVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPEK-NILLTIgSYKNKSELLPTVRLLESLGY 1340
Cdd:PRK05294  886 KEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLELGF 964

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1341 SLYASLGTADFYTEHGVKVTAVDWHFEEAVDgecppqrsILDQLAENHFELVINlSMRGAGGRRlssfvtKGYRTRRLAA 1420
Cdd:PRK05294  965 KILATSGTAKFLREAGIPVELVNKVHEGRPH--------IVDLIKNGEIDLVIN-TPTGRQAIR------DGFSIRRAAL 1029

                        1050      1060
                  ....*....|....*....|
gi 575501534 1421 DFSVPLIIDIKCTKLFVEAL 1440
Cdd:PRK05294 1030 EYKVPYITTLAGARAAVKAI 1049
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 394-1448 0e+00

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 1077.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITLHYVTQVIRNERPDGVL 473
Cdd:PRK12815    8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVL 553
Cdd:PRK12815   88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  554 VRAAFALGGLGSGFASTKEELSALVAPAFA--HTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGES 631
Cdd:PRK12815  168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQasPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDS 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  632 IVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLAL 711
Cdd:PRK12815  248 IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  712 GIPLPELRNSVTGGT-AAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALR--MVDENCV 788
Cdd:PRK12815  328 GYTLNELKNPVTGLTyASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRslEIKRNGL 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  789 GFDHTVKPVSDMEL----ETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHRGQaLPQDLLH 864
Cdd:PRK12815  408 SLPIELSGKSDEELlqdlRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLD-LSADLLR 486

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  865 QAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNThDLDFRA--PHVLVLGSGV 942
Cdd:PRK12815  487 KVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGES-EAEPSSekKKVLILGSGP 565

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  943 YRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNN 1022
Cdd:PRK12815  566 IRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTAIN 645

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1023 MAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVAY 1102
Cdd:PRK12815  646 LAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVY 725

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1103 TDGDLERFLssAAAVSKEHPVVISKFIqEAKEIDVDAVaCDGIVSAIA-ISEHVENAGVHSGDATLVTPPQDITPKTLER 1181
Cdd:PRK12815  726 DEPALEAYL--AENASQLYPILIDQFI-DGKEYEVDAI-SDGEDVTIPgIIEHIEQAGVHSGDSIAVLPPQSLSEEQQEK 801

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1182 IKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMG----EKVEPVGLMTGSG 1257
Cdd:PRK12815  802 IRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGkslaELGYPNGLWPGSP 881

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1258 VVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPEKNILLTIGSYKNKSELLPTVRLLES 1337
Cdd:PRK12815  882 FIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLARRFAQ 961

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1338 LGYSLYASLGTADFYTEHGVKVTAVdwhfeeAVDGECPPQRSILDQLAENHFELVINLSMRGaggrrlssfVTKGYRTRR 1417
Cdd:PRK12815  962 LGFKLLATEGTANWLAEEGITTGVV------EKVQEGSPSLLERIKQHRIVLVVNTSLSDSA---------SEDAIKIRD 1026

                        1050      1060      1070
                  ....*....|....*....|....*....|.
gi 575501534 1418 LAADFSVPLIIDIKCTKLFVEALGQIGPAPP 1448
Cdd:PRK12815 1027 EALSTHIPVFTELETAQAFLQVLESLALTTQ 1057
PLN02735 PLN02735
carbamoyl-phosphate synthase
 394-1440 0e+00

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 877.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITLHYVTQVIRNERPDGVL 473
Cdd:PLN02735   24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLG-YPV 552
Cdd:PLN02735  104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  553 LVRAAFALGGLGSGFASTKEELSALVAPAFA--HTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGE 630
Cdd:PLN02735  184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAasITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  631 SIVVAPSQTLNDREYQLLRRTAIKVTQHLGIvgEC---NVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAA 707
Cdd:PLN02735  264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  708 KLALGIPLPELRNSVTGGT-AAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDEN 786
Cdd:PLN02735  342 KLSVGYTLDQIPNDITLKTpASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  787 CVGFdhTVKPVSDME---------LETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHRGQA 857
Cdd:PLN02735  422 FSGW--GCAKVKELDwdweqlkykLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLSE 499

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  858 LPQDLLHQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRAPHVLV 937
Cdd:PLN02735  500 LSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLI 579

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  938 LGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGG 1017
Cdd:PLN02735  580 LGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGG 659

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1018 QLPNNMAMALHRQ-------------QCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHTVGYP 1084
Cdd:PLN02735  660 QTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYP 739

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1085 CVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVA-CDGIVSAIAISEHVENAGVHSG 1163
Cdd:PLN02735  740 VVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSG 819

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1164 DATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFNLQL-IAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRII 1242
Cdd:PLN02735  820 DSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVM 899

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1243 MGEKVEPVGLmTGSGV---VGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPEKNILLTI 1319
Cdd:PLN02735  900 SGKSLKDLGF-TEEVIpahVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGTVFIS 978

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1320 GSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAV-DWHfeeavdgECPPQrsILDQLAENHFELVINLSMR 1398
Cdd:PLN02735  979 LNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVlKLH-------EGRPH--AGDMLANGQIQLMVITSSG 1049

                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|..
gi 575501534 1399 GAGGRRlssfvtKGYRTRRLAADFSVPLIIDIKCTKLFVEAL 1440
Cdd:PLN02735 1050 DALDQK------DGRQLRRMALAYKVPIITTVAGALATAQAV 1085
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 399-940 0e+00

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 649.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  399 LGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITLHYVTQVIRNERPDGVLLTFGG 478
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  479 QTALNCGVELTKAGVLAryGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAF 558
Cdd:COG0458    81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  559 ALGGLGSGFASTKEELSALVAPAFAH--TSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAP 636
Cdd:COG0458   159 VLGGRGMGIVYNEEELEEYLERALKVspDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  637 SQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNpeSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:COG0458   239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  717 ELRNSvTGgtaaFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDencVGFDHTV-- 794
Cdd:COG0458   317 ELGND-TG----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLE---IGLPGTVll 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  795 KPVSD-----MELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHRgqaLPQDLLHQAKCL 869
Cdd:COG0458   389 SLVADddkeeALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEII---LVINTLLGAKSL 465

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501534  870 GFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRAPHVLVLGS 940
Cdd:COG0458   466 GDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1460-1806 0e+00

The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.


Pssm-ID: 238641 [Multi-domain]  Cd Length: 344  Bit Score: 592.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1460 KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASS 1539
Cdd:cd01316     1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1540 ENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPAHLPIVAHAERQSVAAVLMVAQLTQRPVHICHVARKE 1619
Cdd:cd01316    81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1620 EILLIKTAKAQGLPVTCEVAPHHLFLNREDLERlgpGKGEVRPELGSREDMEALWENMAVIDCFASDHAPHTLEEKCGPK 1699
Cdd:cd01316   161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPR---GQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1700 PPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVEVDLEHEWTVPSHMPFSKARWTPFEGQKV 1779
Cdd:cd01316   238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317

                         330       340
                  ....*....|....*....|....*..
gi 575501534 1780 KGTVRRVVLRGEVAYIDGQVLVPPGYG 1806
Cdd:cd01316   318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 938-1440 3.47e-176

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 548.71  E-value: 3.47e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  938 LGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGG 1017
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1018 QLPNNMAMALHRQQ----CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHTVGYPCVVRPSYVL 1093
Cdd:COG0458    81 QTALNLAVELEEAGilegVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1094 SGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaCDG----IVsaIAISEHVENAGVHSGDATLVT 1169
Cdd:COG0458   161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVV-RDGednvII--VGIMEHIEPAGVHSGDSICVA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1170 PPQDITPKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVEP 1249
Cdd:COG0458   238 PPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1250 VGLMTG----SGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPeKNILLTIGSYKNK 1325
Cdd:COG0458   318 LGNDTGfeptLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP-GTVLLSLVADDDK 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1326 SELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILDQLAENHFELVINLSMRGAGGRRL 1405
Cdd:COG0458   397 EEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEG--------RPIIVDEIELEEIILVINTLLGAKSLGDS 468

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 575501534 1406 SSF------VTKGYRTRRLAADFSVPLIIDIKCTKLFVEAL 1440
Cdd:COG0458   469 DGIirralaAKVPYVTTLAAAAAAALAIKAVETEAGEFEEA 509
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-355 6.92e-159

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 493.44  E-value: 6.92e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534    1 MAALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDeedefglskWFESSE 80
Cdd:PRK12564    4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESDR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   81 IHVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALP-----FVDPNA 155
Cdd:PRK12564   75 PHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLLG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  156 RPLAPEVSIKTPRVFNAGGA---PRICALDCGLKYNQIRCLCQLGAEVTVVPWD---HELDSQKYDGLFLSNGPGDPASY 229
Cdd:PRK12564  155 LDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPAAL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  230 PGVVSTLSRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWA 309
Cdd:PRK12564  235 DYAIEMIRELLEKK--IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLE 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 575501534  310 PLFTNANDCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDVFLE 355
Cdd:PRK12564  313 VTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 2-359 1.63e-154

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 481.36  E-value: 1.63e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534     2 AALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDeedefglskWFESSEI 81
Cdd:TIGR01368    1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDE---------DAESKGI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534    82 HVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVqkgTEPSALPF------VDPNA 155
Cdd:TIGR01368   72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVIS---TEDSNDEElvekarVSPDI 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   156 RP--LAPEVSIKTPRVFNA--GGAPRICALDCGLKYNQIRCLCQLGAEVTVVPWDHELDS-QKY--DGLFLSNGPGDPAS 228
Cdd:TIGR01368  149 TGinLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEiKKYnpDGIFLSNGPGDPAA 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   229 YPGVVSTLSRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAG- 307
Cdd:TIGR01368  229 VEPAIETIRKLLEK---IPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGd 305

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 575501534   308 WAPLFTNANDCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDVFLETVRE 359
Cdd:TIGR01368  306 LEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 2-358 4.52e-154

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 480.29  E-value: 4.52e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534    2 AALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDeedefglskWFESSEI 81
Cdd:COG0505     5 ALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDE---------DFESDRP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   82 HVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALP-----FVDPNAR 156
Cdd:COG0505    76 WVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLekaraAPGMEGL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  157 PLAPEVSIKTPRVFNAGGAP--RICALDCGLKYNQIRCLCQLGAEVTVVPWD---HELDSQKYDGLFLSNGPGDPASYPG 231
Cdd:COG0505   156 DLVKEVSTKEPYEWTEAPGAgfHVVALDFGVKRNILRELAERGCRVTVVPATtsaEEILALNPDGVFLSNGPGDPAALDY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  232 VVSTLSRVLSEpnPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPA-GWAP 310
Cdd:COG0505   236 AIETIRELLGK--GIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEV 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 575501534  311 LFTNANDCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDVFLETVR 358
Cdd:COG0505   314 THVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 4-361 2.59e-124

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 396.18  E-value: 2.59e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534    4 LVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEedefglskwFESSEIHV 83
Cdd:PRK12838    5 LILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADD---------YESKQPQV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   84 AGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSA---LPFVDPNArpLAP 160
Cdd:PRK12838   76 KGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDDAHAFdqiKALVLPKN--VVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  161 EVSIKTPRVFNAGGaPRICALDCGLKYNQIRCLCQLGAEVTVVPWD---HELDSQKYDGLFLSNGPGDPASYPGVVSTLS 237
Cdd:PRK12838  154 QVSTKEPYTYGNGG-KHVALIDFGYKKSILRSLSKRGCKVTVLPYDtslEEIKNLNPDGIVLSNGPGDPKELQPYLPEIK 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  238 RVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSL-PAGWAPLFTNAN 316
Cdd:PRK12838  233 KLISS---YPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRFFNVN 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 575501534  317 DCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDVFLETVREAA 361
Cdd:PRK12838  310 DGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKAR 354
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
 1461-1786 3.93e-118

Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.


Pssm-ID: 238627 [Multi-domain]  Cd Length: 337  Bit Score: 377.50  E-value: 3.93e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1461 LVRLPGLIDVHVHLREPGGT-HKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASS 1539
Cdd:cd01302     1 LLVLPGFIDIHVHLRDPGGTtYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1540 E-NAGTL-GAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPA-HLPIVAHAERqsvaaVLMVAQLTQRPVHICHVA 1616
Cdd:cd01302    81 GdVTDELkKLFDAGINSLKVFMNYYFGELFDVDDGTLMRTFLEIASrGGPVMVHAER-----AAQLAEEAGANVHIAHVS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1617 RKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPgKGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEE 1694
Cdd:cd01302   156 SGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGA-WGKVNPPLRSKEDREALWEGVKngKIDTIASDHAPHSKEE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1695 KCGPKPPPGFPG----LETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQED---------TYVEVDLEHEWTVP 1761
Cdd:cd01302   235 KESGKDIWKAPPgfpgLETRLPILLTEGVKRGLSLETLVEILSENPARIFGLYPKGTiavgydadlVIVDPKKEWKVTAE 314

                         330       340
                  ....*....|....*....|....*
gi 575501534 1762 SHMpfSKARWTPFEGQKVKGTVRRV 1786
Cdd:cd01302   315 EIE--SKADWTPFEGMEVTGKPVST 337
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 514-716 1.48e-102

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 327.34  E-value: 1.48e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   514 DRRAFAARMAEIGEHVAPSEAA--NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELSALVAPAFAHT------ 585
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   586 SQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLgiHTGESIVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGEC 665
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 575501534   666 NVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:pfam02786  159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 1437-1810 5.59e-101

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 332.44  E-value: 5.59e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1437 VEALGQIGPAPPLKVHVDCmtSQKLVrLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPAL 1516
Cdd:COG0044    25 IAAIGPDLAAPEAAEVIDA--TGLLV-LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEAL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1517 ALAQKLAEAGARCDFTLFLGAS---SENAGTLGAVAGS-AAGLKLYLNETFSELRLDS----------------VAQWME 1576
Cdd:COG0044   102 EFKLARAEEKALVDVGPHGALTkglGENLAELGALAEAgAVAFKVFMGSDDGNPVLDDgllrraleyaaefgalVAVHAE 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1577 HFET------------WPAHLPIV-AHAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHL 1643
Cdd:COG0044   182 DPDLirggvmnegktsPRLGLKGRpAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHL 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1644 FLNREDLERLGPgKGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPG--FPGLETMLPLLLT-AV 1718
Cdd:COG0044   262 TLTDEDLERYGT-NFKVNPPLRTEEDREALWEGLAdgTIDVIATDHAPHTLEEKELPFAEAPngIPGLETALPLLLTeLV 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1719 SEGRLSLDDLLQRLHHNPRRIFHLP----LQEDTY---VEVDLEHEWTV-PSHMpFSKARWTPFEGQKVKGTVRRVVLRG 1790
Cdd:COG0044   341 HKGRLSLERLVELLSTNPARIFGLPrkgrIAVGADadlVLFDPDAEWTVtAEDL-HSKSKNTPFEGRELTGRVVATIVRG 419

                         410       420
                  ....*....|....*....|
gi 575501534 1791 EVAYIDGQVLVPPgYGQDVR 1810
Cdd:COG0044   420 RVVYEDGEVVGEP-RGRFLR 438
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 178-354 1.95e-97

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 311.35  E-value: 1.95e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  178 ICALDCGLKYNQIRCLCQLGAEVTVVPWDH---ELDSQKYDGLFLSNGPGDPASYPGVVSTLSRVLSEPnpRPVFGICLG 254
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTdaeEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK--IPIFGICLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  255 HQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDSLPFFSVQ 334
Cdd:cd01744    79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158

                         170       180
                  ....*....|....*....|
gi 575501534  335 FHPEHRAGPSDMELLFDVFL 354
Cdd:cd01744   159 FHPEASPGPHDTEYLFDEFL 178
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1919-2163 1.06e-96

Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440306 [Multi-domain]  Cd Length: 306  Bit Score: 314.68  E-value: 1.06e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1919 HSLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYE--------------------------- 1971
Cdd:COG0540     1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEpstrtrlsfelaakrlgadvinfsast 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1972 -----------------------------------LAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2016
Cdd:COG0540    81 ssvskgesladtirtleaygadaivirhpqegaarLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2017 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPSVRDFVAsrgtkqEEFESIEEALPDTDVLYMTRIQKERF--GSV 2094
Cdd:COG0540   161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEIEELGV------EVTTDLDEALPDADVVYMLRIQKERFtdGLF 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501534 2095 QEYEACFGQFILTPHIMTRAKKKMVVMH--PMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2163
Cdd:COG0540   234 PSYREYKRSYGLTAERLALAKPDAIVMHpgPRNRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
PLN02527 PLN02527
aspartate carbamoyltransferase
 1924-2162 2.06e-90

aspartate carbamoyltransferase


Pssm-ID: 178142 [Multi-domain]  Cd Length: 306  Bit Score: 296.66  E-value: 2.06e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1924 QHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYE-------------------------------- 1971
Cdd:PLN02527    1 SDVIEAQQFDREMLELLFEVAREMEKVERGSPGSQMLKGYLMATLFYEpstrtrlsfesamkrlggevlttenagefssa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1972 -------------------------------LAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDL 2020
Cdd:PLN02527   81 akgetledtirtvegysdiivlrhfesgaarRAAATAEIPVINAGDGPGQHPTQALLDVYTIQREIGRLDGIKVGLVGDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2021 KHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPPSVRDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFG-SVQEYE 2098
Cdd:PLN02527  161 ANGRTVRSLAYLLAKYEdVKIYFVAPDVVKMKDDIKDYLTSKGVEWEESSDLMEVASKCDVLYQTRIQRERFGeRIDLYE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575501534 2099 ACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2162
Cdd:PLN02527  241 AARGKYIVDKKVMDVLPKHAVVMHPLPRLDEITTDVDSDPRAAYFRQAKNGLFIRMALLKLLLG 304
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 1461-1796 1.11e-88

dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273302 [Multi-domain]  Cd Length: 411  Bit Score: 295.89  E-value: 1.11e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSE 1540
Cdd:TIGR00857   35 LLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQG 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1541 NAGTLGAVAGS--AAGL--KLYLNETFSELRLDSVAQWME-----------HFE---------------TWPAHLPIVA- 1589
Cdd:TIGR00857  115 NQGKELTEAYElkEAGAvgRMFTDDGSEVQDILSMRRALEyaaiagvpialHAEdpdliyggvmhegpsAAQLGLPARPp 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1590 HAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGpGKGEVRPELGSRED 1669
Cdd:TIGR00857  195 EAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLD-GNGKVNPPLREKED 273

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1670 MEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPG--FPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP-- 1743
Cdd:TIGR00857  274 RLALIEGLKdgIIDIIATDHAPHTLEEKTKEFAAAPpgIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPdk 353

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 575501534  1744 --LQEDTYVE---VDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAYID 1796
Cdd:TIGR00857  354 gtLEEGNPADitvFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
 1464-1790 2.38e-88

Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.


