|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
391-1440 |
0e+00 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 1783.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 391 PPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPD 470
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 471 GILLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGY 550
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 551 PVLVRAAFALGGLGSGFASTKEELSALVAPAFAHT--SQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHT 628
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 629 GESIVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAK 708
Cdd:TIGR01369 244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 709 LALGIPLPELRNSVTGGT-AAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENC 787
Cdd:TIGR01369 324 LAVGYTLDELKNPVTGTTpASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 788 VGFDHT---VKPVSD--VELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAKLLEQHRGRPLPQDL 862
Cdd:TIGR01369 404 TGFDLPdreVEPDEDlwRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 863 LHQAKCLGFSDKQIALAVLSTELVVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRT-PHVLVLGSG 941
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDkKKVLVLGSG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 942 VYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPN 1021
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1022 NMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVA 1101
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1102 YTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVACDGIVSAIAISEHVENAGVHSGDATLVTPPQDITPKTLER 1181
Cdd:TIGR01369 724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1182 IKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVESVG--LMTGSGVV 1259
Cdd:TIGR01369 804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1260 GVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLG 1339
Cdd:TIGR01369 884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1340 YSLYASLGTADFYTEHGVKVTAVDWHFEEAvdgecppqRSILDQLAENHFELVINLSMRGAGgrrlssFVTKGYRTRRLA 1419
Cdd:TIGR01369 964 YKLYATEGTAKFLGEAGIKPELVLKVSEGR--------PNILDLIKNGEIELVINTTSKGAG------TATDGYKIRREA 1029
|
1050 1060
....*....|....*....|.
gi 158534057 1420 ADFSVPLIIDIKCTKLFVEAL 1440
Cdd:TIGR01369 1030 LDYGVPLITTLNTAEAFAEAL 1050
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
394-1440 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1433.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGIL 473
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVL 553
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 554 VRAAFALGGLGSGFASTKEELSALVAPAFAH--TSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGES 631
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 632 IVVAPSQTLNDREYQLLRRTAIKVTQHLGIV-GECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLA 710
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 711 LGIPLPELRNSVTGGT-AAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVG 789
Cdd:PRK05294 328 VGYTLDEIKNDITGKTpASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 790 FDHTVKPVSDVE-----LETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAKLLEQHrGRPLPQDLLH 864
Cdd:PRK05294 408 LDEDLFEEESLEelreeLKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEN-GLPLDAELLR 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 865 QAKCLGFSDKQIALAVLSTELVVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRTPHVLVLGSGVYR 944
Cdd:PRK05294 487 EAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNR 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 945 IGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMA 1024
Cdd:PRK05294 567 IGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1025 MALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTD 1104
Cdd:PRK05294 647 KALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDE 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1105 GDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaCDGIVSAIA-ISEHVENAGVHSGDATLVTPPQDITPKTLERIK 1183
Cdd:PRK05294 727 EELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEDVLIGgIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIR 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1184 AIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVESVGLMTG--SGVVGV 1261
Cdd:PRK05294 806 EYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGliPPYVAV 885
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1262 KVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKK-NILLTIgSYKNKSELLPTVRLLESLGY 1340
Cdd:PRK05294 886 KEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLELGF 964
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1341 SLYASLGTADFYTEHGVKVTAVDWHFEEAVDgecppqrsILDQLAENHFELVINlSMRGAGGRRlssfvtKGYRTRRLAA 1420
Cdd:PRK05294 965 KILATSGTAKFLREAGIPVELVNKVHEGRPH--------IVDLIKNGEIDLVIN-TPTGRQAIR------DGFSIRRAAL 1029
|
1050 1060
....*....|....*....|
gi 158534057 1421 DFSVPLIIDIKCTKLFVEAL 1440
Cdd:PRK05294 1030 EYKVPYITTLAGARAAVKAI 1049
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
394-1448 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1078.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGIL 473
Cdd:PRK12815 8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVL 553
Cdd:PRK12815 88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 554 VRAAFALGGLGSGFASTKEELSALVAPAFA--HTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGES 631
Cdd:PRK12815 168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQasPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 632 IVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLAL 711
Cdd:PRK12815 248 IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 712 GIPLPELRNSVTGGT-AAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALR--MVDENCV 788
Cdd:PRK12815 328 GYTLNELKNPVTGLTyASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRslEIKRNGL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 789 GFDHTVKPVSDVEL----ETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAKLLEQHrGRPLPQDLLH 864
Cdd:PRK12815 408 SLPIELSGKSDEELlqdlRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAED-GLDLSADLLR 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 865 QAKCLGFSDKQIALAVLSTELVVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNThDLDFRT--PHVLVLGSGV 942
Cdd:PRK12815 487 KVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGES-EAEPSSekKKVLILGSGP 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 943 YRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNN 1022
Cdd:PRK12815 566 IRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTAIN 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1023 MAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAY 1102
Cdd:PRK12815 646 LAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVY 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1103 TDGDLERFLssAAAVSKEHPVVISKFIqEAKEIDVDAVaCDGIVSAIA-ISEHVENAGVHSGDATLVTPPQDITPKTLER 1181
Cdd:PRK12815 726 DEPALEAYL--AENASQLYPILIDQFI-DGKEYEVDAI-SDGEDVTIPgIIEHIEQAGVHSGDSIAVLPPQSLSEEQQEK 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1182 IKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVESVGLMTG----SG 1257
Cdd:PRK12815 802 IRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELGYPNGlwpgSP 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1258 VVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLES 1337
Cdd:PRK12815 882 FIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLARRFAQ 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1338 LGYSLYASLGTADFYTEHGVKVTAVdwhfeeAVDGECPPQRSILDQLAENHFELVINLSMRGaggrrlssfVTKGYRTRR 1417
Cdd:PRK12815 962 LGFKLLATEGTANWLAEEGITTGVV------EKVQEGSPSLLERIKQHRIVLVVNTSLSDSA---------SEDAIKIRD 1026
|
1050 1060 1070
....*....|....*....|....*....|.
gi 158534057 1418 LAADFSVPLIIDIKCTKLFVEALGQIGPAPP 1448
Cdd:PRK12815 1027 EALSTHIPVFTELETAQAFLQVLESLALTTQ 1057
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
394-1440 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 881.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGIL 473
Cdd:PLN02735 24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLG-YPV 552
Cdd:PLN02735 104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 553 LVRAAFALGGLGSGFASTKEELSALVAPAFA--HTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGE 630
Cdd:PLN02735 184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAasITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 631 SIVVAPSQTLNDREYQLLRRTAIKVTQHLGIvgEC---NVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAA 707
Cdd:PLN02735 264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 708 KLALGIPLPELRNSVTGGT-AAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDEN 786
Cdd:PLN02735 342 KLSVGYTLDQIPNDITLKTpASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 787 CVGFdhTVKPVSDVE---------LETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAKLLEQHRGRP 857
Cdd:PLN02735 422 FSGW--GCAKVKELDwdweqlkykLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLSE 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 858 LPQDLLHQAKCLGFSDKQIALAVLSTELVVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRTPHVLV 937
Cdd:PLN02735 500 LSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLI 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 938 LGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGG 1017
Cdd:PLN02735 580 LGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGG 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1018 QLPNNMAMALHRQ-------------QCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYP 1084
Cdd:PLN02735 660 QTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYP 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1085 CVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVA-CDGIVSAIAISEHVENAGVHSG 1163
Cdd:PLN02735 740 VVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSG 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1164 DATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFNLQL-IAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRII 1242
Cdd:PLN02735 820 DSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVM 899
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1243 MGEKVESVGLmTGSGV---VGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTI 1319
Cdd:PLN02735 900 SGKSLKDLGF-TEEVIpahVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGTVFIS 978
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1320 GSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAV-DWHfeeavdgECPPQrsILDQLAENHFELVINLSMR 1398
Cdd:PLN02735 979 LNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVlKLH-------EGRPH--AGDMLANGQIQLMVITSSG 1049
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|..
