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Conserved domains on  [gi|21361331|ref|NP_001866|]
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carbamoyl-phosphate synthase [ammonia], mitochondrial isoform b precursor [Homo sapiens]

Protein Classification

carbamoyl-phosphate synthase( domain architecture ID 12854909)

carbamoylphosphate synthetase (CPS) catalyzes the formation of carbamoylphosphate from C02, ATP, and ammonia or glutamine, for pyrimidine biosynthesis, arginine biosynthesis, or the urea cycle

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSaseII_lrg super family cl36884
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 419-1477 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]


The actual alignment was detected with superfamily member TIGR01369:

Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 1531.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    419 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEvglKQADTVYFLPITPQFVTEVIKA 498
Cdd:TIGR01369    3 RTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDP---EMADKVYIEPLTPEAVEKIIEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    499 EQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAAD 578
Cdd:TIGR01369   80 ERPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    579 TIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAMT--NQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAM 656
Cdd:TIGR01369  160 EIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPM 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    657 GVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAF 736
Cdd:TIGR01369  240 GVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    737 IAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMC 816
Cdd:TIGR01369  320 VAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSL 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    817 HPSIEGFtpRLPMNKEWPsNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNS 896
Cdd:TIGR01369  400 EIGATGF--DLPDREVEP-DEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKL 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    897 ESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDVNF-DDHG 975
Cdd:TIGR01369  477 TDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKK 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    976 MMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGCIIS 1055
Cdd:TIGR01369  557 VLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1056 VGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLS 1135
Cdd:TIGR01369  637 FGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLG 716

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1136 GSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAGVHSGDATLMLPTQTI 1215
Cdd:TIGR01369  717 GRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTL 796

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1216 SQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDEkhLPT 1295
Cdd:TIGR01369  797 SAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEE--LGV 874

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1296 LDHPiiPADYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQSFRPRF 1374
Cdd:TIGR01369  875 GKEK--EPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGsVLLSVRDKDKEEL 952

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1375 LGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRR 1454
Cdd:TIGR01369  953 LDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPN-----ILDLIKNGEIELVINTTSKGAGTATDGYKIRR 1027

                         1050      1060
                   ....*....|....*....|...
gi 21361331   1455 TAVDSGIPLLTNFQVTKLFAEAV 1477
Cdd:TIGR01369 1028 EALDYGVPLITTLNTAEAFAEAL 1050
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 46-400 3.38e-176

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: 529.89  E-value: 3.38e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331     46 AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTAldelglskylESNG 125
Cdd:TIGR01368    1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDA----------ESKG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    126 IKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVDF------VDPNKQ- 198
Cdd:TIGR01368   71 IHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEElvekarVSPDITg 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    199 -NLIAEVSTKDVKVYGK--GNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFT---KMEYDGILIAGGPGNPALAE 272
Cdd:TIGR01368  151 iNLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEeikKYNPDGIFLSNGPGDPAAVE 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    273 PLIQNVRKILEsdrKEPLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDN-TLPAG-WK 350
Cdd:TIGR01368  231 PAIETIRKLLE---KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPdSLPAGdLE 307

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 21361331    351 PLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKK 400
Cdd:TIGR01368  308 VTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 419-1477 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: 1531.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    419 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEvglKQADTVYFLPITPQFVTEVIKA 498
Cdd:TIGR01369    3 RTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDP---EMADKVYIEPLTPEAVEKIIEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    499 EQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAAD 578
Cdd:TIGR01369   80 ERPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    579 TIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAMT--NQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAM 656
Cdd:TIGR01369  160 EIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPM 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    657 GVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAF 736
Cdd:TIGR01369  240 GVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    737 IAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMC 816
Cdd:TIGR01369  320 VAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSL 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    817 HPSIEGFtpRLPMNKEWPsNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNS 896
Cdd:TIGR01369  400 EIGATGF--DLPDREVEP-DEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKL 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    897 ESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDVNF-DDHG 975
Cdd:TIGR01369  477 TDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKK 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    976 MMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGCIIS 1055
Cdd:TIGR01369  557 VLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1056 VGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLS 1135
Cdd:TIGR01369  637 FGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLG 716

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1136 GSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAGVHSGDATLMLPTQTI 1215
Cdd:TIGR01369  717 GRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTL 796

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1216 SQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDEkhLPT 1295
Cdd:TIGR01369  797 SAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEE--LGV 874

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1296 LDHPiiPADYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQSFRPRF 1374
Cdd:TIGR01369  875 GKEK--EPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGsVLLSVRDKDKEEL 952

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1375 LGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRR 1454
Cdd:TIGR01369  953 LDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPN-----ILDLIKNGEIELVINTTSKGAGTATDGYKIRR 1027

                         1050      1060
                   ....*....|....*....|...
gi 21361331   1455 TAVDSGIPLLTNFQVTKLFAEAV 1477
Cdd:TIGR01369 1028 EALDYGVPLITTLNTAEAFAEAL 1050
carB PRK05294
carbamoyl-phosphate synthase large subunit;
419-1491 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1419.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   419 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTN-EVglkqADTVYFLPITPQFVTEVIK 497
Cdd:PRK05294    4 RTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDpEM----ADATYIEPITPEFVEKIIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   498 AEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAA 577
Cdd:PRK05294   80 KERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   578 DTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAM--TNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDA 655
Cdd:PRK05294  160 EEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   656 MGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIV-GECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPL 734
Cdd:PRK05294  240 MGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPI 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   735 AFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALR 814
Cdd:PRK05294  320 AKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALR 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   815 MCHPSIEGFTPRL--PMNKEwpsnlDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLK 892
Cdd:PRK05294  400 SLEIGVTGLDEDLfeEESLE-----ELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELK 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   893 GlNSESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDVNFD 972
Cdd:PRK05294  475 E-NGLPLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSD 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   973 DHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGC 1052
Cdd:PRK05294  554 RKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGV 633

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1053 IISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSY 1132
Cdd:PRK05294  634 IVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSY 713

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1133 VLSGSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAV--GKDgrVISHAISEHVEDAGVHSGDATLML 1210
Cdd:PRK05294  714 VLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAIcdGED--VLIGGIMEHIEEAGVHSGDSACSL 791

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1211 PTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDE 1290
Cdd:PRK05294  792 PPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAE 871

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1291 KHLPTldhPIIPaDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQS 1369
Cdd:PRK05294  872 LGYTK---GLIP-PYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGtVFLSVRDR 947

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1370 FRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKfVHDN 1449
Cdd:PRK05294  948 DKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPH-----IVDLIKNGEIDLVINTPTGRQA-IRDG 1021

                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....
gi 21361331  1450 YVIRRTAVDSGIPLLTNFQVTKLFAEAVQ--KSRKVDSKSLFHY 1491
Cdd:PRK05294 1022 FSIRRAALEYKVPYITTLAGARAAVKAIEalKFGELEVRSLQEY 1065
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 428-962 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: 616.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  428 LGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQT-NEVglkqADTVYFLPITPQFVTEVIKAEQPDGLIL 506
Cdd:COG0458    1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTdYDT----ADRLYFEPLTVEDVLDIIEKEKPDGVIV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  507 GMGGQTALNCGVELFKRGVLKeyGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMI 586
Cdd:COG0458   77 QFGGQTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  587 RSAYALGGLGSGICPNRETLMDLSTKAFA--MTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHTGDSV 664
Cdd:COG0458  155 RPSYVLGGRGMGIVYNEEELEEYLERALKvsPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  665 VVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHptSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALG 744
Cdd:COG0458  235 CVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALG 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  745 IPLPEIKNVVSgktsacFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIegft 824
Cdd:COG0458  313 YTLDELGNDTG------FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGL---- 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  825 PRLPMNKEWPSNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGlnsESMTEETL 904
Cdd:COG0458  383 PGTVLLSLVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEE---IILVINTL 459

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21361331  905 KRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTY 962
Cdd:COG0458  460 LGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTY 517
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 46-400 3.38e-176

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: 529.89  E-value: 3.38e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331     46 AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTAldelglskylESNG 125
Cdd:TIGR01368    1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDA----------ESKG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    126 IKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVDF------VDPNKQ- 198
Cdd:TIGR01368   71 IHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEElvekarVSPDITg 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    199 -NLIAEVSTKDVKVYGK--GNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFT---KMEYDGILIAGGPGNPALAE 272
Cdd:TIGR01368  151 iNLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEeikKYNPDGIFLSNGPGDPAAVE 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    273 PLIQNVRKILEsdrKEPLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDN-TLPAG-WK 350
Cdd:TIGR01368  231 PAIETIRKLLE---KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPdSLPAGdLE 307