Pssm-ID: 238643 [Multi-domain]  Cd Length: 361  Bit Score: 293.09  E-value: 2.38e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENAG 1543
Cdd:cd01318     5 LPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTGSEDL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1544 TLgAVAGSAAGLKLYLNETFSELRLDsvaqwMEHFETWPAH--LPIVAHAERQ--------------------------- 1594
Cdd:cd01318    85 EE-LDKAPPAGYKIFMGDSTGDLLDD-----EETLERIFAEgsVLVTFHAEDEdrlrenrkelkgesahprirdaeaaav 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1595 SVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQglpVTCEVAPHHLFLNREDLERLGpGKGEVRPELGSREDMEALW 1674
Cdd:cd01318   159 ATARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDRLG-TLGKVNPPLRSREDRKALL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1675 ENMA--VIDCFASDHAPHTLEEKCGPKPPPGF--PGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPL---QED 1747
Cdd:cd01318   235 QALAdgRIDVIASDHAPHTLEEKRKGYPAAPSgiPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIFGIKNkgrIAE 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 575501534 1748 TY----VEVDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRG 1790
Cdd:cd01318   315 GYdadlTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
pyrB PRK00856
aspartate carbamoyltransferase catalytic subunit;
1920-2163 4.86e-86

aspartate carbamoyltransferase catalytic subunit;


Pssm-ID: 234849 [Multi-domain]  Cd Length: 305  Bit Score: 284.27  E-value: 4.86e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1920 SLVGQHILSVKQFTKDQMSHLFNVAHTLR-MMVQKERSLDILKGKVMASMFYE--------------------------- 1971
Cdd:PRK00856    2 PLKMKHLLSIEDLSREEIELLLDTAEEFKeVLRREVKKVPLLRGKTVANLFFEpstrtrlsfelaakrlgadvinfsast 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1972 -----------------------------------LAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2016
Cdd:PRK00856   82 ssvskgetladtirtlsamgadaivirhpqsgaarLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVAI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2017 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPSVRDFvasrgtkqEEFESIEEALPDTDVLYMTRIQKERF--GSV 2094
Cdd:PRK00856  162 VGDIKHSRVARSNIQALTRLGAEVRLIAPPTL-LPEGMPEY--------GVHTDLDEVIEDADVVMMLRVQKERMdgGLL 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501534 2095 QEYEACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2163
Cdd:PRK00856  233 PSYEEYKRSYGLTAERLALAKPDAIVMHPGPvnRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLELLLGG 303
pyrC PRK09357
dihydroorotase; Validated
 1461-1796 6.49e-83

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 279.77  E-value: 6.49e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIiDAPA-----LALAQK-------------- 1521
Cdd:PRK09357   49 LVVAPGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVI-DTPEvveyvLDRAKEaglvdvlpvgaitk 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1522 ------------LAEAGARC---DftlflGASSENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWME-------HFE 1579
Cdd:PRK09357  128 glageeltefgaLKEAGVVAfsdD-----GIPVQDARLMRRALEYAKALDLLIAQHCEDPSLTEGGVMNEgevsarlGLP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1580 TWPAHlpivahAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPgKGE 1659
Cdd:PRK09357  203 GIPAV------AEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDP-NYK 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1660 VRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPGF--PGLETMLPLLLTA-VSEGRLSLDDLLQRLHH 1734
Cdd:PRK09357  276 VNPPLRTEEDREALIEGLKdgTIDAIATDHAPHAREEKECEFEAAPFgiTGLETALSLLYTTlVKTGLLDLEQLLEKMTI 355

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575501534 1735 NPRRIFHLP---LQE---DTYVEVDLEHEWTV-PSHMpFSKARWTPFEGQKVKGTVRRVVLRGEVAYID 1796
Cdd:PRK09357  356 NPARILGLPagpLAEgepADLVIFDPEAEWTVdGEDF-ASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 2-355 1.82e-82

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 277.06  E-value: 1.82e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534    2 AALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEedefglskwFESSEI 81
Cdd:CHL00197    7 AILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLED---------IESVKI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   82 HVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALP--FVDPNARP-- 157
Cdd:CHL00197   78 QVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSYLRakIKESPHMPss 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  158 -LAPEVSIKTPRVFNAGGAP----------------RICALDCGLKYNQIRCLCQLGAEVTVVPWD---HELDSQKYDGL 217
Cdd:CHL00197  158 dLIPRVTTSSYYEWDEKSHPsfyladnkrphssyqlKIIVIDFGVKYNILRRLKSFGCSITVVPATspyQDILSYQPDGI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  218 FLSNGPGDPASYPGVVSTLSRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPcllVGTGRCF-LTSQNHG 296
Cdd:CHL00197  238 LLSNGPGDPSAIHYGIKTVKKLLKYN--IPIFGICMGHQILSLALEAKTFKLKFGHRGLNHP---SGLNQQVeITSQNHG 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501534  297 FAVDADSL--PAGWAPLFtNANDCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDVFLE 355
Cdd:CHL00197  313 FAVNLESLakNKFYITHF-NLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIE 372
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 2-350 1.94e-77

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 263.76  E-value: 1.94e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534    2 AALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEEdefglskwfESSEI 81
Cdd:PLN02771   57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDE---------ESRQC 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   82 HVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVQKG--TEPSALPFV---DPNAR 156
Cdd:PLN02771  128 FLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDskTDEELLKMSrswDIVGI 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  157 PLAPEVSIKTPRV----------FNAGGAP----RICALDCGLKYNQIRCLCQLGAEVTVVP--WD-HELDSQKYDGLFL 219
Cdd:PLN02771  208 DLISGVSCKSPYEwvdktnpewdFNTNSRDgesyHVIAYDFGIKHNILRRLASYGCKITVVPstWPaSEALKMKPDGVLF 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  220 SNGPGDPASYPGVVSTLSRVLSEPnprPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAV 299
Cdd:PLN02771  288 SNGPGDPSAVPYAVETVKELLGKV---PVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAV 364

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 575501534  300 DADSLPAGWAPLFTNANDCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLF 350
Cdd:PLN02771  365 DPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
asp_carb_tr TIGR00670
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ...
 1925-2162 1.59e-75

aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273209 [Multi-domain]  Cd Length: 301  Bit Score: 253.82  E-value: 1.59e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1925 HILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYE--------------------------------- 1971
Cdd:TIGR00670    2 HLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEpstrtrlsfetamkrlggsvvnfsdsetssvak 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1972 -----------------------------LAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKH 2022
Cdd:TIGR00670   82 getladtiktlsgyvdaivirhplegaarLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDLKY 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  2023 GRTVHSLACLLTQYRVSLRYVAPPSLRMPPSVRDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSVQEYEACFG 2102
Cdd:TIGR00670  162 GRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEYEKVKG 241

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  2103 QFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2162
Cdd:TIGR00670  242 SYGITLERLEAAKKGVIIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 4-138 2.76e-74

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.


Pssm-ID: 460017 [Multi-domain]  Cd Length: 126  Bit Score: 243.00  E-value: 2.76e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534     4 LVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEedefglskwFESSEIHV 83
Cdd:pfam00988    1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPED---------FESDKIHV 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 575501534    84 AGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:pfam00988   72 AGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
PRK04250 PRK04250
dihydroorotase; Provisional
 1464-1803 5.09e-72

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 247.37  E-value: 5.09e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTL-FLGASseNA 1542
Cdd:PRK04250   46 LPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALnFLIAG--NC 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1543 GTLGAVA--------GSAAGlKLYLnETFSE-----LRLDSV-AQWMEHFETWPAHLPIvahAERQSVAAVLMVAQLTQR 1608
Cdd:PRK04250  124 EKAEEIKadfykifmGASTG-GIFS-ENFEVdyacaPGIVSVhAEDPELIREFPERPPE---AEVVAIERALEAGKKLKK 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1609 PVHICHVARKEEILLIKtaKAQGLPVTCEVAPHHLFLNREDLERlGPgKGEVRPELGSREDMEALWENMAVIDCFASDHA 1688
Cdd:PRK04250  199 PLHICHISTKDGLKLIL--KSNLPWVSFEVTPHHLFLTRKDYER-NP-LLKVYPPLRSEEDRKALWENFSKIPIIASDHA 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1689 PHTLEEKcgPKPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPL------QEDTYVEVDLEHEWTVPS 1762
Cdd:PRK04250  275 PHTLEDK--EAGAAGIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIKNygieegNYANFAVFDMKKEWTIKA 352

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 575501534 1763 HMPFSKARWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1803
Cdd:PRK04250  353 EELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKP 393
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 2-138 6.46e-70

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.


Pssm-ID: 198165 [Multi-domain]  Cd Length: 130  Bit Score: 230.72  E-value: 6.46e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534      2 AALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDeedefglskWFESSEI 81
Cdd:smart01097    3 AYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDE---------DFESDKI 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 575501534     82 HVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:smart01097   74 QVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 1453-1786 4.41e-68

Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.


Pssm-ID: 238642 [Multi-domain]  Cd Length: 374  Bit Score: 235.21  E-value: 4.41e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1453 VDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIiDAPAL--ALAQKLAEAGARCD 1530
Cdd:cd01317     5 IDA---EGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVI-DNPAVveLLKNRAKDVGIVRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1531 FTL------FLGASSENAGTL---GAVAGSAAGLKLYLNETfselrLDSVAQWMEHFEtwpahLPIVAH----------- 1590
Cdd:cd01317    81 LPIgaltkgLKGEELTEIGELleaGAVGFSDDGKPIQDAEL-----LRRALEYAAMLD-----LPIIVHpedpslagggv 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1591 ------------------AERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLER 1652
Cdd:cd01317   151 mnegkvasrlglpgippeAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALES 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1653 LGPGkGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPG--FPGLETMLPLLLT-AVSEGRLSLDD 1727
Cdd:cd01317   231 YDTN-AKVNPPLRSEEDREALIEALKdgTIDAIASDHAPHTDEEKDLPFAEAPpgIIGLETALPLLWTlLVKGGLLTLPD 309

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575501534 1728 LLQRLHHNPRRIFHLPLQEDTYVE------VDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRV 1786
Cdd:cd01317   310 LIRALSTNPAKILGLPPGRLEVGApadlvlFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
PRK02382 PRK02382
dihydroorotase; Provisional
 1464-1810 6.15e-65

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 228.38  E-value: 6.15e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGAS----- 1538
Cdd:PRK02382   53 LPGGIDVHVHFREPGYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTgnwdp 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1539 -----SENAGTLGAV--AGSAAGLKLYLnETFSEL-----RLDSVAQWmeHFE-------------------TWPAHLPi 1587
Cdd:PRK02382  133 leslwERGVFALGEIfmADSTGGMGIDE-ELFEEAlaeaaRLGVLATV--HAEdedlfdelakllkgdadadAWSAYRP- 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1588 vAHAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKaqglpVTCEVAPHHLFLNREDLERLGPgKGEVRPELGSR 1667
Cdd:PRK02382  209 -AAAEAAAVERALEVASETGARIHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGT-FGKMNPPLRSE 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1668 EDMEALWE--NMAVIDCFASDHAPHTLEEKCGPKPPPGFPG--LETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP 1743
Cdd:PRK02382  282 KRREALWErlNDGTIDVVASDHAPHTREEKDADIWDAPSGVpgVETMLPLLLAAVRKNRLPLERVRDVTAANPARIFGLD 361

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575501534 1744 LQ---EDTY----VEVDLEHEWTVPSHMPFSKARWTPFEGqkVKGTVRRVVL-RGEVAYIDGQVLVPPGYGQDVR 1810
Cdd:PRK02382  362 GKgriAEGYdadlVLVDPDAAREIRGDDLHSKAGWTPFEG--MEGVFPELTMvRGTVVWDGDDINAKRGRGEFLR 434
PRK07575 PRK07575
dihydroorotase; Provisional
 1442-1799 7.12e-65

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 228.02  E-value: 7.12e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1442 QIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPalALAQK 1521
Cdd:PRK07575   33 AIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRACAKGGVTSFLEMPNTKPLTTTQA--ALDDK 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1522 LAEAGARC--DFTLFLGASSENAGTLGAVAGsAAGLKLYLNETFSELRLDSVAQWMEHF-ETwpaHLPIVAHAERQSV-- 1596
Cdd:PRK07575  111 LARAAEKCvvNYGFFIGATPDNLPELLTANP-TCGIKIFMGSSHGPLLVDEEAALERIFaEG---TRLIAVHAEDQARir 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1597 ---------------------AAVLMVAQLT-------QRPVHICHVARKEEILLIKTAKaqGLPVTCEVAPHHLFLNRE 1648
Cdd:PRK07575  187 arraefagisdpadhsqiqdeEAALLATRLAlklskkyQRRLHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLNTD 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1649 DLERLGPgKGEVRPELGSREDMEALWENM--AVIDCFASDHAPHTLEEKCGP--KPPPGFPGLETMLPLLLTAVSEGRLS 1724
Cdd:PRK07575  265 AYERIGT-LAQMNPPLRSPEDNEALWQALrdGVIDFIATDHAPHTLEEKAQPypNSPSGMPGVETSLPLMLTAAMRGKCT 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1725 LDDLLQRLHHNPRRIFHLP---LQEDTY----VEVDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAYIDG 1797
Cdd:PRK07575  344 VAQVVRWMSTAVARAYGIPnkgRIAPGYdadlVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRG 423


                  ..
gi 575501534 1798 QV 1799
Cdd:PRK07575  424 QV 425
GATase pfam00117
Glutamine amidotransferase class-I;
181-355 3.82e-64

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 216.33  E-value: 3.82e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   181 LDCGL--KYNQIRCLCQLGAEVTVVPWDH---ELDSQKYDGLFLSNGPGDPASYPGVVSTLSRVLsePNPRPVFGICLGH 255
Cdd:pfam00117    3 IDNGDsfTYNLARALRELGVEVTVVPNDTpaeEILEENPDGIILSGGPGSPGAAGGAIEAIREAR--ELKIPILGICLGH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   256 QLLALAIGAKTYKM-RYGNRGHNQPC------LLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDSL 328
Cdd:pfam00117   81 QLLALAFGGKVVKAkKFGHHGKNSPVgddgcgLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKL 160

                          170       180
                   ....*....|....*....|....*..
gi 575501534   329 PFFSVQFHPEHRAGPSDMELLFDVFLE 355
Cdd:pfam00117  161 PIFGVQFHPESILTPHGPEILFNFFIK 187
PRK09060 PRK09060
dihydroorotase; Validated
 1429-1810 9.47e-63

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 222.10  E-value: 9.47e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1429 DIKCTKLFVEALGQIGPAPPLKVhVDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRP 1508
Cdd:PRK09060   24 DIGIRDGRIAAIGDLSGASAGEV-IDC---RGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAAVLGGVTAVFEMPNTNP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1509 PIIDAPALALAQKLAEAGARCDFTLFLGASSENAGTLGAV--AGSAAGLKLYLNETFSELRLD---SVAQWMEHfetwpA 1583
Cdd:PRK09060  100 LTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELerLPGCAGIKVFMGSSTGDLLVEddeGLRRILRN-----G 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1584 HLPIVAHAE-----------------------RQSVAAVLM------VAQLTQRPVHICHVARKEEILLIKTAKAQglpV 1634
Cdd:PRK09060  175 RRRAAFHSEdeyrlrerkglrvegdpsshpvwRDEEAALLAtrrlvrLARETGRRIHVLHVSTAEEIDFLADHKDV---A 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1635 TCEVAPHHLFLNREDL-ERLGpGKGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGP--KPPPGFPGLET 1709
Cdd:PRK09060  252 TVEVTPHHLTLAAPECyERLG-TLAQMNPPIRDARHRDGLWRGVRqgVVDVLGSDHAPHTLEEKAKPypASPSGMTGVQT 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1710 MLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP--------LQEDTYVeVDLEHEWTVPSHMPFSKARWTPFEGQKVKG 1781
Cdd:PRK09060  331 LVPIMLDHVNAGRLSLERFVDLTSAGPARIFGIAgkgriavgYDADFTI-VDLKRRETITNEWIASRCGWTPYDGKEVTG 409

                         410       420
                  ....*....|....*....|....*....
gi 575501534 1782 TVRRVVLRGEVAYIDGQVLVPPGyGQDVR 1810
Cdd:PRK09060  410 WPVGTIVRGQRVMWDGELVGPPT-GEPVR 437
PRK08192 PRK08192
aspartate carbamoyltransferase; Provisional
 1923-2162 9.81e-63

aspartate carbamoyltransferase; Provisional


Pssm-ID: 169269 [Multi-domain]  Cd Length: 338  Bit Score: 218.44  E-value: 9.81e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1923 GQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYE------------------------------- 1971
Cdd:PRK08192    5 GSHILSVNQLDRDAIQRIFNVADRMEPYALREKRTRVLEGAILGNLFFEpstrtrvsfgcafnllgghvrettgmasssl 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1972 -------------------LAAKH------------CRRPVINAGDGVGEHPTQALLDIFTIREEL----GTVNGMTITM 2016
Cdd:PRK08192   85 skgeslydtarvlstysdvIAMRHpdagsvkefaegSRVPVINGGDGSNEHPTQALLDLFTIQKELahagRGIDGMHIAM 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2017 VGDLKHGRTVHSLACLLTQY-RVSLRYVAPPSLRMPPSVRDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSVQ 2095
Cdd:PRK08192  165 VGDLKFGRTVHSLSRLLCMYkNVSFTLVSPKELAMPDYVISDIENAGHKITITDQLEGNLDKADILYLTRIQEERFPSQE 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575501534 2096 EYEACFGQFILTPHIMTR-AKKKMVVMHPMPR-----VNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2162
Cdd:PRK08192  245 EANKYRGKFRLNQSIYTQhCKSNTVIMHPLPRdsraqANELDNDLNSHPNLAIFRQADNGLLIRMALFALTLG 317
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 1461-1803 4.97e-59

L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.