gi 158534057 1399 GAGGRRlssfvtKGYRTRRLAADFSVPLIIDIKCTKLFVEAL 1440
Cdd:PLN02735 1050 DALDQK------DGRQLRRMALAYKVPIITTVAGALATAQAV 1085
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
399-940 |
0e+00 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 650.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 399 LGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGILLTFGG 478
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 479 QTALNCGVELTKAGVLAryGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAF 558
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 559 ALGGLGSGFASTKEELSALVAPAFAH--TSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAP 636
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVspDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 637 SQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNpeSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 717 ELRNSvTGgtaaFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDencVGFDHTV-- 794
Cdd:COG0458 317 ELGND-TG----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLE---IGLPGTVll 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 795 KPVSDVE-----LETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAKLLEQHrgrPLPQDLLHQAKCL 869
Cdd:COG0458 389 SLVADDDkeealLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEI---ILVINTLLGAKSL 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158534057 870 GFSDKQIALAVLSTELVVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRTPHVLVLGS 940
Cdd:COG0458 466 GDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
1460-1806 |
0e+00 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 593.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1460 KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASS 1539
Cdd:cd01316 1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1540 ENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPSHLPIVAHAERQSVAAVLMVAQLTRRSVHICHVARKE 1619
Cdd:cd01316 81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1620 EILLIKTAKAQGLPVTCEVAPHHLFLNREDLERlgpGKGEVRPELGSREDMEALWENMAVIDCFASDHAPHTLEEKCGPK 1699
Cdd:cd01316 161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPR---GQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1700 PPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVEVDLEHEWTVPSHMPFSKAHWTPFEGQKV 1779
Cdd:cd01316 238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317
|
330 340
....*....|....*....|....*..
gi 158534057 1780 KGTVRRVVLRGEVAYIDGQVLVPPGYG 1806
Cdd:cd01316 318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
938-1440 |
1.53e-176 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 550.25 E-value: 1.53e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 938 LGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGG 1017
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1018 QLPNNMAMALHRQQ----CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVL 1093
Cdd:COG0458 81 QTALNLAVELEEAGilegVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1094 SGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaCDG----IVsaIAISEHVENAGVHSGDATLVT 1169
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVV-RDGednvII--VGIMEHIEPAGVHSGDSICVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1170 PPQDITPKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVES 1249
Cdd:COG0458 238 PPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1250 VGLMTG----SGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKnILLTIGSYKNK 1325
Cdd:COG0458 318 LGNDTGfeptLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGT-VLLSLVADDDK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1326 SELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILDQLAENHFELVINLSMRGAGGRRL 1405
Cdd:COG0458 397 EEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEG--------RPIIVDEIELEEIILVINTLLGAKSLGDS 468
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 158534057 1406 SSF------VTKGYRTRRLAADFSVPLIIDIKCTKLFVEAL 1440
Cdd:COG0458 469 DGIirralaAKVPYVTTLAAAAAAALAIKAVETEAGEFEEA 509
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-355 |
8.02e-160 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 496.52 E-value: 8.02e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1 MAALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDeedefglskWFESSE 80
Cdd:PRK12564 4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 81 IHVAGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALP-----FVDPNA 155
Cdd:PRK12564 75 PHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 156 RPLAPEVSIKTPRVFNAGGA---PRIFAVDCGLKYNQIRCLCQLGAEVTVVPWN---HELDSRKYDGLFLSNGPGDPASY 229
Cdd:PRK12564 155 LDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPAAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 230 PGVVSTLNRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWA 309
Cdd:PRK12564 235 DYAIEMIRELLEKK--IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 158534057 310 PLFTNANDCSNEGIVHDNLPFFSVQFHPEHRAGPSDMELLFDVFLE 355
Cdd:PRK12564 313 VTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
2-359 |
5.72e-156 |
|
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: 485.98 E-value: 5.72e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2 AALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDeedefglskWFESSEI 81
Cdd:TIGR01368 1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDE---------DAESKGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 82 HVAGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVqkgTEPSALPF------VDPNA 155
Cdd:TIGR01368 72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVIS---TEDSNDEElvekarVSPDI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 156 RP--LAPEVSIKTPRVFNA--GGAPRIFAVDCGLKYNQIRCLCQLGAEVTVVPWNH---ELDSRKYDGLFLSNGPGDPAS 228
Cdd:TIGR01368 149 TGinLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTdaeEIKKYNPDGIFLSNGPGDPAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 229 YPGVVSTLNRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAG- 307
Cdd:TIGR01368 229 VEPAIETIRKLLEK---IPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGd 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 158534057 308 WAPLFTNANDCSNEGIVHDNLPFFSVQFHPEHRAGPSDMELLFDVFLETVRD 359
Cdd:TIGR01368 306 LEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
2-358 |
5.74e-155 |
|
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: 482.98 E-value: 5.74e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2 AALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDeedefglskWFESSEI 81
Cdd:COG0505 5 ALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDE---------DFESDRP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 82 HVAGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALP-----FVDPNAR 156
Cdd:COG0505 76 WVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLekaraAPGMEGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 157 PLAPEVSIKTPRVFNAGGAP--RIFAVDCGLKYNQIRCLCQLGAEVTVVPWN---HELDSRKYDGLFLSNGPGDPASYPG 231
Cdd:COG0505 156 DLVKEVSTKEPYEWTEAPGAgfHVVALDFGVKRNILRELAERGCRVTVVPATtsaEEILALNPDGVFLSNGPGDPAALDY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 232 VVSTLNRVLSEpnPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPA-GWAP 310
Cdd:COG0505 236 AIETIRELLGK--GIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 158534057 311 LFTNANDCSNEGIVHDNLPFFSVQFHPEHRAGPSDMELLFDVFLETVR 358
Cdd:COG0505 314 THVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| PyrB |
COG0540 |
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ... |
1919-2224 |
9.73e-140 |
|
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440306 [Multi-domain] Cd Length: 306 Bit Score: 437.95 E-value: 9.73e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1919 HSLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT 1998
Cdd:COG0540 1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1999 SSVQKGESLADSVQTMSCY-ADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2077
Cdd:COG0540 81 SSVSKGESLADTIRTLEAYgADAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2078 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPSSVWDFVAsrgtkqEEFESIEEALPDTDVLYMTRIQKERFGSSQ- 2156
Cdd:COG0540 161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEIEELGV------EVTTDLDEALPDADVVYMLRIQKERFTDGLf 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158534057 2157 -EYEACFGQFILTPHIMTRAKKKMVVMH--PMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2224
Cdd:COG0540 234 pSYREYKRSYGLTAERLALAKPDAIVMHpgPRNRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
|
|
| pyrB |
PRK00856 |
aspartate carbamoyltransferase catalytic subunit; |
1920-2224 |
1.34e-127 |
|
aspartate carbamoyltransferase catalytic subunit;