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 21361331    351 PLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKK 400
Cdd:TIGR01368  308 VTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
44-398 2.01e-143

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 443.36  E-value: 2.01e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    44 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTtalDElglskylES 123
Cdd:PRK12564    3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---DF-------ES 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   124 NGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI--------EFEGQPVDFVDP 195
Cdd:PRK12564   73 DRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIatedfdaeELLEKARAFPGL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   196 NKQNLIAEVSTKDVKVYGKGNPT---KVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTKMEYDGILIAGGPGNPA 269
Cdd:PRK12564  153 LGLDLVKEVSTKEPYPWPGPGGElkyKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   270 LAEPLIQNVRKILESDRkePLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPAG 348
Cdd:PRK12564  233 ALDYAIEMIRELLEKKI--PIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDeDSLPAN 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 21361331   349 WKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLI 398
Cdd:PRK12564  311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 44-399 2.21e-137

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: 427.13  E-value: 2.21e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   44 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTtalDElglskylES 123
Cdd:COG0505    3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDE---DF-------ES 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  124 NGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVD--------FVDP 195
Cdd:COG0505   73 DRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEellekaraAPGM 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  196 NKQNLIAEVSTKDVKVYG--KGNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTKMEYDGILIAGGPGNPAL 270
Cdd:COG0505  153 EGLDLVKEVSTKEPYEWTeaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATtsaEEILALNPDGVFLSNGPGDPAA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  271 AEPLIQNVRKILESDRkePLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPA-G 348
Cdd:COG0505  233 LDYAIETIRELLGKGI--PIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDeDSLPAtD 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21361331  349 WKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIK 399
Cdd:COG0505  311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 546-748 5.06e-104

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: 330.04  E-value: 5.06e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    546 DRQLFSDKLNEINEKIAPSFA--VESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAMT------ 617
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    618 NQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMgvHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGEC 697
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 21361331    698 NIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLP 748
Cdd:pfam02786  159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 220-395 8.69e-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: 308.27  E-value: 8.69e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  220 VVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDF---TKMEYDGILIAGGPGNPALAEPLIQNVRKILESdrKEPLFGISTG 296
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAeeiLKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGK--KIPIFGICLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  297 NLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPAGWKPLFVNVNDQTNEGIMHESKPFFAVQ 375
Cdd:cd01744   79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDpDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158

                        170       180
                 ....*....|....*....|
gi 21361331  376 FHPEVTPGPIDTEYLFDSFF 395
Cdd:cd01744  159 FHPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 48-183 3.67e-64

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: 213.34  E-value: 3.67e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331     48 IVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDttaldelglsKYLESNGIK 127
Cdd:pfam00988    1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNP----------EDFESDKIH 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 21361331    128 VSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI 183
Cdd:pfam00988   71 VAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 44-183 3.29e-63

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: 211.08  E-value: 3.29e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331      44 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDttaldelglsKYLES 123
Cdd:smart01097    1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVND----------EDFES 70

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331     124 NGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI 183
Cdd:smart01097   71 DKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 839-962 5.36e-55

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: 187.27  E-value: 5.36e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331     839 LRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNSESMTEETLKRAKEIGFSDKQIS 918
Cdd:smart01096    1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 21361331     919 KCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTY 962
Cdd:smart01096   81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
MGS_CPS_I_III cd01423
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ...
 1360-1475 1.74e-49

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: 170.94  E-value: 1.74e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1360 KGILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSlSSIRKLIRDGSIDLVINLP 1439
Cdd:cd01423    1 KGILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK-PSLRELLAEGKIDLVINLP 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 21361331 1440 NNNTKFVHDN-YVIRRTAVDSGIPLLTNFQVTKLFAE 1475
Cdd:cd01423   80 SNRGKRVLDNdYVMRRAADDFAVPLITNPKCAKLFIE 116
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 419-1477 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: 1531.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    419 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEvglKQADTVYFLPITPQFVTEVIKA 498
Cdd:TIGR01369    3 RTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDP---EMADKVYIEPLTPEAVEKIIEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    499 EQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAAD 578
Cdd:TIGR01369   80 ERPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    579 TIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAMT--NQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAM 656
Cdd:TIGR01369  160 EIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPM 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    657 GVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAF 736
Cdd:TIGR01369  240 GVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    737 IAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMC 816
Cdd:TIGR01369  320 VAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSL 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    817 HPSIEGFtpRLPMNKEWPsNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNS 896
Cdd:TIGR01369  400 EIGATGF--DLPDREVEP-DEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKL 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    897 ESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDVNF-DDHG 975
Cdd:TIGR01369  477 TDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKK 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    976 MMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGCIIS 1055
Cdd:TIGR01369  557 VLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1056 VGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLS 1135
Cdd:TIGR01369  637 FGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLG 716

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1136 GSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAGVHSGDATLMLPTQTI 1215
Cdd:TIGR01369  717 GRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTL 796

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1216 SQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDEkhLPT 1295
Cdd:TIGR01369  797 SAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEE--LGV 874

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1296 LDHPiiPADYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQSFRPRF 1374
Cdd:TIGR01369  875 GKEK--EPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGsVLLSVRDKDKEEL 952

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1375 LGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRR 1454
Cdd:TIGR01369  953 LDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPN-----ILDLIKNGEIELVINTTSKGAGTATDGYKIRR 1027

                         1050      1060
                   ....*....|....*....|...
gi 21361331   1455 TAVDSGIPLLTNFQVTKLFAEAV 1477
Cdd:TIGR01369 1028 EALDYGVPLITTLNTAEAFAEAL 1050
carB PRK05294
carbamoyl-phosphate synthase large subunit;
419-1491 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1419.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   419 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTN-EVglkqADTVYFLPITPQFVTEVIK 497
Cdd:PRK05294    4 RTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDpEM----ADATYIEPITPEFVEKIIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   498 AEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAA 577
Cdd:PRK05294   80 KERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   578 DTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAM--TNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDA 655
Cdd:PRK05294  160 EEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   656 MGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIV-GECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPL 734
Cdd:PRK05294  240 MGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPI 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   735 AFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALR 814
Cdd:PRK05294  320 AKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALR 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   815 MCHPSIEGFTPRL--PMNKEwpsnlDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLK 892
Cdd:PRK05294  400 SLEIGVTGLDEDLfeEESLE-----ELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELK 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   893 GlNSESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDVNFD 972
Cdd:PRK05294  475 E-NGLPLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSD 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   973 DHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGC 1052
Cdd:PRK05294  554 RKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGV 633

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1053 IISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSY 1132
Cdd:PRK05294  634 IVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSY 713

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1133 VLSGSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAV--GKDgrVISHAISEHVEDAGVHSGDATLML 1210
Cdd:PRK05294  714 VLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAIcdGED--VLIGGIMEHIEEAGVHSGDSACSL 791

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1211 PTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDE 1290
Cdd:PRK05294  792 PPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAE 871

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1291 KHLPTldhPIIPaDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQS 1369
Cdd:PRK05294  872 LGYTK---GLIP-PYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGtVFLSVRDR 947

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1370 FRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKfVHDN 1449
Cdd:PRK05294  948 DKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPH-----IVDLIKNGEIDLVINTPTGRQA-IRDG 1021

                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....
gi 21361331  1450 YVIRRTAVDSGIPLLTNFQVTKLFAEAVQ--KSRKVDSKSLFHY 1491
Cdd:PRK05294 1022 FSIRRAALEYKVPYITTLAGARAAVKAIEalKFGELEVRSLQEY 1065
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 419-1478 0e+00

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 1106.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   419 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEvglKQADTVYFLPITPQFVTEVIKA 498
Cdd:PRK12815    4 DTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDP---APADTVYFEPLTVEFVKRIIAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   499 EQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAAD 578
Cdd:PRK12815   81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   579 TIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFA--MTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAM 656
Cdd:PRK12815  161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQasPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   657 GVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAF 736
Cdd:PRK12815  241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   737 IAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRmc 816
Cdd:PRK12815  321 IAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALR-- 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   817 hpSIEGFTP--RLPMNKEWPSNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGl 894
Cdd:PRK12815  399 --SLEIKRNglSLPIELSGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAE- 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   895 NSESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQ-EHDVNFDD 973
Cdd:PRK12815  476 DGLDLSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGEsEAEPSSEK 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   974 HGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGCI 1053
Cdd:PRK12815  556 KKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVI 635

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1054 ISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYV 1133
Cdd:PRK12815  636 VQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYV 715