Pssm-ID: 238640 [Multi-domain]  Cd Length: 447  Bit Score: 211.38  E-value: 4.97e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFTLFLGASS 1539
Cdd:cd01315    48 LVVMPGLIDTHVHINEPGRTEWEGFETGTKAAAAGGITTIIDMPlNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVP 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1540 ENAGTLGAVAGSAA-GLKLYLNET-FSELRLDSVAQWMEHFETWPAH-LPIVAHAE----------------RQSVAA-- 1598
Cdd:cd01315   128 GNLDQLRPLDEAGVvGFKCFLCPSgVDEFPAVDDEQLEEAMKELAKTgSVLAVHAEnpeitealqeqakakgKRDYRDyl 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1599 --------------VLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPgKGEVRPEL 1664
Cdd:cd01315   208 asrpvfteveaiqrILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGT-EFKCAPPI 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1665 GSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPGFP-----GLETMLPLLLT-AVSEGRLSLDDLLQRLHHNP 1736
Cdd:cd01315   287 RDAANQEQLWEALEngDIDMVVSDHSPCTPELKLLGKGDFFKAwggisGLQLGLPVMLTeAVNKRGLSLEDIARLMCENP 366

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575501534 1737 RRIFHLPLQEDT--------YVEVDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1803
Cdd:cd01315   367 AKLFGLSHQKGRiavgydadFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVGEP 441
PRK11891 PRK11891
aspartate carbamoyltransferase; Provisional
 1924-2162 4.21e-57

aspartate carbamoyltransferase; Provisional


Pssm-ID: 183362 [Multi-domain]  Cd Length: 429  Bit Score: 205.10  E-value: 4.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1924 QHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYE--------LAAKHCRR---------------- 1979
Cdd:PRK11891   88 PQLLSVDQFSRDSVEALFRVADVMQPIARRQKISRVLEGAVLGNLFFEastrtrvsFGAAFCRLggsvcdttgftfssma 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1980 --------------------------------------PVINAGDGVGEHPTQALLDIFTIREE---LG-TVNGMTITMV 2017
Cdd:PRK11891  168 kgesiydtsrvmsgyvdalvirhpeqgsvaefaratnlPVINGGDGPGEHPSQALLDLYTIQREfsrLGkIVDGAHIALV 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2018 GDLKHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPPSVRDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSvQE 2096
Cdd:PRK11891  248 GDLKYGRTVHSLVKLLALYRgLKFTLVSPPTLEMPAYIVEQISRNGHVIEQTDDLAAGLRGADVVYATRIQKERFAD-ES 326

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575501534 2097 YEACFGQFILTPHIMTRA-KKKMVVMHPMPR-----VNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2162
Cdd:PRK11891  327 FEGYTPDFQINQALVDAVcKPDTLIMHPLPRdsrpgANDLSTDLNRDPRLAIFRQTDNGIPVRMAIFAVLLG 398
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 799-921 1.68e-54

Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 198164 [Multi-domain]  Cd Length: 124  Bit Score: 186.12  E-value: 1.68e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534    799 DMELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHRGQALPQDLLHQAKCLGFSDKQIAL 878
Cdd:smart01096    2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 575501534    879 AVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTY 921
Cdd:smart01096   82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
PRK09236 PRK09236
dihydroorotase; Reviewed
 1464-1799 1.79e-53

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 195.09  E-value: 1.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENAG 1543
Cdd:PRK09236   53 LPGMIDDQVHFREPGLTHKGDIASESRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNLD 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1544 TLGAV-AGSAAGLKLY---------------LNETFSELRL---------DSVAQWMEHF-ETWPAHLPIVAHAERQSVA 1597
Cdd:PRK09236  133 EIKRLdPKRVCGVKVFmgastgnmlvdnpetLERIFRDAPTliathcedtPTIKANLAKYkEKYGDDIPAEMHPLIRSAE 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1598 AVLM-------VAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGpGKGEVRPELGSREDM 1670
Cdd:PRK09236  213 ACYKssslavsLAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLG-NLIKCNPAIKTASDR 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1671 EALWENMA--VIDCFASDHAPHTLEEKcgpkpppGFPGLETM---------LPLLLTAVSEGRLSLDDLLQRLHHNPRRI 1739
Cdd:PRK09236  292 EALRQALAddRIDVIATDHAPHTWEEK-------QGPYFQAPsglplvqhaLPALLELVHEGKLSLEKVVEKTSHAPAIL 364

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501534 1740 FHLP----LQEDTY---VEVDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAYIDGQV 1799
Cdd:PRK09236  365 FDIKergfIREGYWadlVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQL 431
PRK06189 PRK06189
allantoinase; Provisional
 1464-1811 3.63e-49

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 182.59  E-value: 3.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENA 1542
Cdd:PRK06189   53 FPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1543 GTLGAVA-GSAAGLKLYLNET-FSELRLDSVAQWMEHFETWPAHLPIVA-HAER-------------------------- 1593
Cdd:PRK06189  133 EHLRELAeAGVIGFKAFMSNSgTDEFRSSDDLTLYEGMKEIAALGKILAlHAESdaltrhlttqarqqgktdvrdylesr 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1594 ------QSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPgKGEVRPELGSR 1667
Cdd:PRK06189  213 pvvaelEAVQRALLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGA-VAKCAPPLRSR 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1668 EDMEALWENMAV--IDCFASDHAPHTLEEKCGPKPPPGFPGL---ETMLPLLLT-AVSEGRLSLDDLLQRLHHNPRRIFH 1741
Cdd:PRK06189  292 SQKEELWRGLLAgeIDMISSDHSPCPPELKEGDDFFLVWGGIsggQSTLLVMLTeGYIERGIPLETIARLLATNPAKRFG 371

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501534 1742 LPL-------QEDTYVEVDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAYIDGQVlVPPGYGQDVRK 1811
Cdd:PRK06189  372 LPQkgrlevgADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEV-FPPPRGQLLRP 447
allantoinase TIGR03178
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ...
 1461-1803 2.34e-46

allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.


Pssm-ID: 163175 [Multi-domain]  Cd Length: 443  Bit Score: 174.11  E-value: 2.34e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFTLFLGASS 1539
Cdd:TIGR03178   47 LVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAAGGITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVP 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1540 ENAGTLGAVAGSAA-GLKLYLN----ETFSELRLDSVAQWM---------------------EHFETWPAHLPIVAH--- 1590
Cdd:TIGR03178  127 YNLDDLRELDEAGVvGFKAFLSpsgdDEFPHVDDWQLYKGMrelarlgqlllvhaenpaitsALGEEAPPQGGVGADayl 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1591 ------AERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPgKGEVRPEL 1664
Cdd:TIGR03178  207 asrpvfAEVEAIRRTLALAKVTGCRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGT-LAKCAPPI 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1665 GSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPG---FPGLETMLPLLLTAVSEGR-LSLDDLLQRLHHNPRR 1738
Cdd:TIGR03178  286 RDLANQEGLWEALLngLIDCVVSDHSPCTPDLKRAGDFFKAwggIAGLQSTLDVMFDEAVQKRgLPLEDIARLMATNPAK 365

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575501534  1739 IFHL-------PLQEDTYVEVDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1803
Cdd:TIGR03178  366 RFGLaqkgriaPGKDADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFIGAP 437
PRK01211 PRK01211
dihydroorotase; Provisional
 1464-1811 2.78e-42

dihydroorotase; Provisional


Pssm-ID: 179247 [Multi-domain]  Cd Length: 409  Bit Score: 161.18  E-value: 2.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENAG 1543
Cdd:PRK01211   45 LPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNAL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1544 TLGAVagsAAGLKLYLNETFSELRLDSVAQWMEHFETwpAHLPIVAHAERQ------------------------SVAAV 1599
Cdd:PRK01211  125 ILDER---SIGLKVYMGGTTNTNGTDIEGGEIKKINE--ANIPVFFHAELSeclrkhqfesknlrdhdlarpiecEIKAV 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1600 LMVAQLTQRPVHICHVARKEEIlliktakaqgLPVTCEVAPHHLFLNREdlERLGpGKGEVRPELGSREDMEALWENM-- 1677
Cdd:PRK01211  200 KYVKNLDLKTKIIAHVSSIDVI----------GRFLREVTPHHLLLNDD--MPLG-SYGKVNPPLRDRWTQERLLEEYis 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1678 AVIDCFASDHAPHTLEEKCG-PKPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHL---PLQEDTYVE-- 1751
Cdd:PRK01211  267 GRFDILSSDHAPHTEEDKQEfEYAKSGIIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGIkkgKIEEGYDADfm 346

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501534 1752 -VDLEHEWTVPSHMPFSKARWTPFEGQKVKGTvRRVVLRGEVAyIDGQVLVPPGYGQDVRK 1811
Cdd:PRK01211  347 aFDFTNIKKINDKRLHSKCPVSPFNGFDAIFP-SHVIMRGEVV-IDNYELISERTGKFVPK 405
pyrC PRK00369
dihydroorotase; Provisional
 1464-1804 6.74e-42

dihydroorotase; Provisional


Pssm-ID: 234738 [Multi-domain]  Cd Length: 392  Bit Score: 159.54  E-value: 6.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPiIDAPAlALAQKLAE--AGARCDFTLFLGA--SS 1539
Cdd:PRK00369   46 LPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPP-LNTPE-AITEKLAEleYYSRVDYFVYSGVtkDP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1540 ENAGTLGavagsAAGLKLY---LNETFSELRLDSVAQW-MEHFEtwpahLPIVAHAER-------QSVAAVLMVAQLTQr 1608
Cdd:PRK00369  124 EKVDKLP-----IAGYKIFpedLEREETFRVLLKSRKLkILHPE-----VPLALKSNRklrrncwYEIAALYYVKDYQN- 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1609 pVHICHVARKEEILLiktAKAQGLpvTCEVAPHHLFLNREdlerlGPGKGEVRPELGSREDMEALWENMAVIDCFASDHA 1688
Cdd:PRK00369  193 -VHITHASNPRTVRL---AKELGF--TVDITPHHLLVNGE-----KDCLTKVNPPIRDINERLWLLQALSEVDAIASDHA 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1689 PHTLEEKCGPKPPPGF--PGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPlqeDTYVEVDLEHEWTVPS---- 1762
Cdd:PRK00369  262 PHSSFEKLQPYEVCPPgiAALSFTPPFIYTLVSKGILSIDRAVELISTNPARILGIP---YGEIKEGYRANFTVIQfedw 338

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 575501534 1763 --HMPFSKARWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPG 1804
Cdd:PRK00369  339 rySTKYSKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKG 382
MGS_CPS_I_III cd01423
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ...
 1313-1438 1.08e-41

Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.


Pssm-ID: 238711 [Multi-domain]  Cd Length: 116  Bit Score: 149.37  E-value: 1.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1313 KNILLTIGSYkNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGEcppqRSILDQLAENHFELV 1392
Cdd:cd01423     1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK----PSLRELLAEGKIDLV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 575501534 1393 INLSMRGAGGRRLSsfvtkGYRTRRLAADFSVPLIIDIKCTKLFVE 1438
Cdd:cd01423    76 INLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
PRK07369 PRK07369
dihydroorotase; Provisional
 1442-1783 8.68e-39

dihydroorotase; Provisional


Pssm-ID: 236002 [Multi-domain]  Cd Length: 418  Bit Score: 151.29  E-value: 8.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1442 QIGPAPPLKVHVDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQK 1521
Cdd:PRK07369   37 HIDPIPPDTQIIDA---SGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPPLDNPATLARLQQ 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1522 LAEAGARCDFtLFLGASSENA--------GTLGA--VAGSAAGLKLylnETFSELR--LDSVAQWMEHFETWPAHL---- 1585
Cdd:PRK07369  114 QAQQIPPVQL-HFWGALTLGGqgkqltelAELAAagVVGFTDGQPL---ENLALLRrlLEYLKPLGKPVALWPCDRslag 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1586 ----------------PIVAHAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNRED 1649
Cdd:PRK07369  190 ngvmregllalrlglpGDPASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEA 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1650 LERLGPgkgEVR--PELGSREDMEALWENM--AVIDCFASDHAPHTLEEKCGPKPPPGFPG--LETMLPLLL-TAVSEGR 1722
Cdd:PRK07369  270 LASYDP---NLRldPPLGNPSDRQALIEGVrtGVIDAIAIDHAPYTYEEKTVAFAEAPPGAigLELALPLLWqNLVETGE 346

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501534 1723 LSLDDLLQRLHHNPRRIFHLP---LQEDTYVEV---DLEHEWTVPSHMPFSKARWTPFEGQKVKGTV 1783
Cdd:PRK07369  347 LSALQLWQALSTNPARCLGQEppsLAPGQPAELilfDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRV 413
OTCace pfam00185
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;
2013-2160 1.29e-38

Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;


Pssm-ID: 425511 [Multi-domain]  Cd Length: 154  Bit Score: 141.98  E-value: 1.29e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  2013 TITMVGDlKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPSV----RDFVASRGTKQEEFESIEEALPDTDVLYMTRIQ- 2087
Cdd:pfam00185    1 KIAYVGD-GHNNVAHSLIIAAAKLGMDVRLATPKGYPPDPEVldkaKKIAEKSGGSIEITDDPAEAVKGADVVYTDVWQs 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575501534  2088 ----KERFgsvQEYEAcFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATV 2160
Cdd:pfam00185   80 mgqeKERE---ERLKA-FKPYQVNEELMKLAKKDAIFMHCLPahRGEEVTDDVFDGPRSVVFDQAENRLHAQKALLALL 154
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 1439-1806 1.84e-38

D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.


Pssm-ID: 238639 [Multi-domain]  Cd Length: 447  Bit Score: 151.22  E-value: 1.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1439 ALGQ-IGPAPPLKVhVDCmtSQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPA 1515
Cdd:cd01314    28 AIGPnLEAPGGVEV-IDA--TGKYV-LPGGIDPHTHLELPfmGTVTADDFESGTRAAAAGGTTTIIDFAIPNKGQSLLEA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1516 LALAQKLAEAGARCDFTLFLGASSENAGTLG----AVAGSAAGLKLY-------------LNETFSELRL---------- 1568
Cdd:cd01314   104 VEKWRGKADGKSVIDYGFHMIITDWTDSVIEelpeLVKKGISSFKVFmaykgllmvddeeLLDVLKRAKElgalvmvhae 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1569 --DSVAQWMEHFE----TWPahlpiVAHA-------ERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVT 1635
Cdd:cd01314   184 ngDVIAELQKKLLaqgkTGP-----EYHAlsrppevEAEATARAIRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVY 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1636 CEVAPHHLFLNREDLERLGP-GKGEV-RPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPG-----FPG 1706
Cdd:cd01314   259 GETCPQYLLLDDSDYWKDWFeGAKYVcSPPLRPKEDQEALWDGLSsgTLQTVGSDHCPFNFAQKARGKDDFTkipngVPG 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1707 LETMLPLLLTA-VSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVE--------VDLEHEWTVPSHMPFSKARWTPFEGQ 1777
Cdd:cd01314   339 VETRMPLLWSEgVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVgsdadlviWDPNAEKTISADTHHHNVDYNIFEGM 418

                         410       420
                  ....*....|....*....|....*....
gi 575501534 1778 KVKGTVRRVVLRGEVAYIDGQVLVPPGYG 1806
Cdd:cd01314   419 KVKGWPVVTISRGKVVVEDGELVGEKGSG 447
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
 1442-1811 5.76e-37

D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.