Pssm-ID: 234849 [Multi-domain] Cd Length: 305 Bit Score: 403.30 E-value: 1.34e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1920 SLVGQHILSVKQFTKDQMSHLFNVAHTLR-MMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT 1998
Cdd:PRK00856 2 PLKMKHLLSIEDLSREEIELLLDTAEEFKeVLRREVKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1999 SSVQKGESLADSVQTMSCY-ADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2077
Cdd:PRK00856 82 SSVSKGETLADTIRTLSAMgADAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2078 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPSSVWDFvasrgtkqEEFESIEEALPDTDVLYMTRIQKERFGSSQ- 2156
Cdd:PRK00856 162 VGDIKHSRVARSNIQALTRLGAEVRLIAPPTL-LPEGMPEY--------GVHTDLDEVIEDADVVMMLRVQKERMDGGLl 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158534057 2157 -EYEACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2224
Cdd:PRK00856 233 pSYEEYKRSYGLTAERLALAKPDAIVMHPGPvnRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLELLLGG 303
|
|
| PLN02527 |
PLN02527 |
aspartate carbamoyltransferase |
1924-2223 |
5.58e-127 |
|
aspartate carbamoyltransferase
Pssm-ID: 178142 [Multi-domain] Cd Length: 306 Bit Score: 401.82 E-value: 5.58e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1924 QHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEA--TSSV 2001
Cdd:PLN02527 1 SDVIEAQQFDREMLELLFEVAREMEKVERGSPGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENAgeFSSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2002 QKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDL 2081
Cdd:PLN02527 81 AKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATAEIPVINAGDGPGQHPTQALLDVYTIQREIGRLDGIKVGLVGDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2082 KHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPSSVWDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSSQE-YE 2159
Cdd:PLN02527 161 ANGRTVRSLAYLLAKYEdVKIYFVAPDVVKMKDDIKDYLTSKGVEWEESSDLMEVASKCDVLYQTRIQRERFGERIDlYE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158534057 2160 ACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2223
Cdd:PLN02527 241 AARGKYIVDKKVMDVLPKHAVVMHPLPRLDEITTDVDSDPRAAYFRQAKNGLFIRMALLKLLLG 304
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
4-357 |
3.41e-124 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 395.80 E-value: 3.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 4 LVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEedefglskwFESSEIHV 83
Cdd:PRK12838 5 LILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADD---------YESKQPQV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 84 AGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSA---LPFVDPNArpLAP 160
Cdd:PRK12838 76 KGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDDAHAFdqiKALVLPKN--VVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 161 EVSIKTPRVFNAGGaPRIFAVDCGLKYNQIRCLCQLGAEVTVVPWN---HELDSRKYDGLFLSNGPGDPASYPGVVSTLN 237
Cdd:PRK12838 154 QVSTKEPYTYGNGG-KHVALIDFGYKKSILRSLSKRGCKVTVLPYDtslEEIKNLNPDGIVLSNGPGDPKELQPYLPEIK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 238 RVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSL-PAGWAPLFTNAN 316
Cdd:PRK12838 233 KLISS---YPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRFFNVN 309
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 158534057 317 DCSNEGIVHDNLPFFSVQFHPEHRAGPSDMELLFDVFLETV 357
Cdd:PRK12838 310 DGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMM 350
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
1461-1786 |
1.55e-118 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 379.04 E-value: 1.55e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1461 LVRLPGLIDVHVHLREPGGT-HKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASS 1539
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTtYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1540 E-NAGTL-GAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPS-HLPIVAHAERqsvaaVLMVAQLTRRSVHICHVA 1616
Cdd:cd01302 81 GdVTDELkKLFDAGINSLKVFMNYYFGELFDVDDGTLMRTFLEIASrGGPVMVHAER-----AAQLAEEAGANVHIAHVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1617 RKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPgKGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEE 1694
Cdd:cd01302 156 SGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGA-WGKVNPPLRSKEDREALWEGVKngKIDTIASDHAPHSKEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1695 KCGPKPPPGFPG----LETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQED---------TYVEVDLEHEWTVP 1761
Cdd:cd01302 235 KESGKDIWKAPPgfpgLETRLPILLTEGVKRGLSLETLVEILSENPARIFGLYPKGTiavgydadlVIVDPKKEWKVTAE 314
|
330 340
....*....|....*....|....*
gi 158534057 1762 SHMpfSKAHWTPFEGQKVKGTVRRV 1786
Cdd:cd01302 315 EIE--SKADWTPFEGMEVTGKPVST 337
|
|
| asp_carb_tr |
TIGR00670 |
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ... |
1925-2223 |
1.98e-112 |
|
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273209 [Multi-domain] Cd Length: 301 Bit Score: 359.75 E-value: 1.98e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1925 HILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEA-TSSVQK 2003
Cdd:TIGR00670 2 HLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFSDSeTSSVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2004 GESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKH 2083
Cdd:TIGR00670 82 GETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDLKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2084 GRTVHSLACLLTQYRVSLRYVAPPSLRMPSSVWDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSSQEYEACFG 2163
Cdd:TIGR00670 162 GRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEYEKVKG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2164 QFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2223
Cdd:TIGR00670 242 SYGITLERLEAAKKGVIIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
514-716 |
1.39e-102 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 327.72 E-value: 1.39e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 514 DRRAFAARMAEIGEHVAPSEAA--NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELSALVAPAFAHT------ 585
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 586 SQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLgiHTGESIVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGEC 665
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 158534057 666 NVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
1437-1810 |
2.68e-99 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 327.82 E-value: 2.68e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1437 VEALGQIGPAPPLKVHVDCmtSQKLVrLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPAL 1516
Cdd:COG0044 25 IAAIGPDLAAPEAAEVIDA--TGLLV-LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1517 ALAQKLAEAGARCDFTLFLGAS---SENAGTLGAVAGS-AAGLKLYLNETFSELRLDS----------------VAQWME 1576
Cdd:COG0044 102 EFKLARAEEKALVDVGPHGALTkglGENLAELGALAEAgAVAFKVFMGSDDGNPVLDDgllrraleyaaefgalVAVHAE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1577 HFET------------WPSHLPIV-AHAERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHL 1643
Cdd:COG0044 182 DPDLirggvmnegktsPRLGLKGRpAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1644 FLNREDLERLGPgKGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPG--FPGLETMLPLLLT-AV 1718
Cdd:COG0044 262 TLTDEDLERYGT-NFKVNPPLRTEEDREALWEGLAdgTIDVIATDHAPHTLEEKELPFAEAPngIPGLETALPLLLTeLV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1719 SEGRLSLDDLLQRLHHNPRRIFHLP----LQEDTY---VEVDLEHEWTV-PSHMpFSKAHWTPFEGQKVKGTVRRVVLRG 1790
Cdd:COG0044 341 HKGRLSLERLVELLSTNPARIFGLPrkgrIAVGADadlVLFDPDAEWTVtAEDL-HSKSKNTPFEGRELTGRVVATIVRG 419
|
410 420
....*....|....*....|
gi 158534057 1791 EVAYIDGQVLVPPgYGQDVR 1810
Cdd:COG0044 420 RVVYEDGEVVGEP-RGRFLR 438
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
178-354 |
9.00e-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: 309.43 E-value: 9.00e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 178 IFAVDCGLKYNQIRCLCQLGAEVTVVPWNH---ELDSRKYDGLFLSNGPGDPASYPGVVSTLNRVLSEPnpRPVFGICLG 254
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTdaeEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK--IPIFGICLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 255 HQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDNLPFFSVQ 334
Cdd:cd01744 79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158
|
170 180
....*....|....*....|
gi 158534057 335 FHPEHRAGPSDMELLFDVFL 354
Cdd:cd01744 159 FHPEASPGPHDTEYLFDEFL 178
|
|
| PRK08192 |
PRK08192 |
aspartate carbamoyltransferase; Provisional |
1923-2223 |
4.70e-93 |
|
aspartate carbamoyltransferase; Provisional