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1134 LSGSAMNVVFSEDEMKKFLEEAtrVSQEHPVVLTKFVEGArEVEMDAVgKDGRVISHA-ISEHVEDAGVHSGDATLMLPT 1212
Cdd:PRK12815  716 IGGQGMAVVYDEPALEAYLAEN--ASQLYPILIDQFIDGK-EYEVDAI-SDGEDVTIPgIIEHIEQAGVHSGDSIAVLPP 791

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1213 QTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDEKH 1292
Cdd:PRK12815  792 QSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELG 871

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1293 LPTLDHPIipADYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQSFR 1371
Cdd:PRK12815  872 YPNGLWPG--SPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGtIFISVRDEDK 949

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1372 PRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAwPSQEGQNPSLSsirklIRDGSIDLVINLPNNNTKFVHDNYV 1451
Cdd:PRK12815  950 PEVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVE-KVQEGSPSLLE-----RIKQHRIVLVVNTSLSDSASEDAIK 1023

                        1050      1060
                  ....*....|....*....|....*..
gi 21361331  1452 IRRTAVDSGIPLLTNFQVTKLFAEAVQ 1478
Cdd:PRK12815 1024 IRDEALSTHIPVFTELETAQAFLQVLE 1050
PLN02735 PLN02735
carbamoyl-phosphate synthase
 403-1481 0e+00

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 902.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   403 ATTITSVLPKPALVASRVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEvglKQADTV 482
Cdd:PLN02735    4 ADTVTRAWSAATKAGKRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDP---ETADRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   483 YFLPITPQFVTEVIKAEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIA 562
Cdd:PLN02735   81 YIAPMTPELVEQVIAKERPDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   563 PSFAVESIEDALKAADTIG-YPVMIRSAYALGGLGSGICPNRETLMDLSTKAFA--MTNQILVEKSVTGWKEIEYEVVRD 639
Cdd:PLN02735  161 PSGIATTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAasITSQVLVEKSLLGWKEYELEVMRD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   640 ADDNCVTVCNMENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIvgEC---NIQFALHPTSMEYCIIEVN 716
Cdd:PLN02735  241 LADNVVIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   717 ARLSRSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVG 796
Cdd:PLN02735  319 PRVSRSSALASKATGFPIAKMAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVG 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   797 EVMAIGRTFEESFQKALRMCHPSIEGFTPrlPMNKEWPSNLD-LRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDK 875
Cdd:PLN02735  399 EAMALGRTFQESFQKALRSLETGFSGWGC--AKVKELDWDWEqLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDP 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   876 WFLYKMRDILNMEKTLKGLNSESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVT 955
Cdd:PLN02735  477 WFLTQLKELVDVEQFLKSRSLSELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANT 556

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   956 NYLYVTYNGQEHDVNFDDHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEEL 1035
Cdd:PLN02735  557 PYMYSSYDGECESAPTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPL 636

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1036 SLERILDIYHQEACGGCIISVGGQIPNNLAVPLYK------------NG-VKIMGTSPLQIDRAEDRSIFSAVLDELKVA 1102
Cdd:PLN02735  637 TVEDVLNVIDLERPDGIIVQFGGQTPLKLALPIQKyldknpppsasgNGnVKIWGTSPDSIDAAEDRERFNAILNELKIE 716

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1103 QAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVG 1182
Cdd:PLN02735  717 QPKGGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALA 796

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1183 -KDGRVISHAISEHVEDAGVHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLV-KGNDVLVIECNLRA 1260
Cdd:PLN02735  797 dSEGNVVIGGIMEHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRA 876

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1261 SRSFPFVSKTLGVDFIDVATKVMIGenvdeKHLPTLD--HPIIPAdYVAIKAPMFSWPRLRDADPILRCEMASTGEVACF 1338
Cdd:PLN02735  877 SRTVPFVSKAIGHPLAKYASLVMSG-----KSLKDLGftEEVIPA-HVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGI 950

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1339 GEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAwPSQEGQn 1417
Cdd:PLN02735  951 DYEFSKAFAKAQIAAGQRLPLSGtVFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVL-KLHEGR- 1028

                        1050      1060      1070      1080      1090      1100
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361331  1418 pslSSIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRRTAVDSGIPLLTNFQVTKLFAEAVQKSR 1481
Cdd:PLN02735 1029 ---PHAGDMLANGQIQLMVITSSGDALDQKDGRQLRRMALAYKVPIITTVAGALATAQAVKSLK 1089
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 428-962 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: 616.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  428 LGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQT-NEVglkqADTVYFLPITPQFVTEVIKAEQPDGLIL 506
Cdd:COG0458    1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTdYDT----ADRLYFEPLTVEDVLDIIEKEKPDGVIV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  507 GMGGQTALNCGVELFKRGVLKeyGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMI 586
Cdd:COG0458   77 QFGGQTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  587 RSAYALGGLGSGICPNRETLMDLSTKAFA--MTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHTGDSV 664
Cdd:COG0458  155 RPSYVLGGRGMGIVYNEEELEEYLERALKvsPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  665 VVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHptSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALG 744
Cdd:COG0458  235 CVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALG 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  745 IPLPEIKNVVSgktsacFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIegft 824
Cdd:COG0458  313 YTLDELGNDTG------FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGL---- 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  825 PRLPMNKEWPSNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGlnsESMTEETL 904
Cdd:COG0458  383 PGTVLLSLVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEE---IILVINTL 459

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21361331  905 KRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTY 962
Cdd:COG0458  460 LGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTY 517
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 979-1495 9.86e-178

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: 541.01  E-value: 9.86e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  979 LGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGCIISVGG 1058
Cdd:COG0458    1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1059 QIPNNLAVPLYKN----GVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVL 1134
Cdd:COG0458   81 QTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1135 SGSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVG-KDGRVISHAISEHVEDAGVHSGDATLMLPTQ 1213
Cdd:COG0458  161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRdGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1214 TISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDEKHL 1293
Cdd:COG0458  241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1294 PTLDHPIIpaDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPR 1373
Cdd:COG0458  321 DTGFEPTL--DYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLLSLVADDDKEE 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1374 FLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKFVHDNYVIR 1453
Cdd:COG0458  399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPI-----IVDEIELEEIILVINTLLGAKSLGDSDGIIR 473

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 21361331 1454 RTAVDSGIPLLTNFQVTK-LFAEAVQKSRKVDSKSLFHYRQYS 1495
Cdd:COG0458  474 RALAAKVPYVTTLAAAAAaALAIKAVETEAGEFEEATAYYYST 516
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 46-400 3.38e-176

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: 529.89  E-value: 3.38e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331     46 AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTAldelglskylESNG 125
Cdd:TIGR01368    1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDA----------ESKG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    126 IKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVDF------VDPNKQ- 198
Cdd:TIGR01368   71 IHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEElvekarVSPDITg 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    199 -NLIAEVSTKDVKVYGK--GNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFT---KMEYDGILIAGGPGNPALAE 272
Cdd:TIGR01368  151 iNLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEeikKYNPDGIFLSNGPGDPAAVE 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    273 PLIQNVRKILEsdrKEPLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDN-TLPAG-WK 350
Cdd:TIGR01368  231 PAIETIRKLLE---KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPdSLPAGdLE 307

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 21361331    351 PLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKK 400
Cdd:TIGR01368  308 VTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
44-398 2.01e-143

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 443.36  E-value: 2.01e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    44 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTtalDElglskylES 123
Cdd:PRK12564    3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---DF-------ES 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   124 NGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI--------EFEGQPVDFVDP 195
Cdd:PRK12564   73 DRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIatedfdaeELLEKARAFPGL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   196 NKQNLIAEVSTKDVKVYGKGNPT---KVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTKMEYDGILIAGGPGNPA 269
Cdd:PRK12564  153 LGLDLVKEVSTKEPYPWPGPGGElkyKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   270 LAEPLIQNVRKILESDRkePLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPAG 348
Cdd:PRK12564  233 ALDYAIEMIRELLEKKI--PIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDeDSLPAN 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 21361331   349 WKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLI 398
Cdd:PRK12564  311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 44-399 2.21e-137

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: 427.13  E-value: 2.21e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   44 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTtalDElglskylES 123
Cdd:COG0505    3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDE---DF-------ES 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  124 NGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVD--------FVDP 195
Cdd:COG0505   73 DRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEellekaraAPGM 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  196 NKQNLIAEVSTKDVKVYG--KGNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTKMEYDGILIAGGPGNPAL 270
Cdd:COG0505  153 EGLDLVKEVSTKEPYEWTeaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATtsaEEILALNPDGVFLSNGPGDPAA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  271 AEPLIQNVRKILESDRkePLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPA-G 348
Cdd:COG0505  233 LDYAIETIRELLGKGI--PIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDeDSLPAtD 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21361331  349 WKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIK 399
Cdd:COG0505  311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 46-402 2.15e-107