Pssm-ID: 273937 [Multi-domain]  Cd Length: 454  Bit Score: 146.76  E-value: 5.76e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1442 QIGP--APPLKVHV-DCmtSQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPAL 1516
Cdd:TIGR02033   28 AVGDnlIPPDAVEViDA--TGKYV-LPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAAGGTTTIIDFVVPEKGSSLTEAL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1517 ALAQKLAEAGARCDFTLFLGASSENAGTLG-----AVAGSAAGLKLY-------------LNETFSELRlDSVAQWMEHF 1578
Cdd:TIGR02033  105 ETWHEKAEGKSVIDYGFHMDITHWNDSVLEehipeVKEEGINSFKVFmayknllmvddeeLFEILKRLK-ELGALLQVHA 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1579 E-----------------TWPAHLPIV--AHAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVA 1639
Cdd:TIGR02033  184 EngdiiaelqarmlaqgiTGPEYHALSrpPELEAEAVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETC 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1640 PHHLFLNREDLERLG--PGKGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPGFPG------LET 1709
Cdd:TIGR02033  264 PQYLVLDDTHYDKPGfeGAKYVCSPPLREPEDQDALWSALSsgALQTVGSDHCTFNFAQKKAIGKDDFTKIpnggpgVEE 343

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1710 MLPLLLTA-VSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVE--------VDLEHEWTVPSHMPFSKARWTPFEGQKVK 1780
Cdd:TIGR02033  344 RMSLLFDEgVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVgsdadiviWDPNRTTVISAETHHSNADYNPFEGFKVR 423

                          410       420       430
                   ....*....|....*....|....*....|.
gi 575501534  1781 GTVRRVVLRGEVAYIDGQVLVPPGYGQDVRK 1811
Cdd:TIGR02033  424 GAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
PRK08323 PRK08323
phenylhydantoinase; Validated
 1460-1810 4.65e-35

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 141.08  E-value: 4.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1460 KLVrLPGLIDVHVHLREP-GGTH-KEDFASGTAAALAGGVTMVC--AMPNTRPPIIDApaLALAQKLAEAGARCD--FTL 1533
Cdd:PRK08323   45 KYV-MPGGIDPHTHMEMPfGGTVsSDDFETGTRAAACGGTTTIIdfALQPKGQSLREA--LEAWHGKAAGKAVIDygFHM 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1534 FLGASSENAGT-LGAVAgsAAG---LKLYLN-------------ETFSELRL------------DSVAQWMEHFE----T 1580
Cdd:PRK08323  122 IITDWNEVVLDeMPELV--EEGitsFKLFMAykgalmldddellRALQRAAElgalpmvhaengDAIAYLQAKLLaegkT 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1581 WPAHLPIV--AHAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPGKG 1658
Cdd:PRK08323  200 GPEYHALSrpPEVEGEATNRAIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEG 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1659 EVR---PELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPP------GFPGLETMLPLLLTA-VSEGRLSLD 1726
Cdd:PRK08323  280 AKYvmsPPLRDKEHQDALWRGLQdgDLQVVATDHCPFCFEQKKQLGRGDftkipnGTPGVEDRMPLLFSEgVMTGRITLN 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1727 DLLQRLHHNPRRIFHLPLQEDTyVEV---------DLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAYIDG 1797
Cdd:PRK08323  360 RFVELTSTNPAKIFGLYPRKGT-IAVgadadiviwDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDG 438

                         410
                  ....*....|...
gi 575501534 1798 QVLVPPGYGQDVR 1810
Cdd:PRK08323  439 EFRGKAGHGRFLK 451
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
 801-877 5.51e-32

Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 460695  Cd Length: 79  Bit Score: 120.17  E-value: 5.51e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501534   801 ELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHrGQALPQDLLHQAKCLGFSDKQIA 877
Cdd:pfam02787    2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEA-GLDLDAELLREAKRLGFSDRQIA 77
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 1460-1811 6.17e-32

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 132.13  E-value: 6.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1460 KLVrLPGLIDVHVHLREPGGT---HKEDFASGTAAALAGGVTMVC--AMPNTRPPIIDApaLALAQKLAEAGARCDFTLF 1534
Cdd:PRK13404   50 RLV-LPGGVDSHCHIDQPSGDgimMADDFYTGTVSAAFGGTTTVIpfAAQHRGQSLREA--VEDYHRRAAGKAVIDYAFH 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1535 LGASSENAGTLG-----AVAGSAAGLKLYLneTFSELRLD--------SVAQ-----------------WM-----EHFE 1579
Cdd:PRK13404  127 LIVADPTEEVLTeelpaLIAQGYTSFKVFM--TYDDLKLDdrqildvlAVARrhgamvmvhaenhdmiaWLtkrllAAGL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1580 TWPAH----LPIVAhaERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERlgP 1655
Cdd:PRK13404  205 TAPKYhaisRPMLA--EREATHRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDR--P 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1656 G----KGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPGFPG----------LETMLPLLLTA-V 1718
Cdd:PRK13404  281 GmegaKYICSPPPRDKANQEAIWNGLAdgTFEVFSSDHAPFRFDDTDGKLAAGANPSfkaiangipgIETRLPLLFSEgV 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1719 SEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYV---EVDL-----EHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRG 1790
Cdd:PRK13404  361 VKGRISLNRFVALTSTNPAKLYGLYPRKGAIAigaDADIaiwdpDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRG 440

                         410       420
                  ....*....|....*....|.
gi 575501534 1791 EVAYIDGQVLVPPGYGQDVRK 1811
Cdd:PRK13404  441 RVVVEDGELVAERGSGQFLAR 461
ArgF COG0078
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine ...
 1920-2163 1.89e-30

Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine carbamoyltransferase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439848 [Multi-domain]  Cd Length: 310  Bit Score: 123.62  E-value: 1.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1920 SLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFY----------ELA---------------- 1973
Cdd:COG0078     2 NLKGRHFLSLLDLTPEELRALLDLAAELKAKRKAGIPHRPLKGKTLAMIFEkpstrtrvsfEVGmaqlgghaiyldpgds 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1974 -----------------------------------AKHCRRPVINA-GDGvgEHPTQALLDIFTIREELGTVNGMTITMV 2017
Cdd:COG0078    82 qlgrgesikdtarvlsryvdgimirtfghetleelAKYAGVPVINGlTDL--FHPCQALADLLTIREHFGKLKGLKVAYV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2018 GDlkhGRTV-HSLACLLTQYRVSLRYVAPPSLRMPPSV----RDFVASRGTKQEEFESIEEALPDTDVLY------MTri 2086
Cdd:COG0078   160 GD---GNNVaNSLLLAAAKLGMDVRIATPEGYEPDPEIvakaKEIAAESGGSITITHDPAEAVKGADVVYtdvwvsMG-- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2087 QKErfgSVQEYEACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEV-DSdPRAAYFRQAENGMYIRMALLATVLGR 2163
Cdd:COG0078   235 QEE---EAEERIKAFKPYQVNEELMALAKPDAIFMHCLPahRGEEVTDEViDG-PQSVVFDEAENRLHAQKALLAWLLGG 310
PRK07627 PRK07627
dihydroorotase; Provisional
 1443-1794 1.11e-29

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 124.40  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1443 IGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIiDAPALA----- 1517
Cdd:PRK07627   33 IGQAPAGFNADKTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAAVAGGVTSLVCPPDTDPVL-DEPGLVemlkf 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1518 LAQKLAEA-----GArcdFTLFLGAS--SENAGTL--GAVAGSAAGLKLYLNETFseLRLDSVAQ------WMEHFETWP 1582
Cdd:PRK07627  112 RARNLNQAhvyplGA---LTVGLKGEvlTEMVELTeaGCVGFSQANVPVVDTQVL--LRALQYAStfgftvWLRPLDAFL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1583 AHLPiVAH----------------AERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLN 1646
Cdd:PRK07627  187 GRGG-VAAsgavasrlglsgvpvaAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLI 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1647 REDLERLGPgKGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCG--PKPPPGFPGLETMLPLLLTAVSEGR 1722
Cdd:PRK07627  266 DVDIGYFDS-QFRLDPPLRSQRDREAIRAALAdgTIDAICSDHTPVDDDEKLLpfAEATPGATGLELLLPLTLKWADEAK 344

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575501534 1723 LSLDDLLQRLHHNPRRIFHLP---LQEDTYVEV---DLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAY 1794
Cdd:PRK07627  345 VPLARALARITSAPARVLGLPagrLAEGAPADLcvfDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAF 422
PRK09059 PRK09059
dihydroorotase; Validated
 1453-1794 4.09e-29

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 122.84  E-value: 4.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1453 VDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPpIIDAPAL---------------- 1516
Cdd:PRK09059   51 VDC---AGKAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMPDTDP-VIDDVALvefvkrtardtaivni 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1517 ----ALAQKLA-----------EAGARCdFTLflGASS-ENAGTLGAVAGSAAGLK-LYLNETFSElrlDSVAQWMEH-- 1577
Cdd:PRK09059  127 hpaaAITKGLAgeemtefgllrAAGAVA-FTD--GRRSvANTQVMRRALTYARDFDaVIVHETRDP---DLGGNGVMNeg 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1578 -FETWPAHLPIVAHAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLerlgpg 1656
Cdd:PRK09059  201 lFASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVSINHLSLNENDI------ 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1657 kGEVR------PELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCG--PKPPPGFPGLETMLPLLLTAVSEGRLSLD 1726
Cdd:PRK09059  275 -GEYRtffklsPPLRTEDDRVAMVEAVAsgTIDIIVSSHDPQDVDTKRLpfSEAAAGAIGLETLLAAALRLYHNGEVPLL 353

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575501534 1727 DLLQRLHHNPRRIFHLP---LQEDTYVE---VDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAY 1794
Cdd:PRK09059  354 RLIEALSTRPAEIFGLPagtLKPGAPADiivIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVY 427
PLN02795 PLN02795
allantoinase
 1462-1797 5.63e-28

allantoinase


Pssm-ID: 178392 [Multi-domain]  Cd Length: 505  Bit Score: 120.65  E-value: 5.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1462 VRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSE 1540
Cdd:PLN02795   96 VVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPE 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1541 NAGTLGA----VAGSAAGLKLYL-NETFSELRLDSVAQWMEHFETWPAH-LPIVAHAERQS------------------- 1595
Cdd:PLN02795  176 NAHNASVleelLDAGALGLKSFMcPSGINDFPMTTATHIKAALPVLAKYgRPLLVHAEVVSpvesdsrldadprsystyl 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1596 -----------VAAVLMVAQLTQR-------PVHICHVARKEEIL-LIKTAKAQGLPVTCEVAPHHLFLNREDLerlgpG 1656
Cdd:PLN02795  256 ksrppsweqeaIRQLLEVAKDTRPggvaegaHVHIVHLSDAESSLeLIKEAKAKGDSVTVETCPHYLAFSAEEI-----P 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1657 KGEVR----PELGSREDMEALWENMA--VIDCFASDHAPHT-----LEEKCGPKPPPGFPGLETMLPLLLTAVSEGRLSL 1725
Cdd:PLN02795  331 DGDTRykcaPPIRDAANRELLWKALLdgDIDMLSSDHSPSPpdlklLEEGNFLRAWGGISSLQFVLPATWTAGRAYGLTL 410

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1726 DDLLQRLHHNPRRIFHLPL--------QEDtYVEVDLEHEWTVPSHMP--FSKARWTPFEGQKVKGTVRRVVLRGEVAYI 1795
Cdd:PLN02795  411 EQLARWWSERPAKLAGLDSkgaiapgkDAD-IVVWDPEAEFVLDESYPiyHKHKSLSPYLGTKLSGKVIATFVRGNLVFL 489


                  ..
gi 575501534 1796 DG 1797
Cdd:PLN02795  490 EG 491
pyrB PRK13814
aspartate carbamoyltransferase;
1981-2163 7.29e-27

aspartate carbamoyltransferase;


Pssm-ID: 139876 [Multi-domain]  Cd Length: 310  Bit Score: 113.27  E-value: 7.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1981 VINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLA-CLLTQYRVSLRYVAPPSLrMPpsvrDFVA 2059
Cdd:PRK13814  127 VINAGDGNHQHPSQALIDLMTIKQHKPHWNKLCVTIIGDIRHSRVANSLMdGLVTMGVPEIRLVGPSSL-LP----DKVG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2060 SRGTKQeeFESIEEALPDTDVLYMTRIQKERFGSVQEYEACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSD 2137
Cdd:PRK13814  202 NDSIKK--FTELKPSLLNSDVIVTLRLQKERHDNSVDIDAFRGSFRLTPEKLYSAKPDAIVMHPGPvnREVEINSDVADN 279

                         170       180
                  ....*....|....*....|....*.
gi 575501534 2138 PRAAYFRQAENGMYIRMALLATVLGR 2163
Cdd:PRK13814  280 QQSVILQQVRNGVAMRMAVLELFLLR 305
pyrB PRK13376
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase ...
 1971-2162 1.04e-26

bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase regulatory subunit; Provisional


Pssm-ID: 237369 [Multi-domain]  Cd Length: 525  Bit Score: 117.17  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1971 ELAAKH-CRRPV-INAGDGVGEHPTQALLDIFTIREELGTVNG-MTITMVGDLKHGRTVHSLACLLTQYR-VSLRYVAPP 2046
Cdd:PRK13376  131 EFASRNgIEVPAfINAGDGKHEHPTQELLDEFTFLEQNNFDNSfIHIALVGDLLHGRTVHSKVNGLKIFKnVKVDLIAPE 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2047 SLRMPPSVRDFVASRGTKQEEFESIEEALPDTDVL---YMTRIQKERFGSvqeyeacfgQFILTPHIMTRA---KKKMV- 2119
Cdd:PRK13376  211 ELAMPEHYVEKMKKNGFEVRIFSSIEEYLSQKDVAkiwYFTRLQLERMGE---------DILEKEHILRKAvtfRKEFLd 281

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 575501534 2120 -------VMHPMPRVN---EISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2162
Cdd:PRK13376  282 klpegvkFYHPLPRHKvypTIPTFLDTLPLNGWETQAINGYWVRIVLLSMLGG 334
PRK08044 PRK08044
allantoinase AllB;
1454-1794 2.64e-26

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 114.95  E-value: 2.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1454 DCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFT 1532
Cdd:PRK08044   42 EVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1533 LFLGASSENAGTLGAV-AGSAAGLKLYLnETFSELRLDS----VAQW----------------MEHFETWP--------- 1582
Cdd:PRK08044  122 QLGGLVSYNLDRLHELdEVGVVGFKCFV-ATCGDRGIDNdfrdVNDWqfykgaqklgelgqpvLVHCENALicdelgeea 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1583 -AHLPIVAHA---------ERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLER 1652
Cdd:PRK08044  201 kREGRVTAHDyvasrpvftEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEE 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1653 LGPgKGEVRPELGSREDMEALWENM--AVIDCFASDHAPHTLEEKCGPKPPP--GFPGLETMLPLLL-TAVSEGRLSLDD 1727
Cdd:PRK08044  281 IGT-LAKCSPPIRDLENQKGMWEKLfnGEIDCLVSDHSPCPPEMKAGNIMEAwgGIAGLQNCMDVMFdEAVQKRGMSLPM 359

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575501534 1728 LLQRLHHNPRRIFHL-------PLQEDTYVEVDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAY 1794
Cdd:PRK08044  360 FGKLMATNAADIFGLqqkgriaPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIY 433
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 187-338 3.02e-26

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 107.62  E-value: 3.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  187 YNQIRCLCQLGAEVTVVPWDH----ELDSQKYDGLFLSNGPGDPASYPGVVSTLSRVLSEpnpRPVFGICLGHQLLALAI 262
Cdd:cd01743    12 YNLVQYLRELGAEVVVVRNDEitleELELLNPDAIVISPGPGHPEDAGISLEIIRALAGK---VPILGVCLGHQAIAEAF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  263 GAKTYKMRYGNRG------HNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWapLFTNANDcsnEGIV----HDSLPFFS 332
Cdd:cd01743    89 GGKVVRAPEPMHGktseihHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLL--EVTASTE---DGVImalrHRDLPIYG 163


                  ....*.
gi 575501534  333 VQFHPE 338
Cdd:cd01743   164 VQFHPE 169
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 1029-1247 2.09e-23

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 101.87  E-value: 2.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1029 RQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVAYTDGDLE 1108
Cdd:COG0439    36 AEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1109 RFL----SSAAAVSKEHPVVISKFIqEAKEIDVDAVACDGIVSAIAISEHvENAGVHSGDATLVTPPqDITPKTLERIKA 1184
Cdd:COG0439   116 AALaearAEAKAGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGE 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501534 1185 IVHAVGQELQV-TGPFNLQ-LIAKDDQLKVIECNVRVS--RSFPFVSKTLGVDLVALATRIIMGEKV 1247
Cdd:COG0439   193 LVARALRALGYrRGAFHTEfLLTPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEPR 259
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 1048-1248 2.46e-22

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 97.38  E-value: 2.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1048 RFKFSRLLDTIGISQPQW--RELSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKE----H 1121
Cdd:pfam02786    2 KVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgnP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1122 PVVISKFIQEAKEIDVDAVAcDGIVSAIAISEhVENA-GVHSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFN 1200
Cdd:pfam02786   82 QVLVEKSLKGPKHIEYQVLR-DAHGNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 575501534  1201 LQLI--AKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVE 1248
Cdd:pfam02786  160 VEFAldPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 457-714 1.40e-21