Pssm-ID: 169269 [Multi-domain] Cd Length: 338 Bit Score: 305.88 E-value: 4.70e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1923 GQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVL-SFSEATSSV 2001
Cdd:PRK08192 5 GSHILSVNQLDRDAIQRIFNVADRMEPYALREKRTRVLEGAILGNLFFEPSTRTRVSFGCAFNLLGGHVReTTGMASSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2002 QKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREEL----GTVNGMTITM 2077
Cdd:PRK08192 85 SKGESLYDTARVLSTYSDVIAMRHPDAGSVKEFAEGSRVPVINGGDGSNEHPTQALLDLFTIQKELahagRGIDGMHIAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2078 VGDLKHGRTVHSLACLLTQY-RVSLRYVAPPSLRMPSSVWDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSSQ 2156
Cdd:PRK08192 165 VGDLKFGRTVHSLSRLLCMYkNVSFTLVSPKELAMPDYVISDIENAGHKITITDQLEGNLDKADILYLTRIQEERFPSQE 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158534057 2157 EYEACFGQFILTPHIMTR-AKKKMVVMHPMPR-----VNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2223
Cdd:PRK08192 245 EANKYRGKFRLNQSIYTQhCKSNTVIMHPLPRdsraqANELDNDLNSHPNLAIFRQADNGLLIRMALFALTLG 317
|
|
| PRK11891 |
PRK11891 |
aspartate carbamoyltransferase; Provisional |
1924-2223 |
2.05e-88 |
|
aspartate carbamoyltransferase; Provisional
Pssm-ID: 183362 [Multi-domain] Cd Length: 429 Bit Score: 296.01 E-value: 2.05e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1924 QHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT-SSVQ 2002
Cdd:PRK11891 88 PQLLSVDQFSRDSVEALFRVADVMQPIARRQKISRVLEGAVLGNLFFEASTRTRVSFGAAFCRLGGSVCDTTGFTfSSMA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2003 KGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREE---LG-TVNGMTITMV 2078
Cdd:PRK11891 168 KGESIYDTSRVMSGYVDALVIRHPEQGSVAEFARATNLPVINGGDGPGEHPSQALLDLYTIQREfsrLGkIVDGAHIALV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2079 GDLKHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPSSVWDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFgSSQE 2157
Cdd:PRK11891 248 GDLKYGRTVHSLVKLLALYRgLKFTLVSPPTLEMPAYIVEQISRNGHVIEQTDDLAAGLRGADVVYATRIQKERF-ADES 326
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158534057 2158 YEACFGQFILTPHIMTRA-KKKMVVMHPMPR-----VNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2223
Cdd:PRK11891 327 FEGYTPDFQINQALVDAVcKPDTLIMHPLPRdsrpgANDLSTDLNRDPRLAIFRQTDNGIPVRMAIFAVLLG 398
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
1461-1796 |
1.31e-87 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 292.81 E-value: 1.31e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSE 1540
Cdd:TIGR00857 35 LLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1541 NAGTLGAVAGS--AAGL--KLYLNETFSELRLDSVAQWME-----------HFE---------------TWPSHLPIVA- 1589
Cdd:TIGR00857 115 NQGKELTEAYElkEAGAvgRMFTDDGSEVQDILSMRRALEyaaiagvpialHAEdpdliyggvmhegpsAAQLGLPARPp 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1590 HAERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGpGKGEVRPELGSRED 1669
Cdd:TIGR00857 195 EAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLD-GNGKVNPPLREKED 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1670 MEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPG--FPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP-- 1743
Cdd:TIGR00857 274 RLALIEGLKdgIIDIIATDHAPHTLEEKTKEFAAAPpgIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPdk 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 158534057 1744 --LQEDTYVE---VDLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYID 1796
Cdd:TIGR00857 354 gtLEEGNPADitvFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
1464-1790 |
1.75e-87 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 290.77 E-value: 1.75e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENAG 1543
Cdd:cd01318 5 LPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTGSEDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1544 TLgAVAGSAAGLKLYLNETFSELRLDsvaqwMEHFETWPSH--LPIVAHAERQ--------------------------- 1594
Cdd:cd01318 85 EE-LDKAPPAGYKIFMGDSTGDLLDD-----EETLERIFAEgsVLVTFHAEDEdrlrenrkelkgesahprirdaeaaav 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1595 SVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQglpVTCEVAPHHLFLNREDLERLGpGKGEVRPELGSREDMEALW 1674
Cdd:cd01318 159 ATARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDRLG-TLGKVNPPLRSREDRKALL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1675 ENMA--VIDCFASDHAPHTLEEKCGPKPPPGF--PGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPL---QED 1747
Cdd:cd01318 235 QALAdgRIDVIASDHAPHTLEEKRKGYPAAPSgiPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIFGIKNkgrIAE 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 158534057 1748 TY----VEVDLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRG 1790
Cdd:cd01318 315 GYdadlTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
2-355 |
4.90e-85 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 284.38 E-value: 4.90e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2 AALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEedefglskwFESSEI 81
Cdd:CHL00197 7 AILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLED---------IESVKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 82 HVAGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALP--FVDPNARP-- 157
Cdd:CHL00197 78 QVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSYLRakIKESPHMPss 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 158 -LAPEVSIKTPRVFNAGGAP----------------RIFAVDCGLKYNQIRCLCQLGAEVTVVPWN---HELDSRKYDGL 217
Cdd:CHL00197 158 dLIPRVTTSSYYEWDEKSHPsfyladnkrphssyqlKIIVIDFGVKYNILRRLKSFGCSITVVPATspyQDILSYQPDGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 218 FLSNGPGDPASYPGVVSTLNRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPcllVGTGRCF-LTSQNHG 296
Cdd:CHL00197 238 LLSNGPGDPSAIHYGIKTVKKLLKYN--IPIFGICMGHQILSLALEAKTFKLKFGHRGLNHP---SGLNQQVeITSQNHG 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158534057 297 FAVDADSL--PAGWAPLFtNANDCSNEGIVHDNLPFFSVQFHPEHRAGPSDMELLFDVFLE 355
Cdd:CHL00197 313 FAVNLESLakNKFYITHF-NLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIE 372
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1461-1796 |
8.29e-82 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 276.69 E-value: 8.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIiDAPA-----LALAQK-------------- 1521
Cdd:PRK09357 49 LVVAPGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVI-DTPEvveyvLDRAKEaglvdvlpvgaitk 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1522 ------------LAEAGARC---DftlflGASSENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWME-------HFE 1579
Cdd:PRK09357 128 glageeltefgaLKEAGVVAfsdD-----GIPVQDARLMRRALEYAKALDLLIAQHCEDPSLTEGGVMNEgevsarlGLP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1580 TWPshlpivAHAERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPgKGE 1659
Cdd:PRK09357 203 GIP------AVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDP-NYK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1660 VRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPGF--PGLETMLPLLLTA-VSEGRLSLDDLLQRLHH 1734
Cdd:PRK09357 276 VNPPLRTEEDREALIEGLKdgTIDAIATDHAPHAREEKECEFEAAPFgiTGLETALSLLYTTlVKTGLLDLEQLLEKMTI 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158534057 1735 NPRRIFHLP---LQE---DTYVEVDLEHEWTV-PSHMpFSKAHWTPFEGQKVKGTVRRVVLRGEVAYID 1796
Cdd:PRK09357 356 NPARILGLPagpLAEgepADLVIFDPEAEWTVdGEDF-ASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
2-350 |
5.59e-77 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 262.61 E-value: 5.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2 AALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEEdefglskwfESSEI 81
Cdd:PLN02771 57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDE---------ESRQC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 82 HVAGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQKG--TEPSALPFV---DPNAR 156
Cdd:PLN02771 128 FLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDskTDEELLKMSrswDIVGI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 157 PLAPEVSIKTPRV----------FNAGGAP----RIFAVDCGLKYNQIRCLCQLGAEVTVVPWN---HELDSRKYDGLFL 219
Cdd:PLN02771 208 DLISGVSCKSPYEwvdktnpewdFNTNSRDgesyHVIAYDFGIKHNILRRLASYGCKITVVPSTwpaSEALKMKPDGVLF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 220 SNGPGDPASYPGVVSTLNRVLSEPnprPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAV 299
Cdd:PLN02771 288 SNGPGDPSAVPYAVETVKELLGKV---PVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAV 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 158534057 300 DADSLPAGWAPLFTNANDCSNEGIVHDNLPFFSVQFHPEHRAGPSDMELLF 350
Cdd:PLN02771 365 DPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
4-138 |
3.83e-75 |
|