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 345.34  E-value: 2.15e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    46 AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDttaldelglsKYLESNG 125
Cdd:PRK12838    3 AYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINA----------DDYESKQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   126 IKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI------EFEGQPVDFVDPnkQN 199
Cdd:PRK12838   73 PQVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASItttddaHAFDQIKALVLP--KN 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   200 LIAEVSTKDVKVYGKGNPTkVVAVDCGIKNNVIRLLVKRGAEVHLVPWNhdfTKMEY------DGILIAGGPGNPALAEP 273
Cdd:PRK12838  151 VVAQVSTKEPYTYGNGGKH-VALIDFGYKKSILRSLSKRGCKVTVLPYD---TSLEEiknlnpDGIVLSNGPGDPKELQP 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   274 LIQNVRKILESdrkEPLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYAL--DNTLPAGWKP 351
Cdd:PRK12838  227 YLPEIKKLISS---YPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVdeDSLDGTPLSV 303

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21361331   352 LFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKKGK 402
Cdd:PRK12838  304 RFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKAR 354
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 546-748 5.06e-104

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: 330.04  E-value: 5.06e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    546 DRQLFSDKLNEINEKIAPSFA--VESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAMT------ 617
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    618 NQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMgvHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGEC 697
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 21361331    698 NIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLP 748
Cdd:pfam02786  159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 220-395 8.69e-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: 308.27  E-value: 8.69e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  220 VVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDF---TKMEYDGILIAGGPGNPALAEPLIQNVRKILESdrKEPLFGISTG 296
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAeeiLKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGK--KIPIFGICLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  297 NLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPAGWKPLFVNVNDQTNEGIMHESKPFFAVQ 375
Cdd:cd01744   79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDpDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158

                        170       180
                 ....*....|....*....|
gi 21361331  376 FHPEVTPGPIDTEYLFDSFF 395
Cdd:cd01744  159 FHPEASPGPHDTEYLFDEFL 178
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 46-402 2.08e-81

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 273.21  E-value: 2.08e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    46 AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGapdtTALDElglskyLESNG 125
Cdd:CHL00197    7 AILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTG----INLED------IESVK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   126 IKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVDFVDPNKQ------- 198
Cdd:CHL00197   77 IQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSYLRAKIKesphmps 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   199 -NLIAEVSTKDVKVYGK----------------GNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTKMEY---DG 258
Cdd:CHL00197  157 sDLIPRVTTSSYYEWDEkshpsfyladnkrphsSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSyqpDG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   259 ILIAGGPGNPALAEPLIQNVRKILesDRKEPLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLniTNKQAFITAQNHG 338
Cdd:CHL00197  237 ILLSNGPGDPSAIHYGIKTVKKLL--KYNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSG--LNQQVEITSQNHG 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361331   339 YALDntLPAGWKPLF----VNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKKGK 402
Cdd:CHL00197  313 FAVN--LESLAKNKFyithFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSK 378
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 16-391 6.97e-69

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 238.34  E-value: 6.97e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    16 TGFGFTNVTAHQKWKFSRPGIRLLSVKAQT-------------------AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTG 76
Cdd:PLN02771    8 LGFVLPTSLSSQPSFDRRGGVRVSVIRCSSspltsdgagvverpwktsdARLVLEDGSVWKAKSFGARGTQVGEVVFNTS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    77 LGGYPEAITDPAYKGQILTMANPIIGNGGA-PDttalDElglskylESNGIKVSGLLVLDYSKDYNHWLATKSLGQWLQE 155
Cdd:PLN02771   88 LTGYQEILTDPSYAGQFVLMTNPHIGNTGVnFD----DE-------ESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   156 EKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVD--------FVDPNKQNLIAEVSTK-------------DVKVYGK 214
Cdd:PLN02771  157 RNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDeellkmsrSWDIVGIDLISGVSCKspyewvdktnpewDFNTNSR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   215 -GNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTKMEYDGILIAGGPGNPALAEPLIQNVRKILEsdrKEPL 290
Cdd:PLN02771  237 dGESYHVIAYDFGIKHNILRRLASYGCKITVVPSTwpaSEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLG---KVPV 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   291 FGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPAGWKPLFVNVNDQTNEGIMHESK 369
Cdd:PLN02771  314 FGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDpASLPEGVEVTHVNLNDGSCAGLAFPAL 393

                         410       420
                  ....*....|....*....|..
gi 21361331   370 PFFAVQFHPEVTPGPIDTEYLF 391
Cdd:PLN02771  394 NVMSLQYHPEASPGPHDSDNAF 415
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 48-183 3.67e-64

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: 213.34  E-value: 3.67e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331     48 IVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDttaldelglsKYLESNGIK 127
Cdd:pfam00988    1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNP----------EDFESDKIH 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 21361331    128 VSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI 183
Cdd:pfam00988   71 VAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 44-183 3.29e-63

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: 211.08  E-value: 3.29e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331      44 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDttaldelglsKYLES 123
Cdd:smart01097    1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVND----------EDFES 70

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331     124 NGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI 183
Cdd:smart01097   71 DKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 839-962 5.36e-55

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: 187.27  E-value: 5.36e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331     839 LRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNSESMTEETLKRAKEIGFSDKQIS 918
Cdd:smart01096    1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 21361331     919 KCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTY 962
Cdd:smart01096   81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
GATase pfam00117
Glutamine amidotransferase class-I;
221-395 6.39e-55

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 189.76  E-value: 6.39e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    221 VAVDCG--IKNNVIRLLVKRGAEVHLVPWNHDFT---KMEYDGILIAGGPGNPALAEPLIQNVRKILEsdRKEPLFGIST 295
Cdd:pfam00117    1 LLIDNGdsFTYNLARALRELGVEVTVVPNDTPAEeilEENPDGIILSGGPGSPGAAGGAIEAIREARE--LKIPILGICL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    296 GNLITGLAAGAKTYKMSM-ANRGQNQPVLNITN------KQAFITAQNHGYALDN-TLPAGWKPLFVNVNDQTNEGIMHE 367
Cdd:pfam00117   79 GHQLLALAFGGKVVKAKKfGHHGKNSPVGDDGCglfyglPNVFIVRRYHSYAVDPdTLPDGLEVTATSENDGTIMGIRHK 158

                          170       180
                   ....*....|....*....|....*...
gi 21361331    368 SKPFFAVQFHPEVTPGPIDTEYLFDSFF 395
Cdd:pfam00117  159 KLPIFGVQFHPESILTPHGPEILFNFFI 186
MGS_CPS_I_III cd01423
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ...
 1360-1475 1.74e-49

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: 170.94  E-value: 1.74e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1360 KGILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSlSSIRKLIRDGSIDLVINLP 1439
Cdd:cd01423    1 KGILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK-PSLRELLAEGKIDLVINLP 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 21361331 1440 NNNTKFVHDN-YVIRRTAVDSGIPLLTNFQVTKLFAE 1475
Cdd:cd01423   80 SNRGKRVLDNdYVMRRAADDFAVPLITNPKCAKLFIE 116
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
 841-919 5.25e-30

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: 114.01  E-value: 5.25e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361331    841 KELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGlNSESMTEETLKRAKEIGFSDKQISK 919
Cdd:pfam02787    1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKE-AGLDLDAELLREAKRLGFSDRQIAK 78
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 1088-1289 1.23e-27

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: 112.01  E-value: 1.23e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1088 DRSIFSAVLDELKVAQAPWKA--VNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVS----QE 1161
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafGN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1162 HPVVLTKFVEGAREVEMDAVG-KDGRVIsHAISEHVEDAgVHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPF 1240
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRdAHGNCI-TVCNRECSDQ-RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 21361331   1241 NVQFLV--KGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVD 1289
Cdd:pfam02786  159 TVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 1373-1465 7.33e-25

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: 99.87  E-value: 7.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1373 RFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPNNNTKFVHDNYVI 1452
Cdd:pfam02142    1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEGRPGGRVQIGDLIKNGEIDLVINTLYPFKATVHDGYAI 80

                           90
                   ....*....|...
gi 21361331   1453 RRTAVDSGIPLLT 1465
Cdd:pfam02142   81 RRAAENIDIPGPT 93
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 1077-1286 1.05e-22