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 96.48  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  457 LHYVTQVIRNERPDGVLltfggqtALNCGVELTKAGVLARYGVRvlGTPVETIELTEDRRAFAARMAEIGEHVAPSEAAN 536
Cdd:COG0439     6 IAAAAELARETGIDAVL-------SESEFAVETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  537 SLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELSALV------APAFAHTSQVLIDKSLKGwKEIEYE-VVRDay 609
Cdd:COG0439    77 SPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALaearaeAKAGSPNGEVLVEEFLEG-REYSVEgLVRD-- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  610 GNCVtVCNM---ENLDPLGIHTGEsivVAPSQtLNDREYQLLRRTAIKVTQHLGIV-GECNVQYALNPESEqYYIIEVNA 685
Cdd:COG0439   154 GEVV-VCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGE-PYLIEINA 227

                         250       260       270
                  ....*....|....*....|....*....|.
gi 575501534  686 RLS--RSSALASKATGYPLAYVAAKLALGIP 714
Cdd:COG0439   228 RLGgeHIPPLTELATGVDLVREQIRLALGEP 258
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 1467-1739 8.06e-21

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 94.71  E-value: 8.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1467 LIDVHVHLREPGGTH------------------KEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGAR 1528
Cdd:cd01292     1 FIDTHVHLDGSALRGtrlnlelkeaeelspedlYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1529 CDFTLFLGASSENAGTLG------------AVAGSAAGLKLYLNETFSELrldSVAQWMEHFETWPAH-LPIVAHAERQS 1595
Cdd:cd01292    81 IRVVLGLGIPGVPAAVDEdaealllellrrGLELGAVGLKLAGPYTATGL---SDESLRRVLEEARKLgLPVVIHAGELP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1596 VA--AVLMVAQLTQRP--VHICHVARKEEILLIKTAKAQglpVTCEVAPHHLFLNREDlerlgpgkgevrpelgsREDME 1671
Cdd:cd01292   158 DPtrALEDLVALLRLGgrVVIGHVSHLDPELLELLKEAG---VSLEVCPLSNYLLGRD-----------------GEGAE 217

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575501534 1672 ALWENMA--VIDCFASDHAPHTLEekcgpkpppgfpglETMLPLLLTAVSEGRL--SLDDLLQRLHHNPRRI 1739
Cdd:cd01292   218 ALRRLLElgIRVTLGTDGPPHPLG--------------TDLLALLRLLLKVLRLglSLEEALRLATINPARA 275
PRK00779 PRK00779
ornithine carbamoyltransferase; Provisional
 1974-2161 3.04e-20

ornithine carbamoyltransferase; Provisional


Pssm-ID: 234835 [Multi-domain]  Cd Length: 304  Bit Score: 93.62  E-value: 3.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1974 AKHCRRPVINA-GDGvgEHPTQALLDIFTIREELGTVNGMTITMVGDlkhGRTV-HSLACLLTQYRVSLRYVAPPSLRMP 2051
Cdd:PRK00779  116 AEYSTVPVINGlTDL--SHPCQILADLLTIYEHRGSLKGLKVAWVGD---GNNVaNSLLLAAALLGFDLRVATPKGYEPD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2052 PSVRDFVA-SRGTKQEEFESIEEALPDTDVLY------MtriqkerfGsvQEYEA-----CFGQFILTPHIMTRAKKKMV 2119
Cdd:PRK00779  191 PEIVEKIAkETGASIEVTHDPKEAVKGADVVYtdvwvsM--------G--QEAEAeerlkAFAPYQVNEELMALAKPDAI 260

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 575501534 2120 VMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVL 2161
Cdd:PRK00779  261 FMHCLPahRGEEVTDEVIDGPQSVVWDEAENRLHAQKALLAWLL 304
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 1327-1427 1.12e-19

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 460462 [Multi-domain]  Cd Length: 93  Bit Score: 85.62  E-value: 1.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1327 ELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEA-VDGECppqrSILDQLAENHFELVINLSMRGAGGRRl 1405
Cdd:pfam02142    1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEGrPGGRV----QIGDLIKNGEIDLVINTLYPFKATVH- 75

                           90       100
                   ....*....|....*....|..
gi 575501534  1406 ssfvtKGYRTRRLAADFSVPLI 1427
Cdd:pfam02142   76 -----DGYAIRRAAENIDIPGP 92
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 177-361 3.73e-19

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 88.46  E-value: 3.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  177 RICALDCGLKYNQI-----RCLCQLGAEVTVV--------PWDHELDSqkYDGLFLSNGPG---DPASYPGVVSTLSRVL 240
Cdd:COG0518     1 KILILDHDPFGGQYpgliaRRLREAGIELDVLrvyageilPYDPDLED--PDGLILSGGPMsvyDEDPWLEDEPALIREA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  241 SEPNpRPVFGICLGHQLLALAIGAKTYKMRYGNRG------HNQPCLLVGTGRCFLTSQNHGFAVDAdsLPAGWAPLFTN 314
Cdd:COG0518    79 FELG-KPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelTEADPLFAGLPDEFTVWMSHGDTVTE--LPEGAEVLASS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 575501534  315 ANdCSNEGIVHDSlPFFSVQFHPEhrAGPSDMELLFDVFLETVREAA 361
Cdd:COG0518   156 DN-CPNQAFRYGR-RVYGVQFHPE--VTHTMMEAWLEERADELAAEE 198
OTCace_N pfam02729
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
1925-2004 3.89e-19

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;


Pssm-ID: 460665 [Multi-domain]  Cd Length: 140  Bit Score: 85.56  E-value: 3.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1925 HILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFY----------ELA--------------------- 1973
Cdd:pfam02729    1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKLPLLKGKTVALLFEepstrtrvsfEVAakrlgghviylsssdiqlssg 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501534  1974 ------------------------------AKHCRRPVINAGdGVGEHPTQALLDIFTIRE 2004
Cdd:pfam02729   81 esladtarvlsryvdaivirhfghedleelAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 187-338 4.26e-18

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 84.32  E-value: 4.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  187 YNQIRCLCQLGAEVTVVPWDH----ELDSQKYDGLFLSNGPGDPASyPGVvstLSRVLSEPNPR-PVFGICLGHQLLALA 261
Cdd:COG0512    12 YNLVQYLGELGAEVVVVRNDEitleEIEALAPDGIVLSPGPGTPEE-AGI---SLEVIRAFAGKiPILGVCLGHQAIGEA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  262 IGAKTYKMRY------------GN---RGHNQPcLLVgtGRcfltsqNHGFAVDADSLPagwAPLFTNANDCSNE--GIV 324
Cdd:COG0512    88 FGGKVVRAPEpmhgktspithdGSglfAGLPNP-FTA--TR------YHSLVVDRETLP---DELEVTAWTEDGEimGIR 155

                         170
                  ....*....|....
gi 575501534  325 HDSLPFFSVQFHPE 338
Cdd:COG0512   156 HRELPIEGVQFHPE 169
PLN02342 PLN02342
ornithine carbamoyltransferase
 1923-2162 6.45e-16

ornithine carbamoyltransferase


Pssm-ID: 177976 [Multi-domain]  Cd Length: 348  Bit Score: 81.76  E-value: 6.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1923 GQHILSVKQFTKDQMSHLFNVAHTLRMMVQK-ERSLDILKGKVMA------SM---------FYELA------------- 1973
Cdd:PLN02342   45 PKHFLHIDDFDKEEILGLLDRAKEVKALLKSgDRSFQPFKGKSMAmiftkpSMrtrvsfetgFFLLGghalylgpddiql 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1974 ---------------------------------AKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGDl 2020
Cdd:PLN02342  125 gkreetrdiarvlsryndiimarvfahqdvldlAEYSSVPVINGLTDY-NHPCQIMADALTIIEHIGRLEGTKVVYVGD- 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2021 kHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPSVRDfvasrGTKQEEFESIE------EALPDTDVLY------MTriQK 2088
Cdd:PLN02342  203 -GNNIVHSWLLLAAVLPFHFVCACPKGYEPDAKTVE-----KARAAGISKIEitndpaEAVKGADVVYtdvwasMG--QK 274

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575501534 2089 ErfgsvqEYE---ACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2162
Cdd:PLN02342  275 E------EAEkrkKAFQGFQVNEALMKLAGPQAYFMHCLPaeRGVEVTDGVMEAPNSIVFPQAENRMHAQNAIMLHQLG 347
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 1026-1249 2.73e-15

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 79.54  E-value: 2.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1026 ALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHT--VGYPCVVRPSYVLSGAAMNVAYT 1103
Cdd:PRK12767   90 RFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKgeLQFPLFVKPRDGSASIGVFKVND 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1104 DGDLERFLSSAAavskehPVVISKFIQEaKEIDVDA-VACDGIVSAIAISEHVEnagVHSGDATlvtppQDITPKTLERI 1182
Cdd:PRK12767  170 KEELEFLLEYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGETS-----KGVTVKDPELF 234

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501534 1183 KAIVHaVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFvSKTLGVDLVALATRIIMGEKVEP 1249
Cdd:PRK12767  235 KLAER-LAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL-SYMAGANEPDWIIRNLLGGENEP 299
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 178-349 3.57e-15

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 75.81  E-value: 3.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   178 ICALDCGLKYNQI--RCLCQLGAEVTVVPWD---HELDSQKYDGLFLSNGP-----GDPASYPGVVSTLSRvlsepnprP 247
Cdd:TIGR00888    1 ILVLDFGSQYTQLiaRRLRELGVYSELVPNTtplEEIREKNPKGIILSGGPssvyaENAPRADEKIFELGV--------P 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   248 VFGICLGHQLLALAIG---AKTYKMRYGN---RGHNQPCLLVGTGRCFLTSQNHGFAVDAdsLPAGWAPLFTNANdCSNE 321
Cdd:TIGR00888   73 VLGICYGMQLMAKQLGgevGRAEKREYGKaelEILDEDDLFRGLPDESTVWMSHGDKVKE--LPEGFKVLATSDN-CPVA 149

                          170       180
                   ....*....|....*....|....*...
gi 575501534   322 GIVHDSLPFFSVQFHPEHRAGPSDMELL 349
Cdd:TIGR00888  150 AMAHEEKPIYGVQFHPEVTHTEYGNELL 177
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 190-340 4.32e-15

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 75.74  E-value: 4.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  190 IRCLCQLGAEVTVVPW---DHELDSQKYDGLFLSNGPGDP--ASYPGVVST---LSRVLSEPnpRPVFGICLGHQLLALA 261
Cdd:cd01741    20 LREAGAETIEIDVVDVyagELLPDLDDYDGLVILGGPMSVdeDDYPWLKKLkelIRQALAAG--KPVLGICLGHQLLARA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  262 IGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDA--------DSLPAGWAPLFTNAnDCSNEGIVHDSLpFFSV 333
Cdd:cd01741    98 LGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPVfhwhgdtvVELPPGAVLLASSE-ACPNQAFRYGDR-ALGL 175


                  ....*..
gi 575501534  334 QFHPEHR 340
Cdd:cd01741   176 QFHPEER 182
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 395-717 7.04e-15

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 78.00  E-value: 7.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  395 KVLILGSGGlsigqagefdysGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLP-IT-LHYVTQVI---RNERP 469
Cdd:PRK12767    3 NILVTSAGR------------RVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPkVTdPNYIDRLLdicKKEKI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  470 DGVLLTFGgqtalncgVELtkaGVLARY-------GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQ 542
Cdd:PRK12767   71 DLLIPLID--------PEL---PLLAQNrdrfeeiGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFK 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  543 AA--AERLGYPVLVRAAFALGGLGSGFASTKEELSalvaPAFAHTSQVLIDKSLKGwKEIEYEVVRDAYGNCVTVCNMEN 620
Cdd:PRK12767  140 AAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKR 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  621 LDPLGIHTGESIVVapsqtlndrEYQLLRRTAIKVTQHLGIVGECNVQYALNPesEQYYIIEVNARLSrssalaskaTGY 700
Cdd:PRK12767  215 IEVRAGETSKGVTV---------KDPELFKLAERLAEALGARGPLNIQCFVTD--GEPYLFEINPRFG---------GGY 274

                         330       340
                  ....*....|....*....|....*.
gi 575501534  701 PLAYVA---------AKLALGIPLPE 717
Cdd:PRK12767  275 PLSYMAganepdwiiRNLLGGENEPI 300
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
391-724 2.00e-14

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 77.66  E-value: 2.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  391 PPPRKVLILGS--GGLSIgqagefdysgsqaIKALKEENIQTLLInpniATVQTSQGL----ADKVYFLP-------ITL 457
Cdd:COG3919     3 TMRFRVVVLGGdiNALAV-------------ARSLGEAGVRVIVV----DRDPLGPAArsryVDEVVVVPdpgddpeAFV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  458 HYVTQVIRNERPDgVLLTFGGQTALncgveltkagVLARY------GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP 531
Cdd:COG3919    66 DALLELAERHGPD-VLIPTGDEYVE----------LLSRHrdeleeHYRLPYPDADLLDRLLDKERFYELAEELGVPVPK 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  532 SEAANSLEQAQAAAERLGYPVLVRAA--------FALGGLGSGFASTKEELSALVAPAFAHTSQVLIDKSLKGWKEIEY- 602
Cdd:COG3919   135 TVVLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAGYELIVQEYIPGDDGEMRg 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  603 -EVVRDAYGNCVTVCNMENL--DPLGIhtGESIVVapsQTLNDREyqlLRRTAIKVTQHLGIVGECNVQYALNPESEQYY 679
Cdd:COG3919   215 lTAYVDRDGEVVATFTGRKLrhYPPAG--GNSAAR---ESVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYK 286

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 575501534  680 IIEVNARLSRSSALASKAtGYPLAYVAAKLALGIPLPELRNSVTG 724
Cdd:COG3919   287 LIEINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREG 330
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
493-717 2.86e-14

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 77.48  E-value: 2.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  493 VLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFAST 570
Cdd:PRK08462   96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDGAlKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  571 KEEL--SALVAPAFAHTS----QVLIDKSLKGWKEIEYEVVRDAYGNCVTV----CNMENldplgiHTGESIVVAPSQTL 640
Cdd:PRK08462  176 ESDLenLYLAAESEALSAfgdgTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVL 249

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501534  641 NDREYQLLRRTAIKVTQHLGIVGECNVQYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPE 717
Cdd:PRK08462  250 DEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPS 325
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 187-338 5.25e-14

glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.


Pssm-ID: 273144 [Multi-domain]  Cd Length: 188  Bit Score: 72.51  E-value: 5.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   187 YNQIRCLCQLGAEVtVVPWDHELDSQKYDGLF-----LSNGPGDPASypGVVStlSRVLSEPNPR-PVFGICLGHQLLAL 260
Cdd:TIGR00566   13 YNLVQYFCELGAEV-VVKRNDSLTLQEIEALLpllivISPGPCTPNE--AGIS--LEAIRHFAGKlPILGVCLGHQAMGQ 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   261 AIGAKTYKMRYGNRG------HNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDSLPFFSVQ 334
Cdd:TIGR00566   88 AFGGDVVRANTVMHGktseieHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQ 167


                   ....
gi 575501534   335 FHPE 338
Cdd:TIGR00566  168 FHPE 171
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 498-716 2.30e-13

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 74.68  E-value: 2.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  498 GVRVLGTPVETIELTEDRraFAAR--MAEIGEHVAP--SEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEE 573
Cdd:PRK06111   99 GIVFIGPSADIIAKMGSK--IEARraMQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQE 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  574 LSAlvapAFAHTSQ----------VLIDKSLKGWKEIEYEVVRDAYGNCVtvcnmenldplgiHTGE---SI------VV 634
Cdd:PRK06111  177 LTK----AFESNKKraanffgngeMYIEKYIEDPRHIEIQLLADTHGNTV-------------YLWErecSVqrrhqkVI 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  635 --APSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYaLNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALG 712
Cdd:PRK06111  240 eeAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEF-LVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAG 318


                  ....
gi 575501534  713 IPLP 716
Cdd:PRK06111  319 EKLS 322
PRK13566 PRK13566
anthranilate synthase component I;
195-338 2.61e-13

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 75.72  E-value: 2.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  195 QLGAEVTVVPWDH---ELDSQKYDGLFLSNGPGDPASYpGVVSTLSRVLSepnpR--PVFGICLGHQLLALAIGAKTYKM 269
Cdd:PRK13566  548 QTGAEVTTVRYGFaeeMLDRVNPDLVVLSPGPGRPSDF-DCKATIDAALA----RnlPIFGVCLGLQAIVEAFGGELGQL 622

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  270 RYGNRG------HNQPC-LLVGTGRCFLTSQNHGFAVDADSLPAGwapLFTNANdcSNEGIV----HDSLPFFSVQFHPE 338
Cdd:PRK13566  623 AYPMHGkpsrirVRGPGrLFSGLPEEFTVGRYHSLFADPETLPDE---LLVTAE--TEDGVImaieHKTLPVAAVQFHPE 697
MGS smart00851
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 1327-1427 2.64e-13

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 214855 [Multi-domain]  Cd Length: 91  Bit Score: 67.50  E-value: 2.64e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   1327 ELLPTVRLLESLGYSLYASLGTADFYTEHGVKV--TAVDWHFEEavdgecppQRSILDQLAENHFELVINLSMRGAggrr 1404
Cdd:smart00851    1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVvkTLHPKVHGG--------IPQILDLIKNGEIDLVINTLYPFE---- 68

                            90       100
                    ....*....|....*....|...
gi 575501534   1405 lSSFVTKGYRTRRLAADFSVPLI 1427
Cdd:smart00851   69 -AQAHEDGYSIRRAAENIDIPGP 90
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
491-716 2.78e-13