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: 245.31 E-value: 3.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 4 LVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEedefglskwFESSEIHV 83
Cdd:pfam00988 1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPED---------FESDKIHV 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 158534057 84 AGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:pfam00988 72 AGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
2-138 |
7.02e-71 |
|
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: 233.42 E-value: 7.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2 AALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDeedefglskWFESSEI 81
Cdd:smart01097 3 AYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDE---------DFESDKI 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 158534057 82 HVAGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:smart01097 74 QVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
1464-1803 |
7.56e-71 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 243.91 E-value: 7.56e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTL-FLGASseNA 1542
Cdd:PRK04250 46 LPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALnFLIAG--NC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1543 GTLGAVA--------GSAAGlKLYLnETFSE-----LRLDSV-AQWMEHFETWPSHLPIvahAERQSVAAVLMVAQLTRR 1608
Cdd:PRK04250 124 EKAEEIKadfykifmGASTG-GIFS-ENFEVdyacaPGIVSVhAEDPELIREFPERPPE---AEVVAIERALEAGKKLKK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1609 SVHICHVARKEEILLIKtaKAQGLPVTCEVAPHHLFLNREDLERlGPgKGEVRPELGSREDMEALWENMAVIDCFASDHA 1688
Cdd:PRK04250 199 PLHICHISTKDGLKLIL--KSNLPWVSFEVTPHHLFLTRKDYER-NP-LLKVYPPLRSEEDRKALWENFSKIPIIASDHA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1689 PHTLEEKcgPKPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPL------QEDTYVEVDLEHEWTVPS 1762
Cdd:PRK04250 275 PHTLEDK--EAGAAGIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIKNygieegNYANFAVFDMKKEWTIKA 352
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 158534057 1763 HMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1803
Cdd:PRK04250 353 EELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKP 393
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
1453-1786 |
7.71e-68 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 234.44 E-value: 7.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1453 VDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIiDAPAL--ALAQKLAEAGARCD 1530
Cdd:cd01317 5 IDA---EGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVI-DNPAVveLLKNRAKDVGIVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1531 FTL------FLGASSENAGTL---GAVAGSAAGLKLYLNETfselrLDSVAQWMEHFEtwpshLPIVAH----------- 1590
Cdd:cd01317 81 LPIgaltkgLKGEELTEIGELleaGAVGFSDDGKPIQDAEL-----LRRALEYAAMLD-----LPIIVHpedpslagggv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1591 ------------------AERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLER 1652
Cdd:cd01317 151 mnegkvasrlglpgippeAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALES 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1653 LGPGkGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPG--FPGLETMLPLLLT-AVSEGRLSLDD 1727
Cdd:cd01317 231 YDTN-AKVNPPLRSEEDREALIEALKdgTIDAIASDHAPHTDEEKDLPFAEAPpgIIGLETALPLLWTlLVKGGLLTLPD 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158534057 1728 LLQRLHHNPRRIFHLPLQEDTYVE------VDLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRV 1786
Cdd:cd01317 310 LIRALSTNPAKILGLPPGRLEVGApadlvlFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1442-1799 |
9.99e-65 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 227.64 E-value: 9.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1442 QIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPalALAQK 1521
Cdd:PRK07575 33 AIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRACAKGGVTSFLEMPNTKPLTTTQA--ALDDK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1522 LAEAGARC--DFTLFLGASSENAGTLGAVAGsAAGLKLYLNETFSELRLDSVAQWMEHF-ETwpsHLPIVAHAERQSV-- 1596
Cdd:PRK07575 111 LARAAEKCvvNYGFFIGATPDNLPELLTANP-TCGIKIFMGSSHGPLLVDEEAALERIFaEG---TRLIAVHAEDQARir 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1597 ---------------------AAVLMVAQLT-------RRSVHICHVARKEEILLIKTAKaqGLPVTCEVAPHHLFLNRE 1648
Cdd:PRK07575 187 arraefagisdpadhsqiqdeEAALLATRLAlklskkyQRRLHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLNTD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1649 DLERLGPgKGEVRPELGSREDMEALWENM--AVIDCFASDHAPHTLEEKCGP--KPPPGFPGLETMLPLLLTAVSEGRLS 1724
Cdd:PRK07575 265 AYERIGT-LAQMNPPLRSPEDNEALWQALrdGVIDFIATDHAPHTLEEKAQPypNSPSGMPGVETSLPLMLTAAMRGKCT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1725 LDDLLQRLHHNPRRIFHLP---LQEDTY----VEVDLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDG 1797
Cdd:PRK07575 344 VAQVVRWMSTAVARAYGIPnkgRIAPGYdadlVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRG 423
|
..
gi 158534057 1798 QV 1799
Cdd:PRK07575 424 QV 425
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1464-1810 |
1.92e-64 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 227.23 E-value: 1.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGAS----- 1538
Cdd:PRK02382 53 LPGGIDVHVHFREPGYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTgnwdp 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1539 -----SENAGTLGAV--AGSAAGLKLYLnETFSEL-----RLDSVA--------------QWMEHFETWPSHLPI-VAHA 1591
Cdd:PRK02382 133 leslwERGVFALGEIfmADSTGGMGIDE-ELFEEAlaeaaRLGVLAtvhaededlfdelaKLLKGDADADAWSAYrPAAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1592 ERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKaqglpVTCEVAPHHLFLNREDLERLGPgKGEVRPELGSREDME 1671
Cdd:PRK02382 212 EAAAVERALEVASETGARIHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGT-FGKMNPPLRSEKRRE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1672 ALWE--NMAVIDCFASDHAPHTLEEKCGPKPPPGFPG--LETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQ-- 1745
Cdd:PRK02382 286 ALWErlNDGTIDVVASDHAPHTREEKDADIWDAPSGVpgVETMLPLLLAAVRKNRLPLERVRDVTAANPARIFGLDGKgr 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158534057 1746 -EDTY----VEVDLEHEWTVPSHMPFSKAHWTPFEGqkVKGTVRRVVL-RGEVAYIDGQVLVPPGYGQDVR 1810
Cdd:PRK02382 366 iAEGYdadlVLVDPDAAREIRGDDLHSKAGWTPFEG--MEGVFPELTMvRGTVVWDGDDINAKRGRGEFLR 434
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
181-355 |
7.74e-64 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 215.56 E-value: 7.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 181 VDCGL--KYNQIRCLCQLGAEVTVVPWNH---ELDSRKYDGLFLSNGPGDPASYPGVVSTLNRVLsePNPRPVFGICLGH 255
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTpaeEILEENPDGIILSGGPGSPGAAGGAIEAIREAR--ELKIPILGICLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 256 QLLALAIGAKTYKM-RYGNRGHNQPC------LLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDNL 328
Cdd:pfam00117 81 QLLALAFGGKVVKAkKFGHHGKNSPVgddgcgLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKL 160
|
170 180
....*....|....*....|....*..
gi 158534057 329 PFFSVQFHPEHRAGPSDMELLFDVFLE 355
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFFIK 187
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1429-1810 |
1.64e-62 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 221.33 E-value: 1.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1429 DIKCTKLFVEALGQIGPAPPLKVhVDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRP 1508
Cdd:PRK09060 24 DIGIRDGRIAAIGDLSGASAGEV-IDC---RGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAAVLGGVTAVFEMPNTNP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1509 PIIDAPALALAQKLAEAGARCDFTLFLGASSENAGTLGAV--AGSAAGLKLYLNETFSELRLD---SVAQWME------- 1576
Cdd:PRK09060 100 LTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELerLPGCAGIKVFMGSSTGDLLVEddeGLRRILRngrrraa 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1577 -HFE---------------TWPSHlPIVahaeRQSVAAVLM------VAQLTRRSVHICHVARKEEILLIKTAKAQglpV 1634
Cdd:PRK09060 180 fHSEdeyrlrerkglrvegDPSSH-PVW----RDEEAALLAtrrlvrLARETGRRIHVLHVSTAEEIDFLADHKDV---A 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1635 TCEVAPHHLFLNREDL-ERLGpGKGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGP--KPPPGFPGLET 1709
Cdd:PRK09060 252 TVEVTPHHLTLAAPECyERLG-TLAQMNPPIRDARHRDGLWRGVRqgVVDVLGSDHAPHTLEEKAKPypASPSGMTGVQT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1710 MLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP--------LQEDTYVeVDLEHEWTVPSHMPFSKAHWTPFEGQKVKG 1781
Cdd:PRK09060 331 LVPIMLDHVNAGRLSLERFVDLTSAGPARIFGIAgkgriavgYDADFTI-VDLKRRETITNEWIASRCGWTPYDGKEVTG 409
|
410 420
....*....|....*....|....*....