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: 99.56  E-value: 1.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1077 GTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYvLSGSA-MNVVFSEDEMKKFLE-- 1153
Cdd:COG0439   43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPAD-GAGSRgVRVVRDEEELEAALAea 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1154 --EATRVSQEHPVVLTKFVEGaREVEMDAVGKDGRVISHAISEHVEDA--GVHSGDatlMLPTQtISQGAIEKVKDATRK 1229
Cdd:COG0439  122 raEAKAGSPNGEVLVEEFLEG-REYSVEGLVRDGEVVVCSITRKHQKPpyFVELGH---EAPSP-LPEELRAEIGELVAR 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361331 1230 IAKAFAIS-GPFNVQFLVKGNDVLV-IECNLRAS--RSFPFVSKTLGVDFIDVATKVMIGE 1286
Cdd:COG0439  197 ALRALGYRrGAFHTEFLLTPDGEPYlIEINARLGgeHIPPLTELATGVDLVREQIRLALGE 257
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 535-746 1.27e-16

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: 81.46  E-value: 1.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  535 GTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLmdlsTKAF 614
Cdd:COG0439   43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEL----EAAL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  615 AMTNQ----------ILVEKSVTGwKEIEYEVVrdADDNCVTVCNM---ENVDAMGVHTGDsvvVAPAQtLSNAEFQMLR 681
Cdd:COG0439  119 AEARAeakagspngeVLVEEFLEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIG 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361331  682 RTSINVVRHLGIV-GECNIQFALHPtSMEYCIIEVNARLS--RSSALASKATGYPLAFIAAKIALGIP 746
Cdd:COG0439  192 ELVARALRALGYRrGAFHTEFLLTP-DGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
MGS_CPS_II cd01424
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ...
 1371-1466 5.58e-16

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: 75.21  E-value: 5.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1371 RPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNtKFVHDNY 1450
Cdd:cd01424   12 KPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPN-----IVDLIKNGEIQLVINTPSGK-RAIRDGF 85

                         90
                 ....*....|....*.
gi 21361331 1451 VIRRTAVDSGIPLLTN 1466
Cdd:cd01424   86 SIRRAALEYKVPYFTT 101
MGS smart00851
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 1373-1465 1.11e-15

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: 73.66  E-value: 1.11e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    1373 RFLGVAEQLHNEGFKLFATEATSDWLNANNVP--ATPVAWPSqEGQNpslsSIRKLIRDGSIDLVINLPNNNTK-FVHDN 1449
Cdd:smart00851    1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPvvKTLHPKVH-GGIP----QILDLIKNGEIDLVINTLYPFEAqAHEDG 75

                            90
                    ....*....|....*.
gi 21361331    1450 YVIRRTAVDSGIPLLT 1465
Cdd:smart00851   76 YSIRRAAENIDIPGPT 91
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 424-750 1.26e-12

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 70.68  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   424 KVLILGSGGlsigqagefdysGSQAVKAMKEE----NVKTVLMNPNIAsvqtnevGLKQADTVYFLP-ITP----QFVTE 494
Cdd:PRK12767    3 NILVTSAGR------------RVQLVKALKKSllkgRVIGADISELAP-------ALYFADKFYVVPkVTDpnyiDRLLD 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   495 VIKAEQPDGLILGMGgqtalncgVELFK----RGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESI 570
Cdd:PRK12767   64 ICKKEKIDLLIPLID--------PELPLlaqnRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   571 EDALKA--ADTIGYPVMIRSAYALGGLGSGICPNRETLMDLstkaFAMTNQILVEKSVTGwKEIEYEVVRDADDNCVTVC 648
Cdd:PRK12767  136 EDFKAAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELEFL----LEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIV 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   649 NMENVDAMGVHTGDSVVVapaqtlsnaEFQMLRRTSINVVRHLGIVGECNIQFALhpTSMEYCIIEVNARLSRSSALASK 728
Cdd:PRK12767  211 PRKRIEVRAGETSKGVTV---------KDPELFKLAERLAEALGARGPLNIQCFV--TDGEPYLFEINPRFGGGYPLSYM 279

                         330       340
                  ....*....|....*....|...
gi 21361331   729 ATG-YPlAFIAAKIALGIPLPEI 750
Cdd:PRK12767  280 AGAnEP-DWIIRNLLGGENEPII 301
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 563-832 1.15e-11

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 68.90  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   563 PSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLmdlsTKAFAMTNQ----------ILVEKSVTGWKEI 632
Cdd:PRK06111  134 ITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQEL----TKAFESNKKraanffgngeMYIEKYIEDPRHI 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   633 EYEVVRDADDNCvtvcnmenvdamgVHTGD---SV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQF 701
Cdd:PRK06111  210 EIQLLADTHGNT-------------VYLWErecSVqrrhqkVIeeAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEF 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   702 ALHPTSMEYcIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLP----EIKnvVSGKTSAC---------FEPSldy 768
Cdd:PRK06111  277 LVDEQKNFY-FLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSftqdDIK--RSGHAIEVriyaedpktFFPS--- 350

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361331   769 mVTKIPRWDLDRfhGTSSRIGSSMKS-----------VGEVMAIGRTFEESFQK---ALRMCHpsIEGFTPRLPMNKE 832
Cdd:PRK06111  351 -PGKITDLTLPG--GEGVRHDHAVENgvtvtpfydpmIAKLIAHGETREEAISRlhdALEELK--VEGIKTNIPLLLQ 423
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 233-382 7.20e-11

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: 63.81  E-value: 7.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  233 RLLVKRGAEVH--------LVPWNHDFTkmEYDGILIAGGPGNP----ALAEPLIQNVRKILESDRkePLFGISTGNLIT 300
Cdd:COG0518   20 RRLREAGIELDvlrvyageILPYDPDLE--DPDGLILSGGPMSVydedPWLEDEPALIREAFELGK--PVLGICYGAQLL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  301 GLAAGAKTYKMSMANRGQnQPVlNITNKQA--------FITAQNHGYALDnTLPAGWKPLFVNVNDQtNEGIMHEsKPFF 372
Cdd:COG0518   96 AHALGGKVEPGPGREIGW-APV-ELTEADPlfaglpdeFTVWMSHGDTVT-ELPEGAEVLASSDNCP-NQAFRYG-RRVY 170

                        170
                 ....*....|
gi 21361331  373 AVQFHPEVTP 382
Cdd:COG0518  171 GVQFHPEVTH 180
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
528-748 1.18e-10

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 65.89  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   528 EYGVKVLGTSVESImatedRQLfSDKLNEINEKIAPSFAV--------ESIEDALKAADTIGYPVMIRSAYALGGLGSGI 599
Cdd:PRK07178   96 ERGIKFIGPSAEVI-----RRM-GDKTEARRAMIKAGVPVtpgsegnlADLDEALAEAERIGYPVMLKATSGGGGRGIRR 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   600 CPNRETL-------MDLSTKAFAMTnQILVEKSVTGWKEIEYEVVRDADDNCVTV----CNMENVDAMGVHtgdsvvVAP 668
Cdd:PRK07178  170 CNSREELeqnfprvISEATKAFGSA-EVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQRRNQKLIE------IAP 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   669 AQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYcIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLP 748
Cdd:PRK07178  243 SPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVY-FMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLS 321
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 230-379 9.99e-10

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: 59.42  E-value: 9.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    230 NVIRLLVKRGAEVHlVPWNHDFTKMEYDG-----ILIAGGPGNPALAEpliQNVRKILESDRKEPLFGISTGNLITGLAA 304
Cdd:TIGR00566   14 NLVQYFCELGAEVV-VKRNDSLTLQEIEAllpllIVISPGPCTPNEAG---ISLEAIRHFAGKLPILGVCLGHQAMGQAF 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    305 GAKtykMSMANRGQNQPVLNITNKQAFITAqnhgyALDNTLPAG-WKPLFVN---------VNDQTNE-----GIMHESK 369
Cdd:TIGR00566   90 GGD---VVRANTVMHGKTSEIEHNGAGIFR-----GLFNPLTATrYHSLVVEpetlptcfpVTAWEEEnieimAIRHRDL 161

                          170
                   ....*....|
gi 21361331    370 PFFAVQFHPE 379
Cdd:TIGR00566  162 PLEGVQFHPE 171
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 229-379 1.33e-09

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: 59.09  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  229 NNVIRLLVKRGAEVHLVPwNHDFT-----KMEYDGILIAGGPGNPALAEPLIQnVRKILESDRkePLFGISTGNLITGLA 303
Cdd:cd01743   12 YNLVQYLRELGAEVVVVR-NDEITleeleLLNPDAIVISPGPGHPEDAGISLE-IIRALAGKV--PILGVCLGHQAIAEA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  304 AGAKTYKMSMANRGQ------NQPVLNITNKQAFITAQNHGYALD-NTLPAGWKplfvnVNDQTNEG-IM---HESKPFF 372
Cdd:cd01743   88 FGGKVVRAPEPMHGKtseihhDGSGLFKGLPQPFTVGRYHSLVVDpDPLPDLLE-----VTASTEDGvIMalrHRDLPIY 162