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 74.75  E-value: 2.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  491 AGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAAN--SLEQAQAAAERLGYPVLVRAAFALGGLGSGFA 568
Cdd:PRK07178   91 AEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNlaDLDEALAEAERIGYPVMLKATSGGGGRGIRRC 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  569 STKEELS-------ALVAPAFAhTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTV----CNMENldplgiHTGESIVVAPS 637
Cdd:PRK07178  171 NSREELEqnfprviSEATKAFG-SAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPS 243

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575501534  638 QTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEqYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:PRK07178  244 PQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGE-VYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLS 321
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
187-355 3.12e-13

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 70.28  E-value: 3.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  187 YNQIRCLCQLGAEVTVVPWDH----ELDSQKYDGLFLSNGPGDPaSYPGVvsTLSRVLSEPNPRPVFGICLGHQLLALAI 262
Cdd:PRK06774   13 YNLYQYFCELGTEVMVKRNDElqltDIEQLAPSHLVISPGPCTP-NEAGI--SLAVIRHFADKLPILGVCLGHQALGQAF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  263 GAKTYKMRYGNRG------HNQPCLLVGTGRCFLTSQNHGFAVDADSLPA-----GWAPLFTNANDCSneGIVHDSLPFF 331
Cdd:PRK06774   90 GARVVRARQVMHGktsaicHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGcfeltAWSERGGEMDEIM--GIRHRTLPLE 167

                         170       180
                  ....*....|....*....|....
gi 575501534  332 SVQFHPEHRAGPSDMELLfDVFLE 355
Cdd:PRK06774  168 GVQFHPESILSEQGHQLL-DNFLK 190
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
929-1250 4.30e-13

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 73.42  E-value: 4.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  929 DFRAPHVLVLGSgvyrigssvefDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLY------FDEISF-EVVMD 1001
Cdd:COG3919     2 MTMRFRVVVLGG-----------DINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVvvpdpgDDPEAFvDALLE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1002 IYELENPEGVILSMGGQLpnnMAMALHRQQ----CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQF 1077
Cdd:COG3919    71 LAERHGPDVLIPTGDEYV---ELLSRHRDEleehYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDAL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1078 CHTVGYPCVVRPSYvlSGAAMNV----------AYTDGDLERFLSSAAAVskEHPVVISKFIQEAKEIDVDAVAC---DG 1144
Cdd:COG3919   148 AEDLGFPVVVKPAD--SVGYDELsfpgkkkvfyVDDREELLALLRRIAAA--GYELIVQEYIPGDDGEMRGLTAYvdrDG 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1145 ----IVSAIAISEHVENAGVHSgdATLVTPPQDItpktLERIKAIVHAVGqelqVTGPFNLQLI--AKDDQLKVIECNVR 1218
Cdd:COG3919   224 evvaTFTGRKLRHYPPAGGNSA--ARESVDDPEL----EEAARRLLEALG----YHGFANVEFKrdPRDGEYKLIEINPR 293

                         330       340       350
                  ....*....|....*....|....*....|..
gi 575501534 1219 VSRSFPFVSKTlGVDLVALATRIIMGEKVEPV 1250
Cdd:COG3919   294 FWRSLYLATAA-GVNFPYLLYDDAVGRPLEPV 324
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
187-338 5.95e-13

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 70.08  E-value: 5.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  187 YNQIRCLCQLGAEVTVV------PWDHELDSQKYDGLFLSNGPGDPASyPGVVSTLSRVLSEPNpRPVFGICLGHQLLAL 260
Cdd:PRK07765   14 FNLVQYLGQLGVEAEVWrnddprLADEAAVAAQFDGVLLSPGPGTPER-AGASIDMVRACAAAG-TPLLGVCLGHQAIGV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  261 AIGA-----------KTYKMRYGNRGhnqpcLLVGTGRCFLTSQNHGFAVDADSLPA-----GWAPlftnandcsnEGIV 324
Cdd:PRK07765   92 AFGAtvdrapellhgKTSSVHHTGVG-----VLAGLPDPFTATRYHSLTILPETLPAelevtARTD----------SGVI 156

                         170
                  ....*....|....*...
gi 575501534  325 ----HDSLPFFSVQFHPE 338
Cdd:PRK07765  157 mavrHRELPIHGVQFHPE 174
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 178-338 1.35e-12

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 68.33  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  178 ICALDCGLKYNQI--RCLCQLGAEVTVVPWD---HELDSQKYDGLFLSNGPgdpasypgvvstlSRVLSEPNPR------ 246
Cdd:cd01742     1 ILILDFGSQYTHLiaRRVRELGVYSEILPNTtplEEIKLKNPKGIILSGGP-------------SSVYEEDAPRvdpeif 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  247 ----PVFGICLGHQLLALAIGAKTYKMRYGNRGH------NQPCLLVGTGRCFLTSQNHGFAVDAdsLPAGWAPLFTNAN 316
Cdd:cd01742    68 elgvPVLGICYGMQLIAKALGGKVERGDKREYGKaeieidDSSPLFEGLPDEQTVWMSHGDEVVK--LPEGFKVIASSDN 145

                         170       180
                  ....*....|....*....|..
gi 575501534  317 dCSNEGIVHDSLPFFSVQFHPE 338
Cdd:cd01742   146 -CPVAAIANEEKKIYGVQFHPE 166
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 187-338 5.62e-12

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 66.69  E-value: 5.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  187 YNQIRCLCQLGAEVTVVPWD----HELDSQKYDGLFLSNGPGDPA---SYPGVVSTLSRVLsepnprPVFGICLGHQLLA 259
Cdd:PRK05670   13 YNLVQYLGELGAEVVVYRNDeitlEEIEALNPDAIVLSPGPGTPAeagISLELIREFAGKV------PILGVCLGHQAIG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  260 LAIGA-----------KTYKMRygnrgHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGwapLFTNANDCSNE--GIVHD 326
Cdd:PRK05670   87 EAFGGkvvrakeimhgKTSPIE-----HDGSGIFAGLPNPFTVTRYHSLVVDRESLPDC---LEVTAWTDDGEimGVRHK 158

                         170
                  ....*....|..
gi 575501534  327 SLPFFSVQFHPE 338
Cdd:PRK05670  159 ELPIYGVQFHPE 170
PRK06895 PRK06895
anthranilate synthase component II;
187-338 9.55e-12

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 65.91  E-value: 9.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  187 YNQIRCLCQLGAEVTVVPWDhELD---SQKYDGLFLSNGPGDPASYPGVVSTLSRVLSEpnpRPVFGICLGHQLLALAIG 263
Cdd:PRK06895   15 FNLVDLIRKLGVPMQVVNVE-DLDldeVENFSHILISPGPDVPRAYPQLFAMLERYHQH---KSILGVCLGHQTLCEFFG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  264 AKTYKMRYGNRGHNQPCLLVGTGRCF--LTSQ-----NHGFAVDADSLPAgwaPLFTNANdCSNEGIV---HDSLPFFSV 333
Cdd:PRK06895   91 GELYNLNNVRHGQQRPLKVRSNSPLFdgLPEEfniglYHSWAVSEENFPT---PLEITAV-CDENVVMamqHKTLPIYGV 166


                  ....*
gi 575501534  334 QFHPE 338
Cdd:PRK06895  167 QFHPE 171
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
187-338 9.76e-12

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 66.05  E-value: 9.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  187 YNQIRCLCQLGAEVTVVPWDhELDSQKYDGL-----FLSNGPGDPASyPGVvsTLSRVLSEPNPRPVFGICLGHQLLALA 261
Cdd:PRK08857   13 YNLYQYFCELGAQVKVVRND-EIDIDGIEALnpthlVISPGPCTPNE-AGI--SLQAIEHFAGKLPILGVCLGHQAIAQV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  262 IGAKTYKMRYGNRGHNQPclLVGTGRCFLTSQN--------HGFAVDADSLPA-----GWAPLFTNANDcSNEGIVHDSL 328
Cdd:PRK08857   89 FGGQVVRARQVMHGKTSP--IRHTGRSVFKGLNnpltvtryHSLVVKNDTLPEcfeltAWTELEDGSMD-EIMGFQHKTL 165

                         170
                  ....*....|
gi 575501534  329 PFFSVQFHPE 338
Cdd:PRK08857  166 PIEAVQFHPE 175
DHOase cd01294
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ...
 1464-1778 2.06e-11

Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.


Pssm-ID: 238619  Cd Length: 335  Bit Score: 67.69  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1464 LPGLIDVHVHLREpgGTHKEDFASGTAAALAGGVTMvcamPNTRPPIIDAP-ALALAQKLAEAGARCDF----TLFLGAS 1538
Cdd:cd01294     3 IPRPDDMHLHLRD--GAMLKLVLPYTARGFSRAIVM----PNLKPPVTTTAdALAYRERILAADPGPNFtplmTLYLTEN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1539 -SENAGTLGAVAGSAAGLKLYLN--ETFSELRLDSVAQWMEHFETWPAH-LPIVAHAERQSVAAVLM---------VAQL 1605
Cdd:cd01294    77 tTPEELREAKKKGGIRGVKLYPAgaTTNSQGGVTDLEKIYPVLEAMQKLgMPLLVHGEVPDFKIDVLdreakfipvLEPL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1606 TQR-P---VHICHVARKEEILLIKTAKAqglPVTCEVAPHHLFLNREDLerLGPGKGEV---RPELGSREDMEALwENMA 1678
Cdd:cd01294   157 AQRfPklkIVLEHITTADAVEYVKSCNE---NVAATITPHHLLLTRDDL--LGGGLNPHlycKPVAKRPEDREAL-RKAA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1679 VIDC----FASDHAPHTLEEKCGPKPPPGFPGLETMLPLLLTAVSEGRlSLDDLLQRLHHNPRRIFHLPLQEDTYVEVdl 1754
Cdd:cd01294   231 TSGHpkffLGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHN-ALDKLEAFASDNGPNFYGLPPNKKTITLV-- 307

                         330       340
                  ....*....|....*....|....
gi 575501534 1755 EHEWTVPSHMPFSKARWTPFEGQK 1778
Cdd:cd01294   308 KEPWKVPEKIPFGNNGVVPFRAGE 331
PRK00758 PRK00758
GMP synthase subunit A; Validated
 177-338 2.06e-11

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 64.87  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  177 RICALDCGLKYNQI--RCLCQLGAEVTVVPWD---HELDSQKyDGLFLSNGPgdpasypgvvsTLSRV------LSEPNp 245
Cdd:PRK00758    1 KIVVVDNGGQYNHLihRTLRYLGVDAKIIPNTtpvEEIKAFE-DGLILSGGP-----------DIERAgncpeyLKELD- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  246 RPVFGICLGHQLLALAIGAKTYKMRYGNRG--------HNQPclLVGTGRCFLTSQNHgfavdAD---SLPAGWAPLFTN 314
Cdd:PRK00758   68 VPILGICLGHQLIAKAFGGEVGRGEYGEYAlveveildEDDI--LKGLPPEIRVWASH-----ADevkELPDGFEILARS 140

                         170       180
                  ....*....|....*....|....
gi 575501534  315 ANdCSNEGIVHDSLPFFSVQFHPE 338
Cdd:PRK00758  141 DI-CEVEAMKHKEKPIYGVQFHPE 163
MGS_CPS_II cd01424
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ...
 1314-1427 5.77e-11

Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.


Pssm-ID: 238712 [Multi-domain]  Cd Length: 110  Bit Score: 61.34  E-value: 5.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1314 NILLTIgSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILDQLAENHFELVI 1393
Cdd:cd01424     2 TVFISV-ADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEG--------RPNIVDLIKNGEIQLVI 72

                          90       100       110
                  ....*....|....*....|....*....|....
gi 575501534 1394 NlsmrGAGGRRlssFVTKGYRTRRLAADFSVPLI 1427
Cdd:cd01424    73 N----TPSGKR---AIRDGFSIRRAALEYKVPYF 99
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
498-716 8.87e-11

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 66.93  E-value: 8.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  498 GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP--SEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEEL- 574
Cdd:PRK08654   99 GIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELe 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  575 ------SALVAPAFAhTSQVLIDKSLKGWKEIEYEVVRDAYGNCvtvcnmenldplgIHTGES-----------IVVAPS 637
Cdd:PRK08654  179 daiestQSIAQSAFG-DSTVFIEKYLEKPRHIEIQILADKHGNV-------------IHLGDRecsiqrrhqklIEEAPS 244

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575501534  638 QTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALnpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:PRK08654  245 PIMTPELRERMGEAAVKAAKAINYENAGTVEFLY--SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELS 321
PRK08417 PRK08417
metal-dependent hydrolase;
1464-1794 1.13e-10

metal-dependent hydrolase;


Pssm-ID: 236262 [Multi-domain]  Cd Length: 386  Bit Score: 65.88  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1464 LPGLIDVHVHLREPGGTHKeDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQK---------------LAEAGAR 1528
Cdd:PRK08417   29 LPALVDLNVSLKNDSLSSK-NLKSLENECLKGGVGSIVLYPDSTPAIDNEIALELINSaqrelpmqifpsiraLDEDGKL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1529 CDF-TLF-LGA------SSENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPAHLP-IVAHAERQSVAAV 1599
Cdd:PRK08417  108 SNIaTLLkKGAkalelsSDLDANLLKVIAQYAKMLDVPIFCRCEDSSFDDSGVMNDGELSFELGLPgIPSIAETKEVAKM 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1600 LMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPgKGEVRPELGSREDMEALWENM-- 1677
Cdd:PRK08417  188 KELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSACENFNT-AAKLNPPLRSKEDRLALLEALke 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1678 AVIDCFASDHAPHTLEEK--CGPKPPPGFPGLETMLPLLLT-AVSEGRLSLDDLLQRLHHNPRRIFHLPLQEDT------ 1748
Cdd:PRK08417  267 GKIDFLTSLHSAKSNSKKdlAFDEAAFGIDSICEYFSLCYTyLVKEGIITWSELSRFTSYNPAQFLGLNSGEIEvgkead 346

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 575501534 1749 YVEVDLEHEWTVPSHMPfskarwtPFEGQKVKGTVRRVVLRGEVAY 1794
Cdd:PRK08417  347 LVLFDPNESTIIDDNFS-------LYSGDELYGKIEAVIIKGKLYL 385
PRK14805 PRK14805
ornithine carbamoyltransferase; Provisional
 1974-2162 1.61e-10

ornithine carbamoyltransferase; Provisional


Pssm-ID: 237819 [Multi-domain]  Cd Length: 302  Bit Score: 64.71  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1974 AKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGDlkhGRTV-HSL----ACLLTQYRVslryVAPPSL 2048
Cdd:PRK14805  111 AEHGSVPVINALCDL-YHPCQALADFLTLAEQFGDVSKVKLAYVGD---GNNVtHSLmygaAILGATMTV----ICPPGH 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2049 RMPPSV----RDFVASRGTKQEEFESIeEALPDTDVLYM-TRIQKERFGSVQEYEACFGQFILTPHIMTRAKKKMvVMHP 2123
Cdd:PRK14805  183 FPDGQIvaeaQELAAKSGGKLVLTSDI-EAIEGHDAIYTdTWISMGDDTPLAEIKAKFAPYQVNKALMEKAGATF-VMHC 260

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 575501534 2124 MP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2162
Cdd:PRK14805  261 QPahRGVEITSEVMDGEGSLILQQAENRMHAQNAVLVTLLS 301
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 498-716 2.19e-10

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 65.55  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  498 GVRVLGTPVETIELTEDRrAFAARMA-EIGEHVAPSEAA--NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEEL 574
Cdd:PRK12833  102 GLIFVGPDAQTIRTMGDK-ARARRTArRAGVPTVPGSDGvvASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQL 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  575 SALV------APAFAHTSQVLIDKSLKGWKEIEYEVVRDayGNCVTVCnMENLDPLGIHTGESIVVAPSQTLNDREYQLL 648
Cdd:PRK12833  181 AAELplaqreAQAAFGDGGVYLERFIARARHIEVQILGD--GERVVHL-FERECSLQRRRQKILEEAPSPSLTPAQRDAL 257

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575501534  649 RRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:PRK12833  258 CASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLR 325
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 1059-1219 5.31e-10

ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 396689 [Multi-domain]  Cd Length: 169  Bit Score: 60.35  E-value: 5.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1059 GISQPQWRELSDLESARQFCHTVGYPCVV---RPSYvlSGAAMNVAYTDGDLERFLSSAAAVskehPVVISKFIQEAKEI 1135
Cdd:pfam02222    4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEELGDG----PVIVEEFVPFDREL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1136 DVDAV-ACDGIVSAIAISEHVEnagvHSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFNLQL-IAKDDQLKVI 1213
Cdd:pfam02222   78 SVLVVrSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELfVTEDGDLLIN 153


                   ....*.
gi 575501534  1214 ECNVRV 1219
Cdd:pfam02222  154 ELAPRP 159
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
187-361 1.16e-09

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 63.20  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  187 YNQIRCLCQLGAE-VTVVPWDH----ELDSQKYDGLFLSNGPGDPASyPG----VVSTLSRVLsepnprPVFGICLGHQL 257
Cdd:PRK14607   13 YNIYQYIGELGPEeIEVVRNDEitieEIEALNPSHIVISPGPGRPEE-AGisveVIRHFSGKV------PILGVCLGHQA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  258 LALAIGAKTYKMRYGNRGHNQPCLLVGTG------RCFLTSQNHGFAVDADSLPAGWAPLfTNANDCSNEGIVHDSLPFF 331
Cdd:PRK14607   86 IGYAFGGKIVHAKRILHGKTSPIDHNGKGlfrgipNPTVATRYHSLVVEEASLPECLEVT-AKSDDGEIMGIRHKEHPIF 164