gi 158534057 1782 TVRRVVLRGEVAYIDGQVLVPPGyGQDVR 1810
Cdd:PRK09060 410 WPVGTIVRGQRVMWDGELVGPPT-GEPVR 437
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
1461-1803 |
5.04e-58 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 208.68 E-value: 5.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFTLFLGASS 1539
Cdd:cd01315 48 LVVMPGLIDTHVHINEPGRTEWEGFETGTKAAAAGGITTIIDMPlNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1540 ENAGTLGAVAGSAA-GLK----------------LYLNETFSEL------------------RLDSVAQ------WMEHF 1578
Cdd:cd01315 128 GNLDQLRPLDEAGVvGFKcflcpsgvdefpavddEQLEEAMKELaktgsvlavhaenpeiteALQEQAKakgkrdYRDYL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1579 ETWPshlPIvahAERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPgKG 1658
Cdd:cd01315 208 ASRP---VF---TEVEAIQRILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGT-EF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1659 EVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPGFP-----GLETMLPLLLT-AVSEGRLSLDDLLQ 1730
Cdd:cd01315 281 KCAPPIRDAANQEQLWEALEngDIDMVVSDHSPCTPELKLLGKGDFFKAwggisGLQLGLPVMLTeAVNKRGLSLEDIAR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1731 RLHHNPRRIFHLPLQEDT--------YVEVDLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVP 1802
Cdd:cd01315 361 LMCENPAKLFGLSHQKGRiavgydadFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVGE 440
|
.
gi 158534057 1803 P 1803
Cdd:cd01315 441 P 441
|
|
| ArgF |
COG0078 |
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine ... |
1920-2224 |
2.69e-55 |
|
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine carbamoyltransferase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439848 [Multi-domain] Cd Length: 310 Bit Score: 196.04 E-value: 2.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1920 SLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1999
Cdd:COG0078 2 NLKGRHFLSLLDLTPEELRALLDLAAELKAKRKAGIPHRPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIYLDPGDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2000 SVQKGESLADSVQTMSCYADVVVLR-HPQPGAVELaAKHCRRPVINA-GDgvGEHPTQALLDIFTIREELGTVNGMTITM 2077
Cdd:COG0078 82 QLGRGESIKDTARVLSRYVDGIMIRtFGHETLEEL-AKYAGVPVINGlTD--LFHPCQALADLLTIREHFGKLKGLKVAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2078 VGDlkhGRTV-HSLACLLTQYRVSLRYVAPPSLRMPSSVWD----FVASRGTKQEEFESIEEALPDTDVLY------MTR 2146
Cdd:COG0078 159 VGD---GNNVaNSLLLAAAKLGMDVRIATPEGYEPDPEIVAkakeIAAESGGSITITHDPAEAVKGADVVYtdvwvsMGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2147 iQKERfgssQEYEACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEV-DSdPRAAYFRQAENGMYIRMALLATVLG 2223
Cdd:COG0078 236 -EEEA----EERIKAFKPYQVNEELMALAKPDAIFMHCLPahRGEEVTDEViDG-PQSVVFDEAENRLHAQKALLAWLLG 309
|
.
gi 158534057 2224 R 2224
Cdd:COG0078 310 G 310
|
|
| OTCace_N |
pfam02729 |
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain; |
1925-2065 |
3.20e-55 |
|
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
Pssm-ID: 460665 [Multi-domain] Cd Length: 140 Bit Score: 188.79 E-value: 3.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1925 HILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKG 2004
Cdd:pfam02729 1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKLPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSSG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158534057 2005 ESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGdGVGEHPTQALLDIFTIRE 2065
Cdd:pfam02729 81 ESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
801-921 |
1.29e-54 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 186.50 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 801 ELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAKLLEQHRGRPLPQDLLHQAKCLGFSDKQIALAV 880
Cdd:smart01096 4 ELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAKLL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 158534057 881 LSTELVVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTY 921
Cdd:smart01096 84 GVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1464-1799 |
1.57e-53 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 195.09 E-value: 1.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENAG 1543
Cdd:PRK09236 53 LPGMIDDQVHFREPGLTHKGDIASESRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNLD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1544 TLGAV-AGSAAGLKLY---------------LNETFSELRL---------DSVAQWMEHF-ETWPSHLPIVAHAERQSVA 1597
Cdd:PRK09236 133 EIKRLdPKRVCGVKVFmgastgnmlvdnpetLERIFRDAPTliathcedtPTIKANLAKYkEKYGDDIPAEMHPLIRSAE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1598 AVL----MVAQLTRRS---VHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGpGKGEVRPELGSREDM 1670
Cdd:PRK09236 213 ACYksssLAVSLAKKHgtrLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLG-NLIKCNPAIKTASDR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1671 EALWENMA--VIDCFASDHAPHTLEEKcgpkpppGFPGLETM---------LPLLLTAVSEGRLSLDDLLQRLHHNPRRI 1739
Cdd:PRK09236 292 EALRQALAddRIDVIATDHAPHTWEEK-------QGPYFQAPsglplvqhaLPALLELVHEGKLSLEKVVEKTSHAPAIL 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158534057 1740 FHLP----LQEDTY---VEVDLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQV 1799
Cdd:PRK09236 365 FDIKergfIREGYWadlVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQL 431
|
|
| pyrB |
PRK13814 |
aspartate carbamoyltransferase; |
1925-2224 |
2.33e-47 |
|
aspartate carbamoyltransferase;
Pssm-ID: 139876 [Multi-domain] Cd Length: 310 Bit Score: 172.98 E-value: 2.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1925 HILSVKQFTKDQMSHLFNVA-HTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQK 2003
Cdd:PRK13814 7 HLLNMRSLTRDHIEKLIQRAnYFLTQGMEKNSVFETLKGHVVANLFFEPSTRTRNSFEIAAKRLGAMVLNPNLKISAISK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2004 GESLADSVQTMSCYA-DVVVLRHPQPGAVELAAKHCRRPV-INAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDL 2081
Cdd:PRK13814 87 GETLFDTIKTLEAMGvYFFIVRHSENETPEQIAKQLSSGVvINAGDGNHQHPSQALIDLMTIKQHKPHWNKLCVTIIGDI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2082 KHGRTVHSLA-CLLTQYRVSLRYVAPPSLrMPssvwDFVASRGTKQeeFESIEEALPDTDVLYMTRIQKERFGSSQEYEA 2160
Cdd:PRK13814 167 RHSRVANSLMdGLVTMGVPEIRLVGPSSL-LP----DKVGNDSIKK--FTELKPSLLNSDVIVTLRLQKERHDNSVDIDA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158534057 2161 CFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2224
Cdd:PRK13814 240 FRGSFRLTPEKLYSAKPDAIVMHPGPvnREVEINSDVADNQQSVILQQVRNGVAMRMAVLELFLLR 305
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1464-1811 |
2.61e-47 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 177.20 E-value: 2.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENA 1542
Cdd:PRK06189 53 FPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1543 GTLGAVA-GSAAGLKLYLNET-FSELRLDSVAQWMEHFETWPSHLPIVA-HAER-------------------------- 1593
Cdd:PRK06189 133 EHLRELAeAGVIGFKAFMSNSgTDEFRSSDDLTLYEGMKEIAALGKILAlHAESdaltrhlttqarqqgktdvrdylesr 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1594 ------QSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPgKGEVRPELGSR 1667
Cdd:PRK06189 213 pvvaelEAVQRALLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGA-VAKCAPPLRSR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1668 EDMEALWENMAV--IDCFASDHAPHTLEEKCGPKPPPGFPGL---ETMLPLLLT-AVSEGRLSLDDLLQRLHHNPRRIFH 1741
Cdd:PRK06189 292 SQKEELWRGLLAgeIDMISSDHSPCPPELKEGDDFFLVWGGIsggQSTLLVMLTeGYIERGIPLETIARLLATNPAKRFG 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158534057 1742 LPL-------QEDTYVEVDLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVlVPPGYGQDVRK 1811
Cdd:PRK06189 372 LPQkgrlevgADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEV-FPPPRGQLLRP 447
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
1461-1803 |
5.88e-45 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 170.26 E-value: 5.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFTLFLGASS 1539
Cdd:TIGR03178 47 LVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAAGGITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1540 ENAGTLGAVAGSAA-GLKLYLN----ETFSELRLDSVAQWME-----------HFETwPSHL-----------PIVAH-- 1590
Cdd:TIGR03178 127 YNLDDLRELDEAGVvGFKAFLSpsgdDEFPHVDDWQLYKGMRelarlgqlllvHAEN-PAITsalgeeappqgGVGADay 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1591 -------AERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPgKGEVRPE 1663