                 ....*..
gi 21361331  373 AVQFHPE 379
Cdd:cd01743  163 GVQFHPE 169
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
490-748 4.32e-09

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 60.33  E-value: 4.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  490 QFVTEVIKAEQPDgLILGMGgqtalNCGVELF--KRGVLKEYgVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAV 567
Cdd:COG3919   66 DALLELAERHGPD-VLIPTG-----DEYVELLsrHRDELEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVL 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  568 ESIEDALKAADTIGYPVMIRSAY--------ALGGLGSGICPNRETLMDLSTKAFAMTNQILVEKSVTGWKEIEY--EVV 637
Cdd:COG3919  139 DSADDLDALAEDLGFPVVVKPADsvgydelsFPGKKKVFYVDDREELLALLRRIAAAGYELIVQEYIPGDDGEMRglTAY 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  638 RDADDNCVTVC----NMENVDAMGVHTGdsvvvapAQTLSNAEfqmLRRTSINVVRHLGIVGECNIQFALHPTSMEYCII 713
Cdd:COG3919  219 VDRDGEVVATFtgrkLRHYPPAGGNSAA-------RESVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYKLI 288

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 21361331  714 EVNARLSRSSALASKAtGYPLAFIAAKIALGIPLP 748
Cdd:COG3919  289 EINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLE 322
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
525-749 4.36e-09

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 60.53  E-value: 4.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   525 VLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSF--AVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPN 602
Cdd:PRK08462   96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   603 RETLMD--LSTKAFAMT----NQILVEKSVTGWKEIEYEVVRDADDNCVTV----CNMENvdamgvHTGDSVVVAPAQTL 672
Cdd:PRK08462  176 ESDLENlyLAAESEALSafgdGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVL 249

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361331   673 SNAEFQMLRRTSINVVRHLGIVGECNIQFaLHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLPE 749
Cdd:PRK08462  250 DEKTRERLHETAIKAAKAIGYEGAGTFEF-LLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPS 325
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 1070-1290 7.17e-08

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 56.05  E-value: 7.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1070 KNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALE--FAKSVDYPCLLRPsYVLSGSA-MNVVFSED 1146
Cdd:PRK12767   93 EIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAalAKGELQFPLFVKP-RDGSASIgVFKVNDKE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1147 EMKKFLEEATrvsqehPVVLTKFVEGaREVEMDA-VGKDGRVISHAISEHVEdagVHSGDATlmlptQTISqGAIEKVKD 1225
Cdd:PRK12767  172 ELEFLLEYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGETS-----KGVT-VKDPELFK 235

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361331  1226 ATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFvSKTLGVDFIDVATKVMIGENVDE 1290
Cdd:PRK12767  236 LAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL-SYMAGANEPDWIIRNLLGGENEP 299
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
566-719 3.66e-07

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 54.64  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  566 AVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDL--STKAFAMTN----QILVEKSVTGWKEIEYEVVRD 639
Cdd:COG4770  137 PVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAfeSARREAKAAfgddRVYLEKYIERPRHIEVQVLAD 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  640 ADDNCvtvcnmenvdamgVHTGD---SV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPtSM 708
Cdd:COG4770  217 KHGNV-------------VHLGErdcSIqrrhqkVIeeAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDA-DG 282

                        170
                 ....*....|.
gi 21361331  709 EYCIIEVNARL 719
Cdd:COG4770  283 NFYFLEMNTRL 293
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
996-1188 4.55e-07

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 54.22  E-value: 4.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   996 AVSSIRTLRQLGKKTVVVncnpetvstdFDECDK-----LYFEE-------------LSLERILDIyhQEACGGCIISVG 1057
Cdd:PRK08654   14 AIRVMRACRELGIKTVAV----------YSEADKnalfvKYADEaypigpappsksyLNIERIIDV--AKKAGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1058 -GQIPNN--LAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPW--KAVNTLNEALEFAKSVDYPCLLRPSY 1132
Cdd:PRK08654   82 yGFLAENpeFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGteEGIEDIEEAKEIAEEIGYPVIIKASA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361331  1133 VLSGSAMNVVFSEDEMKKFLEEATRVSQ----EHPVVLTKFVEGAREVEMDAVG-KDGRVI 1188
Cdd:PRK08654  162 GGGGIGMRVVYSEEELEDAIESTQSIAQsafgDSTVFIEKYLEKPRHIEIQILAdKHGNVI 222
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
566-651 8.37e-07

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 53.45  E-value: 8.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   566 AVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDL--STKAFAMTN----QILVEKSVTGWKEIEYEVVRD 639
Cdd:PRK08654  137 GIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAieSTQSIAQSAfgdsTVFIEKYLEKPRHIEIQILAD 216

                          90
                  ....*....|..
gi 21361331   640 ADDNCVTVCNME 651
Cdd:PRK08654  217 KHGNVIHLGDRE 228
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 220-296 1.50e-06

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: 47.97  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  220 VVAVDCGIKN-----NVIRLLVKRGAEVHLVPWNHDFTKME-----YDGILIAGGPGNP---ALAEPLIQNVRKILESDR 286
Cdd:cd03128    1 VAVLLFGGSEelelaSPLDALREAGAEVDVVSPDGGPVESDvdlddYDGLILPGGPGTPddlAWDEALLALLREAAAAGK 80

                         90
                 ....*....|
gi 21361331  287 kePLFGISTG 296
Cdd:cd03128   81 --PVLGICLG 88
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 220-296 1.66e-06

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: 48.36  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  220 VVAVDCGIKN-----NVIRLLVKRGAEVHLVPWNHDFTKME-----YDGILIAGGPGNP---ALAEPLIQNVRKILESDR 286
Cdd:cd01653    1 VAVLLFPGFEelelaSPLDALREAGAEVDVVSPDGGPVESDvdlddYDGLILPGGPGTPddlARDEALLALLREAAAAGK 80

                         90
                 ....*....|
gi 21361331  287 kePLFGISTG 296
Cdd:cd01653   81 --PILGICLG 88
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
1070-1288 6.10e-06

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 50.51  E-value: 6.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1070 KNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWK--AVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDE 1147
Cdd:PRK08462   99 HHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESD 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1148 MKK-FL---EEATRVSQEHPVVLTKFVEGAREVEMDAVG-KDGRVIshaisehvedagvHSGDATLMLptQTISQGAIEK 1222
Cdd:PRK08462  179 LENlYLaaeSEALSAFGDGTMYMEKFINNPRHIEVQILGdKHGNVI-------------HVGERDCSL--QRRHQKLIEE 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1223 -----VKDATR--------KIAKAFAISGPFNVQFLVKGN-DVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENV 1288
Cdd:PRK08462  244 spavvLDEKTRerlhetaiKAAKAIGYEGAGTFEFLLDSNlDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
1107-1289 6.49e-06

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 50.48  E-value: 6.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1107 KAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVSQ----EHPVVLTKFVEGAREVEMDAVG 1182
Cdd:PRK05586  136 GEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKaafgDDSMYIEKFIENPKHIEFQILG 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1183 KD-GRVIshaiseHV--EDAGVHSGDATLM--LPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLV-KGNDVLVIEC 1256
Cdd:PRK05586  216 DNyGNVV------HLgeRDCSLQRRNQKVLeeAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEM 289

                         170       180       190
                  ....*....|....*....|....*....|...
gi 21361331  1257 NLRASRSFPFVSKTLGVDFIDVATKVMIGENVD 1289
Cdd:PRK05586  290 NTRIQVEHPITEMITGVDLVKEQIKIAYGEKLS 322
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 566-719 7.99e-06

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 50.91  E-value: 7.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   566 AVESIEDALKAADTIGYPVMIRSayALGGLGSG--ICPNRETLMDLSTKAFAMTNQ------ILVEKSVTGWKEIEYEVV 637
Cdd:PRK12999  141 PIDDIEEALEFAEEIGYPIMLKA--SAGGGGRGmrIVRSEEELEEAFERAKREAKAafgndeVYLEKYVENPRHIEVQIL 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   638 RDADDNCVTV----CnmenvdamgvhtgdSV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFaLHP 705
Cdd:PRK12999  219 GDKHGNVVHLyerdC--------------SVqrrhqkVVeiAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEF-LVD 283

                         170
                  ....*....|....
gi 21361331   706 TSMEYCIIEVNARL 719
Cdd:PRK12999  284 ADGNFYFIEVNPRI 297
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 233-395 1.06e-05