                         170       180       190
                  ....*....|....*....|....*....|
gi 575501534  332 SVQFHPEhRAGPSDMELLFDVFLETVREAA 361
Cdd:PRK14607  165 GVQFHPE-SILTEEGKRILKNFLNYQREEI 193
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
187-362 1.46e-09

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 59.82  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  187 YNQIRCLCQLGAEVTVVPWDH----ELDSQKYDGLFLSNGPGDPaSYPGVvsTLSRVLSEPNPRPVFGICLGHQLLALAI 262
Cdd:PRK07649   13 FNLVQFLGELGQELVVKRNDEvtisDIENMKPDFLMISPGPCSP-NEAGI--SMEVIRYFAGKIPIFGVCLGHQSIAQVF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  263 GA---KTYKMRYGNRG---HNQPCLLVGTGRCFLTSQNHGFAVDADSLPagwaplftnanDC------SNEG----IVHD 326
Cdd:PRK07649   90 GGevvRAERLMHGKTSlmhHDGKTIFSDIPNPFTATRYHSLIVKKETLP-----------DClevtswTEEGeimaIRHK 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 575501534  327 SLPFFSVQFHPEHRAGPSDMELLFDvFLETVREAAA 362
Cdd:PRK07649  159 TLPIEGVQFHPESIMTSHGKELLQN-FIRKYSPSVT 193
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 987-1237 1.46e-09

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 61.50  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  987 DRLYFDEISFEVVMDIYELENPEGVILsmgGQLPNNMAMA----LHRQQCRVLGtSPEAIDSAENRFKFSRLLDTIGISQ 1062
Cdd:COG0189    36 DDLTLDLGRAPELYRGEDLSEFDAVLP---RIDPPFYGLAllrqLEAAGVPVVN-DPEAIRRARDKLFTLQLLARAGIPV 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1063 PQWRELSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEhPVVISKFIQEAKEIDVDAVAC 1142
Cdd:COG0189   112 PPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELGSE-PVLVQEFIPEEDGRDIRVLVV 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1143 DG-IVSAIA-ISEHVENAG-VHSGDATLvtpPQDITPKTLERIKAIVHAVGqeLQVTGpfnLQLIAKDDQLKVIECNVRV 1219
Cdd:COG0189   191 GGePVAAIRrIPAEGEFRTnLARGGRAE---PVELTDEERELALRAAPALG--LDFAG---VDLIEDDDGPLVLEVNVTP 262

                         250
                  ....*....|....*...
gi 575501534 1220 srSFPFVSKTLGVDLVAL 1237
Cdd:COG0189   263 --GFRGLERATGVDIAEA 278
trpG CHL00101
anthranilate synthase component 2
 187-338 1.55e-09

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 59.74  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  187 YNQIRCLCQLGAEVTVVPWDhELDSQKYD-----GLFLSNGPGDPASYP---GVVSTLSrvlsepNPRPVFGICLGHQLL 258
Cdd:CHL00101   13 YNLVQSLGELNSDVLVCRND-EIDLSKIKnlnirHIIISPGPGHPRDSGislDVISSYA------PYIPILGVCLGHQSI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  259 ALAIGAKTYKMRYGNRG------HNQPCLLVGTGRCFLTSQNHGFAVDADSLPagwAPLFTNANdcSNEGIV----HDSL 328
Cdd:CHL00101   86 GYLFGGKIIKAPKPMHGktskiyHNHDDLFQGLPNPFTATRYHSLIIDPLNLP---SPLEITAW--TEDGLImacrHKKY 160

                         170
                  ....*....|.
gi 575501534  329 PF-FSVQFHPE 338
Cdd:CHL00101  161 KMlRGIQFHPE 171
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 498-687 2.05e-09

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 63.23  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  498 GVRVLGTPVETIELTEDRraFAARMA--EIGEHVAPS--EAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEE 573
Cdd:PRK12999  103 GITFIGPTAEVLRLLGDK--VAARNAaiKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  574 LSALVAPA-------FAhTSQVLIDKSLKGWKEIEYEVVRDAYGNCVtvcnmenldplgiHTGE---SI------VV--A 635
Cdd:PRK12999  181 LEEAFERAkreakaaFG-NDEVYLEKYVENPRHIEVQILGDKHGNVV-------------HLYErdcSVqrrhqkVVeiA 246

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 575501534  636 PSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESeQYYIIEVNARL 687
Cdd:PRK12999  247 PAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADG-NFYFIEVNPRI 297
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 498-712 3.51e-09

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 61.75  E-value: 3.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  498 GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAAN--SLEQAQAAAERLGYPVLVRAAFALGGLG---------- 564
Cdd:PRK08463   98 GIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPgTEKLNseSMEEIKIFARKIGYPVILKASGGGGGRGirvvhkeedl 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  565 -SGFASTKEElsalvAPAFAHTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCnmENLDPLGIHTGESIVVAPSQTLNDR 643
Cdd:PRK08463  178 eNAFESCKRE-----ALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLC--ERDCSIQRRHQKVIEIAPCPSISDN 250

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575501534  644 EYQLLRRTAIKVTQHLGIVGECNVQYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALG 712
Cdd:PRK08463  251 LRKTMGVTAVAAAKAVGYTNAGTIEFLLD-DYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318
PRK02102 PRK02102
ornithine carbamoyltransferase; Validated
 1921-2162 9.41e-09

ornithine carbamoyltransferase; Validated


Pssm-ID: 179366 [Multi-domain]  Cd Length: 331  Bit Score: 59.51  E-value: 9.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1921 LVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMF----------YELA----------------- 1973
Cdd:PRK02102    5 LKGRSFLKLLDFTPEEIEYLIDLSIELKAAKKAGIEHQYLEGKNIALIFektstrtrcaFEVAaidlgahvtylgpndsq 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1974 ----------------------------------AKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGD 2019
Cdd:PRK02102   85 lgkkesiedtarvlgrmydgieyrgfkqeiveelAKYSGVPVWNGLTDE-WHPTQMLADFMTMKEHFGPLKGLKLAYVGD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2020 lkhGR--TVHSL---ACLLTqyrVSLRYVAPPSLRmpPS------VRDFVASRGTKQEEFESIEEALPDTDVLYmTRI-- 2086
Cdd:PRK02102  164 ---GRnnMANSLmvgGAKLG---MDVRICAPKELW--PEeelvalAREIAKETGAKITITEDPEEAVKGADVIY-TDVwv 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2087 -------QKERFGSVQEYEacfgqfiLTPHIMTR-AKKKMVVMHPMP-----------------RVNEISV--EVDSDPR 2139
Cdd:PRK02102  235 smgeedeWEERIKLLKPYQ-------VNMDLMKAtGNPDVIFMHCLPafhdtetkvgkeiaekyGLKGLEVtdEVFESKY 307

                         330       340
                  ....*....|....*....|...
gi 575501534 2140 AAYFRQAENGMYIRMALLATVLG 2162
Cdd:PRK02102  308 SIVFDEAENRMHTIKAVMVATLG 330
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 190-263 9.88e-09

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 55.30  E-value: 9.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  190 IRCLCQLGAEVTVVPWDH-----ELDSQKYDGLFLSNGPGDP---ASYPGVVSTLSRVLSepNPRPVFGICLGHQLLALA 261
Cdd:cd01653    18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPddlARDEALLALLREAAA--AGKPILGICLGAQLLVLG 95


                  ..
gi 575501534  262 IG 263
Cdd:cd01653    96 VQ 97
PRK04284 PRK04284
ornithine carbamoyltransferase; Provisional
 1934-2163 1.74e-08

ornithine carbamoyltransferase; Provisional


Pssm-ID: 235269 [Multi-domain]  Cd Length: 332  Bit Score: 58.60  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1934 KDQMSHLFNVAHTLRMMVQKERSLDilKGKVMASMF------------YELAAKHCRRPVINaGDGVGEHPTQALLDIFT 2001
Cdd:PRK04284   68 YDQGAHVTYLGPTGSQMGKKESTKD--TARVLGGMYdgieyrgfsqrtVETLAEYSGVPVWN-GLTDEDHPTQVLADFLT 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2002 IREEL-GTVNGMTITMVGDlkhGRTVHSLACLLTQYRVSLRY--VAPPSLRMPPSV----RDFVASRGTKQEEFESIEEA 2074
Cdd:PRK04284  145 AKEHLkKPYKDIKFTYVGD---GRNNVANALMQGAAIMGMDFhlVCPKELNPDDELlnkcKEIAAETGGKITITDDIDEG 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2075 LPDTDVLYM---------TRIQKERFGSVQEYEacfgqfiLTPHIMTRAKKKMVV-MHPMPRVN---------------- 2128
Cdd:PRK04284  222 VKGSDVIYTdvwvsmgepDEVWEERIKLLKPYQ-------VNKEMMKKTGNPNAIfEHCLPSFHdldtkvgkeifekygl 294

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 575501534 2129 ---EISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2163
Cdd:PRK04284  295 kemEVTDEVFESKASVVFDEAENRMHTIKAVMVATLGE 332
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
502-715 2.22e-08

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 58.96  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  502 LGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLG-----------SGFA 568
Cdd:PRK05586  103 IGPDSETIELMGNKSNAREIMIKAGVPVVPgSEGEiENEEEALEIAKEIGYPVMVKASAGGGGRGirivrseeeliKAFN 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  569 STKEELSAlvapAFAHTSqVLIDKSLKGWKEIEYEVVRDAYGNCVTV----CNMENldplgiHTGESIVVAPSQTLNDRE 644
Cdd:PRK05586  183 TAKSEAKA----AFGDDS-MYIEKFIENPKHIEFQILGDNYGNVVHLgerdCSLQR------RNQKVLEEAPSPVMTEEL 251

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501534  645 YQLLRRTAIKVTQHLGIVGECNVQYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPL 715
Cdd:PRK05586  252 RKKMGEIAVKAAKAVNYKNAGTIEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
187-338 6.84e-08

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 54.54  E-value: 6.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  187 YNQIRCLCQLGAEVTVVPWDH----ELDSQKYDGLFLSNGPGDPaSYPGVvsTLSRVLSEPNPRPVFGICLGHQLLALAI 262
Cdd:PRK08007   13 WNLYQYFCELGADVLVKRNDAltlaDIDALKPQKIVISPGPCTP-DEAGI--SLDVIRHYAGRLPILGVCLGHQAMAQAF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  263 GAKTYKMRYGNRGHNQPCLLVGTG------RCFLTSQNHGFAVDADSLPAGWAplfTNANDCSNE--GIVHDSLPFFSVQ 334
Cdd:PRK08007   90 GGKVVRAAKVMHGKTSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLEGVQ 166


                  ....
gi 575501534  335 FHPE 338
Cdd:PRK08007  167 FHPE 170
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 190-258 8.00e-08

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 51.82  E-value: 8.00e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501534  190 IRCLCQLGAEVTVVPWDH-----ELDSQKYDGLFLSNGPGDP---ASYPGVVSTLSRVLSepNPRPVFGICLGHQLL 258
Cdd:cd03128    18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPddlAWDEALLALLREAAA--AGKPVLGICLGAQLL 92
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 507-687 8.84e-08

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 57.12  E-value: 8.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  507 ETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELsalvAPAFAH 584
Cdd:PRK08591  108 ETIRLMGDKVTAKATMKKAGVPVVPgSDGPvDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAEL----EKAFSM 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  585 TSQ----------VLIDKSLKGWKEIEYEVVRDAYGNcvtvcnmenldplGIHTGE---SI------VV--APSQTLNDR 643
Cdd:PRK08591  184 ARAeakaafgnpgVYMEKYLENPRHIEIQVLADGHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEE 250

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 575501534  644 EYQLLRRTAIKVTQHLGIVGECNVQYaLNPESEQYYIIEVNARL 687
Cdd:PRK08591  251 LRRKIGEAAVKAAKAIGYRGAGTIEF-LYEKNGEFYFIEMNTRI 293
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 498-686 1.56e-07

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 57.01  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  498 GVRVLGTPVETIELTEDRRAfAARMA-EIGEHVAPS--EAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEEL 574
Cdd:COG1038   102 GITFIGPSPEVLEMLGDKVA-ARAAAiEAGVPVIPGteGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEEL 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  575 SALVAPAF--AHTS----QVLIDKSLKGWKEIEYEVVRDAYGNCVtvcnmenldplgiHTGE---SI------VV--APS 637
Cdd:COG1038   181 EEAFESARreAKAAfgddEVFLEKYIERPKHIEVQILGDKHGNIV-------------HLFErdcSVqrrhqkVVeiAPA 247

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 575501534  638 QTLNDREYQLLRRTAIKVTQHLGIVGECNVQYaLNPESEQYYIIEVNAR 686
Cdd:COG1038   248 PNLDEELREAICEAAVKLAKAVGYVNAGTVEF-LVDDDGNFYFIEVNPR 295
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 1464-1792 5.46e-07

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 54.04  E-value: 5.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1464 LPGLIDVHVHLR--------EPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDApalalaqkLAEAgarcdftlfl 1535
Cdd:pfam01979    3 LPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEA--------LLEA---------- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1536 gASSENAGtLGAVAGSAAGLKLYLNETFSELRLDSVAQWM-EHFETWPAHLPIVAHAERQSV-----AAVLMVAQLTQRP 1609
Cdd:pfam01979   65 -AEELPLG-LRFLGPGCSLDTDGELEGRKALREKLKAGAEfIKGMADGVVFVGLAPHGAPTFsddelKAALEEAKKYGLP 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1610 VHIcHVARKEEILLIKTAKAQG----------------LPVTCEVAPHHLFLNREDLERLGPGKGEVR------PELGSR 1667
Cdd:pfam01979  143 VAI-HALETKGEVEDAIAAFGGgiehgthlevaesgglLDIIKLILAHGVHLSPTEANLLAEHLKGAGvahcpfSNSKLR 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1668 EDMEALWE--NMAVIDCFASDHAPHTleekcgpkpPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQ 1745
Cdd:pfam01979  222 SGRIALRKalEDGVKVGLGTDGAGSG---------NSLNMLEELRLALELQFDPEGGLSPLEALRMATINPAKALGLDDK 292

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 575501534  1746 EDTyVEV----DLehewtvpshMPFSKARWTPFEGQKVKGTVRRVVLRGEV 1792
Cdd:pfam01979  293 VGS-IEVgkdaDL---------VVVDLDPLAAFFGLKPDGNVKKVIVKGKI 333
guaA PRK00074
GMP synthase; Reviewed
 177-338 8.32e-07

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 53.90  E-value: 8.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  177 RICALDCGLKYNQ-----IRclcQLGAEVTVVPWDH---ELDSQKYDGLFLSNGPgdpASypgvvstlsrVLSEPNPR-- 246
Cdd:PRK00074    5 KILILDFGSQYTQliarrVR---ELGVYSEIVPYDIsaeEIRAFNPKGIILSGGP---AS----------VYEEGAPRad 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  247 --------PVFGICLGHQLLALAIGAK---TYKMRYGN---RGHNQPCLLVGTGRCFLTSQNHGFAVDAdsLPAGWAPLF 312
Cdd:PRK00074   69 peifelgvPVLGICYGMQLMAHQLGGKverAGKREYGRaelEVDNDSPLFKGLPEEQDVWMSHGDKVTE--LPEGFKVIA 146

                         170       180
                  ....*....|....*....|....*.
gi 575501534  313 TNANdCSNEGIVHDSLPFFSVQFHPE 338
Cdd:PRK00074  147 STEN-CPIAAIANEERKFYGVQFHPE 171
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 215-353 1.46e-06

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 50.65  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  215 DGLFLSNGPG-DPASYPGVVSTlsrVLSEPNPR-----------------PVFGICLGHQLLALAIGAKTYKMRYGNRGH 276
Cdd:cd01745    55 DGLLLTGGGDvDPPLYGEEPHP---ELGPIDPErdafelallraalergkPILGICRGMQLLNVALGGTLYQDIRVNSLH 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575501534  277 NQpcllvgtgrcfltsqnhgfAVDAdsLPAGWAPLFTnANDCSNEGIVHDSLPF-FSVQFHPE-HRAGPSDMELLFDVF 353
Cdd:cd01745   132 HQ-------------------AIKR--LADGLRVEAR-APDGVIEAIESPDRPFvLGVQWHPEwLADTDPDSLKLFEAF 188
PRK14804 PRK14804
ornithine carbamoyltransferase; Provisional
 1980-2161 1.79e-06

ornithine carbamoyltransferase; Provisional


Pssm-ID: 173265 [Multi-domain]  Cd Length: 311  Bit Score: 52.34  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1980 PVINAGDGVGeHPTQALLDIFTIREELGTV--NGMTITMVGdlKHGRTVHSLACLLTQYRVSLRYVAPPSLR--MPPSVR 2055
Cdd:PRK14804  121 PVINGCDNMF-HPCQSLADIMTIALDSPEIplNQKQLTYIG--VHNNVVNSLIGITAALGIHLTLVTPIAAKenIHAQTV 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 2056 DFVASRGTKQEEfESIEEALPDTDVLYM--------------TRIQKERFGSVQEYEacfgqfiLTPHIMTRAKKKmvVM 2121
Cdd:PRK14804  198 ERAKKKGTLSWE-MNLHKAVSHADYVYTdtwldmeffndpsyADKKKQRMELMMPYQ-------INSSLMEKTNAK--VM 267