Cdd:TIGR03178 206 lasrpvfAEVEAIRRTLALAKVTGCRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGT-LAKCAPP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1664 LGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPG---FPGLETMLPLLLTAVSEGR-LSLDDLLQRLHHNPR 1737
Cdd:TIGR03178 285 IRDLANQEGLWEALLngLIDCVVSDHSPCTPDLKRAGDFFKAwggIAGLQSTLDVMFDEAVQKRgLPLEDIARLMATNPA 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158534057 1738 RIFHL-------PLQEDTYVEVDLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1803
Cdd:TIGR03178 365 KRFGLaqkgriaPGKDADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFIGAP 437
|
|
| PRK00779 |
PRK00779 |
ornithine carbamoyltransferase; Provisional |
1920-2222 |
3.53e-44 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 234835 [Multi-domain] Cd Length: 304 Bit Score: 163.72 E-value: 3.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1920 SLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1999
Cdd:PRK00779 1 MLMGRHFLSLDDLSPEELEELLDLAAELKKKRKAGEPHPPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIFLSPRDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2000 SVQKGESLADSVQTMSCYADVVVLR-HPQPGAVELaAKHCRRPVINA-GDgvGEHPTQALLDIFTIREELGTVNGMTITM 2077
Cdd:PRK00779 81 QLGRGEPIEDTARVLSRYVDAIMIRtFEHETLEEL-AEYSTVPVINGlTD--LSHPCQILADLLTIYEHRGSLKGLKVAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2078 VGDlkhGRTV-HSLACLLTQYRVSLRYVAPPSLRMPSSVWDFVA-SRGTKQEEFESIEEALPDTDVLY------Mtriqk 2149
Cdd:PRK00779 158 VGD---GNNVaNSLLLAAALLGFDLRVATPKGYEPDPEIVEKIAkETGASIEVTHDPKEAVKGADVVYtdvwvsM----- 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158534057 2150 erfGSSQEYE---ACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVL 2222
Cdd:PRK00779 230 ---GQEAEAEerlKAFAPYQVNEELMALAKPDAIFMHCLPahRGEEVTDEVIDGPQSVVWDEAENRLHAQKALLAWLL 304
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
1464-1811 |
1.66e-42 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 161.95 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENAG 1543
Cdd:PRK01211 45 LPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1544 TLGAVagsAAGLKLYLNETFSELRLDSVAQWMEHFETwpSHLPIVAHAERQ------------------------SVAAV 1599
Cdd:PRK01211 125 ILDER---SIGLKVYMGGTTNTNGTDIEGGEIKKINE--ANIPVFFHAELSeclrkhqfesknlrdhdlarpiecEIKAV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1600 LMVAQLTRRSVHICHVARKEEIlliktakaqgLPVTCEVAPHHLFLNREdlERLGpGKGEVRPELGSREDMEALWENM-- 1677
Cdd:PRK01211 200 KYVKNLDLKTKIIAHVSSIDVI----------GRFLREVTPHHLLLNDD--MPLG-SYGKVNPPLRDRWTQERLLEEYis 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1678 AVIDCFASDHAPHTLEEKCG-PKPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHL---PLQEDTYVE-- 1751
Cdd:PRK01211 267 GRFDILSSDHAPHTEEDKQEfEYAKSGIIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGIkkgKIEEGYDADfm 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158534057 1752 -VDLEHEWTVPSHMPFSKAHWTPFEGQKVKGTvRRVVLRGEVAyIDGQVLVPPGYGQDVRK 1811
Cdd:PRK01211 347 aFDFTNIKKINDKRLHSKCPVSPFNGFDAIFP-SHVIMRGEVV-IDNYELISERTGKFVPK 405
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
1464-1804 |
1.97e-42 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 161.47 E-value: 1.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPiIDAPAlALAQKLAE--AGARCDFTLFLGA--SS 1539
Cdd:PRK00369 46 LPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPP-LNTPE-AITEKLAEleYYSRVDYFVYSGVtkDP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1540 ENAGTLGavagsAAGLKLY---LNETFSELRLDSVAQW-MEHFEtwpshLPIVAHAER-------QSVAAVLMVAQLTRr 1608
Cdd:PRK00369 124 EKVDKLP-----IAGYKIFpedLEREETFRVLLKSRKLkILHPE-----VPLALKSNRklrrncwYEIAALYYVKDYQN- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1609 sVHICHVARKEEILLiktAKAQGLpvTCEVAPHHLFLNREdlerlGPGKGEVRPELGSREDMEALWENMAVIDCFASDHA 1688
Cdd:PRK00369 193 -VHITHASNPRTVRL---AKELGF--TVDITPHHLLVNGE-----KDCLTKVNPPIRDINERLWLLQALSEVDAIASDHA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1689 PHTLEEKCGPKPPPGF--PGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPlqeDTYVEVDLEHEWTVPS---- 1762
Cdd:PRK00369 262 PHSSFEKLQPYEVCPPgiAALSFTPPFIYTLVSKGILSIDRAVELISTNPARILGIP---YGEIKEGYRANFTVIQfedw 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 158534057 1763 --HMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPG 1804
Cdd:PRK00369 339 rySTKYSKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKG 382
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1313-1438 |
1.11e-41 |
|
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.
Pssm-ID: 238711 [Multi-domain] Cd Length: 116 Bit Score: 149.37 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1313 KNILLTIGSYkNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGEcppqRSILDQLAENHFELV 1392
Cdd:cd01423 1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK----PSLRELLAEGKIDLV 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 158534057 1393 INLSMRGAGGRRLSsfvtkGYRTRRLAADFSVPLIIDIKCTKLFVE 1438
Cdd:cd01423 76 INLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
|
|
| OTCace |
pfam00185 |
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain; |
2074-2221 |
3.20e-38 |
|
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;
Pssm-ID: 425511 [Multi-domain] Cd Length: 154 Bit Score: 140.82 E-value: 3.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2074 TITMVGDlKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPSSVWD----FVASRGTKQEEFESIEEALPDTDVLYMTRIQ- 2148
Cdd:pfam00185 1 KIAYVGD-GHNNVAHSLIIAAAKLGMDVRLATPKGYPPDPEVLDkakkIAEKSGGSIEITDDPAEAVKGADVVYTDVWQs 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158534057 2149 ----KERFgssQEYEAcFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATV 2221
Cdd:pfam00185 80 mgqeKERE---ERLKA-FKPYQVNEELMKLAKKDAIFMHCLPahRGEEVTDDVFDGPRSVVFDQAENRLHAQKALLALL 154
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
1442-1783 |
1.46e-37 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 147.83 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1442 QIGPAPPLKVHVDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQK 1521
Cdd:PRK07369 37 HIDPIPPDTQIIDA---SGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPPLDNPATLARLQQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1522 LAEAGARCDFtLFLGASSENA--------GTLGA--VAGSAAGLKLylnETFSELR--LDSVAQWMEHFETWPSHL---- 1585
Cdd:PRK07369 114 QAQQIPPVQL-HFWGALTLGGqgkqltelAELAAagVVGFTDGQPL---ENLALLRrlLEYLKPLGKPVALWPCDRslag 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1586 ----------------PIVAHAERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNRED 1649
Cdd:PRK07369 190 ngvmregllalrlglpGDPASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1650 LERLGPgkgEVR--PELGSREDMEALWENM--AVIDCFASDHAPHTLEEKCGPKPPPGFPG--LETMLPLLL-TAVSEGR 1722
Cdd:PRK07369 270 LASYDP---NLRldPPLGNPSDRQALIEGVrtGVIDAIAIDHAPYTYEEKTVAFAEAPPGAigLELALPLLWqNLVETGE 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158534057 1723 LSLDDLLQRLHHNPRRIFHLP---LQEDTYVEV---DLEHEWTVPSHMPFSKAHWTPFEGQKVKGTV 1783
Cdd:PRK07369 347 LSALQLWQALSTNPARCLGQEppsLAPGQPAELilfDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRV 413
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
1439-1806 |
2.71e-37 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 147.75 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1439 ALGQ-IGPAPPLKVhVDCmtSQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPA 1515
Cdd:cd01314 28 AIGPnLEAPGGVEV-IDA--TGKYV-LPGGIDPHTHLELPfmGTVTADDFESGTRAAAAGGTTTIIDFAIPNKGQSLLEA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1516 LALAQKLAEAGARCDFTLFLGASSENAGTLG----AVAGSAAGLKLY-------------LNETFSELRL---------- 1568
Cdd:cd01314 104 VEKWRGKADGKSVIDYGFHMIITDWTDSVIEelpeLVKKGISSFKVFmaykgllmvddeeLLDVLKRAKElgalvmvhae 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1569 --DSVAQWMEHFE----TWP-----SHLPIVahaERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCE 1637
Cdd:cd01314 184 ngDVIAELQKKLLaqgkTGPeyhalSRPPEV---EAEATARAIRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVYGE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1638 VAPHHLFLNREDLERLGP-GKGEV-RPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPG-----FPGLE 1708
Cdd:cd01314 261 TCPQYLLLDDSDYWKDWFeGAKYVcSPPLRPKEDQEALWDGLSsgTLQTVGSDHCPFNFAQKARGKDDFTkipngVPGVE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1709 TMLPLLLTA-VSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVE--------VDLEHEWTVPSHMPFSKAHWTPFEGQKV 1779
Cdd:cd01314 341 TRMPLLWSEgVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVgsdadlviWDPNAEKTISADTHHHNVDYNIFEGMKV 420
|
410 420
....*....|....*....|....*..