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: 47.53  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  233 RLLVKR----GAEVHLVPWN---HDFTKMEYDGILIAGGPgNPALAEPLIQNVRKILESdrKEPLFGISTGN-LITgLAA 304
Cdd:cd01742   12 HLIARRvrelGVYSEILPNTtplEEIKLKNPKGIILSGGP-SSVYEEDAPRVDPEIFEL--GVPVLGICYGMqLIA-KAL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  305 GAKTYKMSmaNRGQNQPVLNITNKQAFITAQ--------NHGYALDnTLPAGWKPLFVNVNDQtNEGIMHESKPFFAVQF 376
Cdd:cd01742   88 GGKVERGD--KREYGKAEIEIDDSSPLFEGLpdeqtvwmSHGDEVV-KLPEGFKVIASSDNCP-VAAIANEEKKIYGVQF 163

                        170       180
                 ....*....|....*....|..
gi 21361331  377 HPEVTpgpiDTEY---LFDSFF 395
Cdd:cd01742  164 HPEVT----HTEKgkeILKNFL 181
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
236-379 1.45e-05

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 47.74  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   236 VKRGAEVHLVpwNHDFTKMEYDGILIAGGPGNPALAEPLIQNVRKIleSDRKEPLFGISTGNLITGLAAGA--------- 306
Cdd:PRK07765   29 VWRNDDPRLA--DEAAVAAQFDGVLLSPGPGTPERAGASIDMVRAC--AAAGTPLLGVCLGHQAIGVAFGAtvdrapell 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   307 --KTYKMSMANRG--QNQPvlnitnkQAFITAQNHGYA-LDNTLPAGwkplfVNVNDQTNEGI----MHESKPFFAVQFH 377
Cdd:PRK07765  105 hgKTSSVHHTGVGvlAGLP-------DPFTATRYHSLTiLPETLPAE-----LEVTARTDSGVimavRHRELPIHGVQFH 172


                  ..
gi 21361331   378 PE 379
Cdd:PRK07765  173 PE 174
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 230-395 2.61e-05

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: 46.41  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  230 NVIRLLVKRGAEVHLVPWNHDFTKMEY-----DGILIAGGPGN--PALAEPLIQN---------------VRKILEsdRK 287
Cdd:cd01745   23 YYVDAVRKAGGLPVLLPPVDDEEDLEQylellDGLLLTGGGDVdpPLYGEEPHPElgpidperdafelalLRAALE--RG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  288 EPLFGISTGNLITGLAAGAKTYKMSMANRgqnqpvlnitnkqafitaqNHGYALDnTLPAGWKPLFVnVNDQTNEGIMHE 367
Cdd:cd01745  101 KPILGICRGMQLLNVALGGTLYQDIRVNS-------------------LHHQAIK-RLADGLRVEAR-APDGVIEAIESP 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 21361331  368 SKPF-FAVQFHPEVTP-GPIDTEYLFDSFF 395
Cdd:cd01745  160 DRPFvLGVQWHPEWLAdTDPDSLKLFEAFV 189
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 566-748 3.90e-05

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 47.83  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   566 AVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETL---MDLSTK----AFAmTNQILVEKSVTGWKEIEYEVVR 638
Cdd:PRK12833  140 VVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLaaeLPLAQReaqaAFG-DGGVYLERFIARARHIEVQILG 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   639 DADDncvTVCNMENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNAR 718
Cdd:PRK12833  219 DGER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTR 295

                         170       180       190
                  ....*....|....*....|....*....|
gi 21361331   719 LSRSSALASKATGYPLAFIAAKIALGIPLP 748
Cdd:PRK12833  296 IQVEHPVTEAITGIDLVQEMLRIADGEPLR 325
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 1094-1253 8.92e-05

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: 46.61  E-value: 8.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1094 AVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPS---Y----VLsgsamnVVFSEDEMKKFLEEATRVsqehPVVL 1166
Cdd:COG0026   95 AFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrggYdgkgQV------VIKSAADLEAAWAALGGG----PCIL 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1167 TKFVEGAREVemdAV----GKDGRVISHAISEHVEDAGV-HsgdaTLMLPTQtISQGAIEKVKDATRKIAKAFAISGPFN 1241
Cdd:COG0026  165 EEFVPFEREL---SVivarSPDGEVATYPVVENVHRNGIlD----ESIAPAR-ISEALAAEAEEIAKRIAEALDYVGVLA 236

                        170
                 ....*....|...
gi 21361331 1242 VQ-FLVKGNDVLV 1253
Cdd:COG0026  237 VEfFVTKDGELLV 249
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 566-719 9.42e-05

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 46.72  E-value: 9.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   566 AVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMdlstKAFAMTNQ----------ILVEKSVTGWKEIEYE 635
Cdd:PRK08591  137 PVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELE----KAFSMARAeakaafgnpgVYMEKYLENPRHIEIQ 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   636 VVRDADDNcvtvcnmenvdamGVHTGD---SV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFaLH 704
Cdd:PRK08591  213 VLADGHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEF-LY 278

                         170
                  ....*....|....*
gi 21361331   705 PTSMEYCIIEVNARL 719
Cdd:PRK08591  279 EKNGEFYFIEMNTRI 293
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 233-381 9.77e-05

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: 45.00  E-value: 9.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    233 RLLVKRGAEVHLVPWN---HDFTKMEYDGILIAGGPgNPALAEPLIQNVRKILESDRkePLFGISTGNLITGLAAGAKTY 309
Cdd:TIGR00888   16 RRLRELGVYSELVPNTtplEEIREKNPKGIILSGGP-SSVYAENAPRADEKIFELGV--PVLGICYGMQLMAKQLGGEVG 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331    310 KMSMANRGQNQpvLNITNKQAFITAQN--------HGYALdNTLPAGWKPLFVNVNDQtNEGIMHESKPFFAVQFHPEVT 381
Cdd:TIGR00888   93 RAEKREYGKAE--LEILDEDDLFRGLPdestvwmsHGDKV-KELPEGFKVLATSDNCP-VAAMAHEEKPIYGVQFHPEVT 168
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
527-648 2.44e-04

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 45.47  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   527 KEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSF--AVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRE 604
Cdd:PRK05586   96 KECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSegEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 21361331   605 TLMDL--STKAFAMTN----QILVEKSVTGWKEIEYEVVRDADDNCVTVC 648
Cdd:PRK05586  176 ELIKAfnTAKSEAKAAfgddSMYIEKFIENPKHIEFQILGDNYGNVVHLG 225
PRK14570 PRK14570
D-alanyl-alanine synthetase A; Provisional
 1120-1184 3.20e-04

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173034 [Multi-domain]  Cd Length: 364  Bit Score: 44.82  E-value: 3.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361331  1120 KSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEAtrVSQEHPVVLTKFVEgAREVEMDAVGKD 1184
Cdd:PRK14570  168 EVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEA--FKYDLTVVIEKFIE-AREIECSVIGNE 229
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 566-718 3.61e-04

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: 45.46  E-value: 3.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  566 AVESIEDALKAADTIGYPVMIRSayALGGLGSG--ICPNRETLMDL-------STKAFAmTNQILVEKSVTGWKEIEYEV 636
Cdd:COG1038  140 PVDDLEEALAFAEEIGYPVMLKA--AAGGGGRGmrVVRSEEELEEAfesarreAKAAFG-DDEVFLEKYIERPKHIEVQI 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  637 VRDADDNCVTV----CnmenvdamgvhtgdSV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALH 704
Cdd:COG1038  217 LGDKHGNIVHLferdC--------------SVqrrhqkVVeiAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVD 282

                        170
                 ....*....|....
gi 21361331  705 PTsMEYCIIEVNAR 718
Cdd:COG1038  283 DD-GNFYFIEVNPR 295
ATPgrasp_Ter pfam15632
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ...
 1163-1311 4.13e-04

ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 434824 [Multi-domain]  Cd Length: 131  Bit Score: 41.83  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1163 PVVLTKFVEGArEVEMDAVGKDGRVIShAISEHVEDAGVhsgdatlmlptQTISQ--GAIEkvkdATRKIAKAFAISGPF 1240
Cdd:pfam15632    4 PLLVMEYLPGP-EYSVDCLAGHGELIA-AVPRRKGDGGI-----------QTLEDdpELIE----AARRLAEAFGLDGLF 66

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361331   1241 NVQFLVKGNDVLVIECNLRASRSFPfVSKTLGVDFIDVATKVMIGENVDEkhlptLDHPIIPADYVAIKAP 1311
Cdd:pfam15632   67 NVQFRYDGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLALKLLLGLETPD-----PVEPRLGLRVREIEKV 131
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 535-815 4.55e-04