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 575501534 2122 HPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVL 2161
Cdd:PRK14804  268 HDMPihAGYEITREVVLSDRSIIFQQAENRLDAQKAVILKLL 309
PRK06849 PRK06849
hypothetical protein; Provisional
 1032-1219 2.63e-06

hypothetical protein; Provisional


Pssm-ID: 235876 [Multi-domain]  Cd Length: 389  Bit Score: 51.97  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1032 CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCH-TVGYPCVVRPSYVLSGAAMNVAYTdgdlERF 1110
Cdd:PRK06849  101 CEVLHFDFELLLLLHNKWEFAEQARSLGLSVPKTYLITDPEAIRNFMFkTPHTPYVLKPIYSRFVRRVDLLPK----EAA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1111 LSSaAAVSKEHPVVISKFIQeAKEIDVDAVACDGIVSAIAISEHVENAGVHSGDATlvtppQDITPktlERIKAIVHAVG 1190
Cdd:PRK06849  177 LKE-LPISKDNPWVMQEFIQ-GKEYCSYSIVRSGELRAHSCYKPEYCAGSGAQIAF-----QPINH---PRIEEFVTHFV 246

                         170       180       190
                  ....*....|....*....|....*....|
gi 575501534 1191 QELQVTGPFNLQLI-AKDDQLKVIECNVRV 1219
Cdd:PRK06849  247 KELNYTGQISFDFIeTENGDAYPIECNPRT 276
PLN02942 PLN02942
dihydropyrimidinase
 1446-1809 7.28e-06

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 51.00  E-value: 7.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1446 APPLKVHVDCMT---SQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGVTMvcampntrppIID-------- 1512
Cdd:PLN02942   36 APNLKVPDDVRVidaTGKFV-MPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTTM----------HIDfvipvngn 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1513 -APALALAQKLAEAGArCDFTLFLGAS------SENAGTLGAVAGSAAgLKLYLNETFS-----ELRLDSVAQW------ 1574
Cdd:PLN02942  105 lLAGYEAYEKKAEKSC-MDYGFHMAITkwddtvSRDMETLVKEKGINS-FKFFMAYKGSlmvtdELLLEGFKRCkslgal 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1575 -MEHFETWPA---------HLPIVA---HA-------ERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPV 1634
Cdd:PLN02942  183 aMVHAENGDAvfegqkrmiELGITGpegHAlsrppllEGEATARAIRLAKFVNTPLYVVHVMSIDAMEEIARARKSGQRV 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1635 TCEVAPHHLFLNRE---DLERLGPGKGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKP------PPG 1703
Cdd:PLN02942  263 IGEPVVSGLVLDDSklwDPDFTIASKYVMSPPIRPAGHGKALQAALSsgILQLVGTDHCPFNSTQKAFGKDdfrkipNGV 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1704 FPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFH--------LPLQEDTYVEVDLEHEWTVPSHMPFSKARWTPFE 1775
Cdd:PLN02942  343 NGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNiyprkgaiLAGSDADIIILNPNSTFTISAKTHHSRIDTNVYE 422

                         410       420       430
                  ....*....|....*....|....*....|....
gi 575501534 1776 GQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDV 1809
Cdd:PLN02942  423 GRRGKGKVEVTISQGRVVWENGELKVVRGSGRYI 456
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 536-684 1.29e-05

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 48.47  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   536 NSLEQAQAAAERLGYPVLVRAAfalgGLGSGFASTK----EELSALVAPAFAHTSQVLIDKSLKGwKEIEyevvrdaygn 611
Cdd:pfam07478   23 NPKEWCAQVEEALGYPVFVKPA----RLGSSVGVSKvesrEELQAAIEEAFQYDEKVLVEEGIEG-REIE---------- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   612 cVTVCNMENLDPLGIH------------------TGESIVVAPsqtLNDREYQLLRRTAIKVTQHLGIVGECNVQYALnP 673
Cdd:pfam07478   88 -CAVLGNEDPEVSPVGeivpsggfydyeakyiddSAQIVVPAD---LEEEQEEQIQELALKAYKALGCRGLARVDFFL-T 162

                          170
                   ....*....|.
gi 575501534   674 ESEQYYIIEVN 684
Cdd:pfam07478  163 EDGEIVLNEVN 173
PLN02335 PLN02335
anthranilate synthase
 187-338 1.69e-05

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 48.25  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  187 YNQIRCLCQLGAEVTVVPWDH----ELDSQKYDGLFLSNGPGDPASyPGVvsTLSRVLSEPNPRPVFGICLGHQLLALAI 262
Cdd:PLN02335   32 YNLCQYMGELGCHFEVYRNDEltveELKRKNPRGVLISPGPGTPQD-SGI--SLQTVLELGPLVPLFGVCMGLQCIGEAF 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  263 GAKTYKMRYG-NRGHNQPC---------LLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDSLPFFS 332
Cdd:PLN02335  109 GGKIVRSPFGvMHGKSSPVhydekgeegLFSGLPNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQ 188


                  ....*..
gi 575501534  333 -VQFHPE 338
Cdd:PLN02335  189 gVQFHPE 195
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 1053-1185 3.12e-05

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 48.18  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1053 RLLDTIGISQPQWRELS--DLESARQFCHTVGYPCVVRPsyVLSGAA--MNVAYTDGDLERFLSSAAAVSkeHPVVISKF 1128
Cdd:COG1181   101 RVLAAAGLPTPPYVVLRrgELADLEAIEEELGLPLFVKP--AREGSSvgVSKVKNAEELAAALEEAFKYD--DKVLVEEF 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575501534 1129 IqEAKEIDVdAVACDGIVSAIAISEHVENAGV-------HSGDATLVTPPqDITPKTLERIKAI 1185
Cdd:COG1181   177 I-DGREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPA-RLPEELEERIQEL 237
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 1054-1242 5.79e-05

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 46.16  E-value: 5.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1054 LLDTIGISQPQW-------RELSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLssAAAVSKEHPVVIS 1126
Cdd:pfam07478    1 LLKAAGLPVVPFvtftradWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAI--EEAFQYDEKVLVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1127 KFIqEAKEIDVdAVACDGIVSAIAISEHVENAGV------HSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTG--- 1197
Cdd:pfam07478   79 EGI-EGREIEC-AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGlar 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 575501534  1198 -PFNLQliaKDDQLKVIECN-----VRVSRsFPFVSKTLGVDLVALATRII 1242
Cdd:pfam07478  157 vDFFLT---EDGEIVLNEVNtipgfTSISM-FPKLAAAAGVSFPDLVDQLI 203
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 395-718 6.45e-05

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 47.41  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  395 KVLILgSGGLSigqaGEFD---YSGSQAIKALKEENIQtllinpniatvqtsqgladkVYFLPITLHYVTQVIRNERPDG 471
Cdd:COG1181     2 RVAVL-FGGRS----AEREvslKSGRAVAAALDKAGYD--------------------VVPIGIDVEDLPAALKELKPDV 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  472 VLLtfggqtALNC--GVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANS--LEQAQAAAER 547
Cdd:COG1181    57 VFP------ALHGrgGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRgeLADLEAIEEE 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  548 LGYPVLVRAAFAlgglGSGF----ASTKEELSALVAPAFAHTSQVLIDKSLKGwKEIEyevvrdaygncVTVCNMENLDP 623
Cdd:COG1181   131 LGLPLFVKPARE----GSSVgvskVKNAEELAAALEEAFKYDDKVLVEEFIDG-REVT-----------VGVLGNGGPRA 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  624 LGI----------------HTGESIVVAPSQtLNDREYQLLRRTAIKVTQHLGIVGecnvqYA-----LNPEsEQYYIIE 682
Cdd:COG1181   195 LPPieivpengfydyeakyTDGGTEYICPAR-LPEELEERIQELALKAFRALGCRG-----YArvdfrLDED-GEPYLLE 267

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 575501534  683 VNAR--LSRSSalaskatGYPLAYVAAklalGIPLPEL 718
Cdd:COG1181   268 VNTLpgMTPTS-------LLPKAAAAA----GISYEEL 294
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 529-684 7.92e-05

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 47.03  E-value: 7.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  529 VAPSEAANSLEQAQAAAERLGYPVLVRAafALGG--LGSGFASTKEELSALVAPAFAHTSQVLIDKSLKGwkeIEYevvr 606
Cdd:PRK01372  113 TPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGssVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKG---REL---- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  607 daygncvTVCNMEN--LDPLGI-------------HTGESIVVAPSQtLNDREYQLLRRTAIKVTQHLGIVGECNVQYAL 671
Cdd:PRK01372  184 -------TVAVLGGkaLPVIEIvpagefydyeakyLAGGTQYICPAG-LPAEIEAELQELALKAYRALGCRGWGRVDFML 255

                         170
                  ....*....|...
gi 575501534  672 NpESEQYYIIEVN 684
Cdd:PRK01372  256 D-EDGKPYLLEVN 267
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 247-338 1.41e-04

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 45.33  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534   247 PVFGICLGHQLLALAIGAKTY---KMRYGNRGHNQPC----------LLVGTGRCF--LTSQN-------HGFAVDAdsL 304
Cdd:pfam07722  107 PILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapshaVNVEPGSLLasLLGSEefrvnslHHQAIDR--L 184

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 575501534   305 PAGWAPLFTnANDCSNEGIVHDSLPFF--SVQFHPE 338
Cdd:pfam07722  185 APGLRVEAV-APDGTIEAIESPNAKGFalGVQWHPE 219
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 214-338 3.30e-04

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 45.99  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  214 YDGLFLSNGPGDPASyPGVVSTLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKM------RYGNRGHNQpCLL---VG 284
Cdd:PLN02889  132 FDNIVISPGPGSPTC-PADIGICLRLLLECRDIPILGVCLGHQALGYVHGARIVHApepvhgRLSEIEHNG-CRLfddIP 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  285 TGR--CFLTSQNHGFAVDADSLPAGWAPL-FTNAND----------------CSNE------------------------ 321
Cdd:PLN02889  210 SGRnsGFKVVRYHSLVIDAESLPKELVPIaWTSSSDtlsflesqksglvpdaYESQigqsgssdpfssklkngtswpssh 289

                         170       180
                  ....*....|....*....|....*...
gi 575501534  322 -----------GIVHDSLPFFSVQFHPE 338
Cdd:PLN02889  290 sermqngkilmGIMHSTRPHYGLQFHPE 317
ddl PRK01966
D-alanine--D-alanine ligase;
522-601 5.26e-04

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 44.73  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  522 MAEIGEHVAPSEAANSLEQA----QAAAERLGYPVLVRAAfalgGLGSGF----ASTKEELSALVAPAFAHTSQVLIDKS 593
Cdd:PRK01966  131 LAAAGIPVAPYVVLTRGDWEeaslAEIEAKLGLPVFVKPA----NLGSSVgiskVKNEEELAAALDLAFEYDRKVLVEQG 206


                  ....*...
gi 575501534  594 LKGwKEIE 601
Cdd:PRK01966  207 IKG-REIE 213
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
1068-1249 6.32e-04

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 44.74  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1068 LSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVAYTDGDLER-FL---SSAAAVSKEHPVVISKFIQEAKEIDVDAVAcD 1143
Cdd:PRK08462  140 LKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENlYLaaeSEALSAFGDGTMYMEKFINNPRHIEVQILG-D 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1144 GIVSAIAISEhvENAGVHSGDATLV--TPPQDITPKTLER-----IKAiVHAVGQELQVTGPFnlqLIAKDDQLKVIECN 1216
Cdd:PRK08462  219 KHGNVIHVGE--RDCSLQRRHQKLIeeSPAVVLDEKTRERlhetaIKA-AKAIGYEGAGTFEF---LLDSNLDFYFMEMN 292

                         170       180       190
                  ....*....|....*....|....*....|...
gi 575501534 1217 VRVSRSFPFVSKTLGVDLVALATRIIMGEKVEP 1249
Cdd:PRK08462  293 TRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPS 325
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1842-1921 8.79e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.76  E-value: 8.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  1842 PGLPDGRFHLPPRIHRASDPgLPAEEPKEKPPRKVVE------PELMGTPDGPCYPA--PPVPRQASPQNLgSSGLLHPQ 1913
Cdd:pfam03154  197 AGPTPSAPSVPPQGSPATSQ-PPNQTQSTAAPHTLIQqtptlhPQRLPSPHPPLQPMtqPPPPSQVSPQPL-PQPSLHGQ 274


                   ....*...
gi 575501534  1914 MSPLLHSL 1921
Cdd:pfam03154  275 MPPMPHSL 282
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
1035-1141 9.18e-04

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 44.20  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1035 LGTSPEAIDSAENRFKFSRLLDTIGISQPQWRE--LSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLS 1112
Cdd:PRK08654  103 IGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEegIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIE 182

                          90       100       110
                  ....*....|....*....|....*....|...
gi 575501534 1113 S----AAAVSKEHPVVISKFIQEAKEIDVDAVA 1141
Cdd:PRK08654  183 StqsiAQSAFGDSTVFIEKYLEKPRHIEIQILA 215
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 507-663 9.39e-04

Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439797 [Multi-domain]  Cd Length: 353  Bit Score: 43.91  E-value: 9.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  507 ETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFalGGL-GSG--FASTKEELSALVApafA 583
Cdd:COG0026    82 EALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRR--GGYdGKGqvVIKSAADLEAAWA---A 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  584 HTSQVLIdksLKGWKEIEYE----VVRDAYGNCVT--VCnmENldplgIHTG----ESIVVAP-SQTLNDReyqlLRRTA 652
Cdd:COG0026   157 LGGGPCI---LEEFVPFERElsviVARSPDGEVATypVV--EN-----VHRNgildESIAPARiSEALAAE----AEEIA 222

                         170
                  ....*....|.
gi 575501534  653 IKVTQHLGIVG 663
Cdd:COG0026   223 KRIAEALDYVG 233
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 1443-1595 1.37e-03

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 43.41  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1443 IGPAPPLKV-----HVDCmtSQKLVrLPGLIDVHVHLREPGGTHKEDFASGT---------------AAALAGGVTMVCA 1502
Cdd:COG1228    41 VGPAADLAVpagaeVIDA--TGKTV-LPGLIDAHTHLGLGGGRAVEFEAGGGitptvdlvnpadkrlRRALAAGVTTVRD 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1503 MPNTRPPIIDAPA------LALAQKLAEAGArcdFTLFLGASSENAGTLGAV-----AGSAAGLKLYLNETFSELRLDSV 1571
Cdd:COG1228   118 LPGGPLGLRDAIIagesklLPGPRVLAAGPA---LSLTGGAHARGPEEARAAlrellAEGADYIKVFAEGGAPDFSLEEL 194

                         170       180
                  ....*....|....*....|....
gi 575501534 1572 AQWMEhfETWPAHLPIVAHAERQS 1595
Cdd:COG1228   195 RAILE--AAHALGLPVAAHAHQAD 216
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 1036-1275 1.52e-03

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 43.68  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1036 GTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHTVGYPCVVRPsyVLSGAAMNVAYTDGDLERFLSSAA 1115
Cdd:PRK02186   96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKP--RMGSGSVGVRLCASVAEAAAHCAA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1116 AVSKEHPVVISKFIQEAKEIDVDAVACDGIVSAIAISE-------HVENAGvHSGDATLVTPPQDITPKTLERikaIVHA 1188
Cdd:PRK02186  174 LRRAGTRAALVQAYVEGDEYSVETLTVARGHQVLGITRkhlgpppHFVEIG-HDFPAPLSAPQRERIVRTVLR---ALDA 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534 1189 VGQELqvtGPFNLQLIAKDDQLKVIECNVRVSRSF-P-FVSKTLGVDLVALATRIIMGEKVEPVGLMTGSGVVGVKVPQF 1266
Cdd:PRK02186  250 VGYAF---GPAHTELRVRGDTVVIIEINPRLAGGMiPvLLEEAFGVDLLDHVIDLHLGVAAFADPTAKRYGAIRFVLPAR 326


                  ....*....
gi 575501534 1267 SfSRLAGAD 1275
Cdd:PRK02186  327 S-GVLRGLL 334
PRK14570 PRK14570
D-alanyl-alanine synthetase A; Provisional
 1080-1145 1.93e-03

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173034 [Multi-domain]  Cd Length: 364  Bit Score: 42.90  E-value: 1.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575501534 1080 TVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVskEHPVVISKFIqEAKEIDVDAVACDGI 1145
Cdd:PRK14570  169 VLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKY--DLTVVIEKFI-EAREIECSVIGNEQI 231
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 507-663 5.89e-03

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 41.29  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  507 ETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFaLG--GLGSGFASTKEELSALVApafAH 584
Cdd:PRK06019   93 DALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTRR-GGydGKGQWVIRSAEDLEAAWA---LL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501534  585 TSQVLIdksLKGWKEIEYE----VVRDAYGNCVT---VcnmENLDPLGI-HTgesiVVAPSQtLNDREYQLLRRTAIKVT 656
Cdd:PRK06019  169 GSVPCI---LEEFVPFEREvsviVARGRDGEVVFyplV---ENVHRNGIlRT----SIAPAR-ISAELQAQAEEIASRIA 237


                  ....*..
gi 575501534  657 QHLGIVG 663
Cdd:PRK06019  238 EELDYVG 244
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 191-259 6.43e-03

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 40.17  E-value: 6.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575501534  191 RCLCQLGAEVTVVPWDHELdsQKYDGLFLsngPGDPASYPGVVSTLSRVLSEP------NPRPVFGICLGHQLLA 259
Cdd:cd01748    16 NALERLGAEVIITSDPEEI--LSADKLIL---PGVGAFGDAMANLRERGLIEAlkeaiaSGKPFLGICLGMQLLF 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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