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 44.84  E-value: 4.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   535 GTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAF 614
Cdd:PRK02186   96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALR 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   615 -AMTNQILVEKSVTGwKEIEYEVVRDADDNCVtvcnmenVDAMGVHTGDS---VVVA---PAQtLSNAEFQMLRRTSINV 687
Cdd:PRK02186  176 rAGTRAALVQAYVEG-DEYSVETLTVARGHQV-------LGITRKHLGPPphfVEIGhdfPAP-LSAPQRERIVRTVLRA 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   688 VRHLGI-VGECNIQFALHPTSMeyCIIEVNARLSRS--SALASKATGYPLAFIAAKIALGIP----------------LP 748
Cdd:PRK02186  247 LDAVGYaFGPAHTELRVRGDTV--VIIEINPRLAGGmiPVLLEEAFGVDLLDHVIDLHLGVAafadptakrygairfvLP 324

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361331   749 EiknvVSGK-TSACFEPSLDYMVTKIprwdldRFH-----GTSSRI-GSSMKSVGEVMAIGRTFEESFQKALRM 815
Cdd:PRK02186  325 A----RSGVlRGLLFLPDDIAARPEL------RFHplkqpGDALRLeGDFRDRIAAVVCAGDHRDSVAAAAERA 388
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 568-744 7.80e-04

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 43.65  E-value: 7.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   568 ESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDL------STKAFAMTNQILVEKSVTGWKEIEYEVVRDAD 641
Cdd:PRK08463  139 ESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAfesckrEALAYFNNDEVFMEKYVVNPRHIEFQILGDNY 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   642 DNCVTVCnmENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYcIIEVNARLSR 721
Cdd:PRK08463  219 GNIIHLC--ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFY-FMEMNTRIQV 295

                         170       180
                  ....*....|....*....|...
gi 21361331   722 SSALASKATGYPLAFIAAKIALG 744
Cdd:PRK08463  296 EHGVTEEITGIDLIVRQIRIAAG 318
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 255-379 8.50e-04

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: 42.23  E-value: 8.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  255 EYDGILIAGGPGNPALAE-----PLIQNVRKILESDRkePLFGISTGNLITGLAAGAK-----------TYKMSMANRGQ 318
Cdd:cd01741   46 DYDGLVILGGPMSVDEDDypwlkKLKELIRQALAAGK--PVLGICLGHQLLARALGGKvgrnpkgweigWFPVTLTEAGK 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361331  319 NQPvLNITNKQAFITAQNHGYALDnTLPAGWKPLFVNVNDQtNEGIMHESKpFFAVQFHPE 379
Cdd:cd01741  124 ADP-LFAGLPDEFPVFHWHGDTVV-ELPPGAVLLASSEACP-NQAFRYGDR-ALGLQFHPE 180
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
234-379 1.40e-03

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 41.39  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   234 LLVKRGAEVHLvpwnHDFTKMEYDGILIAGGPGNPALAEPLIQNVRKILEsdrKEPLFGISTGNLITGLAAGAKTYKMSM 313
Cdd:PRK06774   26 VMVKRNDELQL----TDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFAD---KLPILGVCLGHQALGQAFGARVVRARQ 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361331   314 ANRGQN-------QPVLNITNKQAFITaQNHGYALD-NTLPA-----GWKPLFVNVNDQTneGIMHESKPFFAVQFHPE 379
Cdd:PRK06774   99 VMHGKTsaichsgQGVFRGLNQPLTVT-RYHSLVIAaDSLPGcfeltAWSERGGEMDEIM--GIRHRTLPLEGVQFHPE 174
PRK14569 PRK14569
D-alanyl-alanine synthetase A; Provisional
 500-717 1.85e-03

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173033 [Multi-domain]  Cd Length: 296  Bit Score: 41.97  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   500 QPDGLILGMGGQTALNCGVElfkrGVLKEYGVKVLGTSVESIMATEDRQLFSDKLneINEKIaPSFAVESIEDALKAADT 579
Cdd:PRK14569   56 KPDKCFVALHGEDGENGRVS----ALLEMLEIKHTSSSMKSSVITMDKMISKEIL--MHHRM-PTPMAKFLTDKLVAEDE 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   580 IGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAfAMTNQILVEKSVTGwKEIEYEVVRDADDNCVTVCNM-ENVDAMGV 658
Cdd:PRK14569  129 ISFPVAVKPSSGGSSIATFKVKSIQELKHAYEEA-SKYGEVMIEQWVTG-KEITVAIVNDEVYSSVWIEPQnEFYDYESK 206

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 21361331   659 HTGDSVVVAPAQTLSNAEFQmLRRTSINVVRHLGIVGECNIQFaLHPTSMEYCIIEVNA 717
Cdd:PRK14569  207 YSGKSIYHSPSGLCEQKELE-VRQLAKKAYDLLGCSGHARVDF-IYDDRGNFYIMEINS 263
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 1101-1277 2.05e-03

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: 41.15  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1101 VAQAPWKAVN----TLNEALEFAKSVD---YPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRvsQEHPVVLTKFVEGa 1173
Cdd:pfam07478    7 LPVVPFVTFTradwKLNPKEWCAQVEEalgYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQ--YDEKVLVEEGIEG- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   1174 REVEMdAVGKDGRVISHAISEHVEDAGVH-------SGDATLMLPTQtISQGAIEKVKDATRKIAKAFAISGPFNVQFLV 1246
Cdd:pfam07478   84 REIEC-AVLGNEDPEVSPVGEIVPSGGFYdyeakyiDDSAQIVVPAD-LEEEQEEQIQELALKAYKALGCRGLARVDFFL 161

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 21361331   1247 -KGNDVLVIECN----LRASRSFPFVSKTLGVDFID 1277
Cdd:pfam07478  162 tEDGEIVLNEVNtipgFTSISMFPKLAAAAGVSFPD 197
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 1107-1259 3.06e-03

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: 42.37  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1107 KAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVSQ------EhpVVLTKFVEGAREVEMDA 1180
Cdd:COG1038  139 GPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafgddE--VFLEKYIERPKHIEVQI 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1181 VG-KDGRVIshaiseH---------------VEDAgvhsgdatlmlPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQF 1244
Cdd:COG1038  217 LGdKHGNIV------HlferdcsvqrrhqkvVEIA-----------PAPNLDEELREAICEAAVKLAKAVGYVNAGTVEF 279

                        170
                 ....*....|....*.
gi 21361331 1245 LV-KGNDVLVIECNLR 1259
Cdd:COG1038  280 LVdDDGNFYFIEVNPR 295
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
230-379 4.87e-03

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 41.24  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   230 NVIRLLVKRGAEVHLVPWNHDFT-----KMEYDGILIAGGPGNPALAEPLIQNVRKIlesDRKEPLFGISTGNLITGLAA 304
Cdd:PRK14607   14 NIYQYIGELGPEEIEVVRNDEITieeieALNPSHIVISPGPGRPEEAGISVEVIRHF---SGKVPILGVCLGHQAIGYAF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331   305 GAKTYKMSMANRGQNQPV------LNITNKQAFITAQNHGYALD-NTLPAGWKPLfVNVNDQTNEGIMHESKPFFAVQFH 377
Cdd:PRK14607   91 GGKIVHAKRILHGKTSPIdhngkgLFRGIPNPTVATRYHSLVVEeASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFH 169


                  ..
gi 21361331   378 PE 379
Cdd:PRK14607  170 PE 171
MGS-like cd00532
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ...
 1361-1469 5.54e-03

MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 238297 [Multi-domain]  Cd Length: 112  Bit Score: 38.26  E-value: 5.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331 1361 GILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAwpsqEGQNPSLSSIRKLIRD-GSIDLVINLP 1439
Cdd:cd00532    1 GVFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVS----KRHEDGEPTVDAAIAEkGKFDVVINLR 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 21361331 1440 N--NNTKFVHDNYVIRRTAVDSGIPLLTNFQV 1469
Cdd:cd00532   77 DprRDRCTDEDGTALLRLARLYKIPVTTPNAT 108
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 1108-1190 5.57e-03

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 40.89  E-value: 5.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361331  1108 AVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVSQ----EHPVVLTKFVEGAREVEMDAVGk 1183
Cdd:PRK12833  140 VVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQaafgDGGVYLERFIARARHIEVQILG- 218


                  ....*..
gi 21361331  1184 DGRVISH 1190
Cdd:PRK12833  219 DGERVVH 225
PRK00758 PRK00758
GMP synthase subunit A; Validated
 362-401 8.29e-03

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 39.06  E-value: 8.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 21361331   362 EGIMHESKPFFAVQFHPEVTpgpiDTEY---LFDSFFSLIKKG 401
Cdd:PRK00758  146 EAMKHKEKPIYGVQFHPEVA----HTEYgeeIFKNFLEICGKY 184
 
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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