gi 158534057 1780 KGTVRRVVLRGEVAYIDGQVLVPPGYG 1806
Cdd:cd01314 421 KGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
1442-1811 |
1.32e-35 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 142.91 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1442 QIGP--APPLKVHV-DCmtSQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPAL 1516
Cdd:TIGR02033 28 AVGDnlIPPDAVEViDA--TGKYV-LPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAAGGTTTIIDFVVPEKGSSLTEAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1517 ALAQKLAEAGARCDFTLFLGASSENAGTLG-----AVAGSAAGLKLY-------------LNETFSELRlDSVAQWMEHF 1578
Cdd:TIGR02033 105 ETWHEKAEGKSVIDYGFHMDITHWNDSVLEehipeVKEEGINSFKVFmayknllmvddeeLFEILKRLK-ELGALLQVHA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1579 E-----------------TWPSHLPIV--AHAERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVA 1639
Cdd:TIGR02033 184 EngdiiaelqarmlaqgiTGPEYHALSrpPELEAEAVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETC 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1640 PHHLFLNREDLERLG--PGKGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPGFP------GLET 1709
Cdd:TIGR02033 264 PQYLVLDDTHYDKPGfeGAKYVCSPPLREPEDQDALWSALSsgALQTVGSDHCTFNFAQKKAIGKDDFTKipnggpGVEE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1710 MLPLLLTA-VSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVE--------VDLEHEWTVPSHMPFSKAHWTPFEGQKVK 1780
Cdd:TIGR02033 344 RMSLLFDEgVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVgsdadiviWDPNRTTVISAETHHSNADYNPFEGFKVR 423
|
410 420 430
....*....|....*....|....*....|.
gi 158534057 1781 GTVRRVVLRGEVAYIDGQVLVPPGYGQDVRK 1811
Cdd:TIGR02033 424 GAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| pyrB |
PRK13376 |
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase ... |
1920-2223 |
1.19e-34 |
|
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase regulatory subunit; Provisional
Pssm-ID: 237369 [Multi-domain] Cd Length: 525 Bit Score: 141.44 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1920 SLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLD---ILKGKV-MASMFYEVSTRTSSSFA-AAMARLGGAVLSF 1994
Cdd:PRK13376 4 DFLGRTLAVIEDLSVEEQLFLYEKTRELKQRWYEGEDVSefrIKKRDVgIYIVFVEPSTRTKESFInAAKFHKNVKVNIF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1995 SEATSSVQKGESLADSVQTMSCYAD--VVVLRHPQPG--------AVELAAKH-CRRPV-INAGDGVGEHPTQALLDIFT 2062
Cdd:PRK13376 84 DSEHSSFNKQESYTDTFNMLTGYSDysIFIVRTRLEGvcrlleekVSEFASRNgIEVPAfINAGDGKHEHPTQELLDEFT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2063 IREELGTVNG-MTITMVGDLKHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPSSVWDFVASRGTKQEEFESIEEALPDTD 2140
Cdd:PRK13376 164 FLEQNNFDNSfIHIALVGDLLHGRTVHSKVNGLKIFKnVKVDLIAPEELAMPEHYVEKMKKNGFEVRIFSSIEEYLSQKD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2141 VL---YMTRIQKERFGSsqeyeacfgQFILTPHIMTRA---KKKMV--------VMHPMPRVN---EISVEVDSDPRAAY 2203
Cdd:PRK13376 244 VAkiwYFTRLQLERMGE---------DILEKEHILRKAvtfRKEFLdklpegvkFYHPLPRHKvypTIPTFLDTLPLNGW 314
|
330 340
....*....|....*....|
gi 158534057 2204 FRQAENGMYIRMALLATVLG 2223
Cdd:PRK13376 315 ETQAINGYWVRIVLLSMLGG 334
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1460-1817 |
2.10e-33 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 136.45 E-value: 2.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1460 KLVrLPGLIDVHVHLREP-GGTH-KEDFASGTAAALAGGVTMVC--AMPNTRPPIIDApaLALAQKLAEAGARCD--FTL 1533
Cdd:PRK08323 45 KYV-MPGGIDPHTHMEMPfGGTVsSDDFETGTRAAACGGTTTIIdfALQPKGQSLREA--LEAWHGKAAGKAVIDygFHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1534 FLGASSENAGT-LGAVAgsAAG---LKLYLN-------------ETFSELRL------------DSVAQWMEHFE----T 1580
Cdd:PRK08323 122 IITDWNEVVLDeMPELV--EEGitsFKLFMAykgalmldddellRALQRAAElgalpmvhaengDAIAYLQAKLLaegkT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1581 WPSHLPIV--AHAERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPGKG 1658
Cdd:PRK08323 200 GPEYHALSrpPEVEGEATNRAIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1659 EVR---PELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPP------GFPGLETMLPLLLTA-VSEGRLSLD 1726
Cdd:PRK08323 280 AKYvmsPPLRDKEHQDALWRGLQdgDLQVVATDHCPFCFEQKKQLGRGDftkipnGTPGVEDRMPLLFSEgVMTGRITLN 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1727 DLLQRLHHNPRRIFHLPLQEDTyVEV---------DLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDG 1797
Cdd:PRK08323 360 RFVELTSTNPAKIFGLYPRKGT-IAVgadadiviwDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDG 438
|
410 420
....*....|....*....|
gi 158534057 1798 QVLVPPGYGQDVRKWPQGAV 1817
Cdd:PRK08323 439 EFRGKAGHGRFLKRKPFQAV 458
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
801-877 |
1.57e-32 |
|
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 460695 Cd Length: 79 Bit Score: 121.71 E-value: 1.57e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158534057 801 ELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAKLLEQHrGRPLPQDLLHQAKCLGFSDKQIA 877
Cdd:pfam02787 2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEA-GLDLDAELLREAKRLGFSDRQIA 77
|
|
| PLN02342 |
PLN02342 |
ornithine carbamoyltransferase |
1923-2223 |
3.86e-32 |
|
ornithine carbamoyltransferase
Pssm-ID: 177976 [Multi-domain] Cd Length: 348 Bit Score: 129.91 E-value: 3.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1923 GQHILSVKQFTKDQMSHLFNVAHTLRMMVQK-ERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSV 2001
Cdd:PLN02342 45 PKHFLHIDDFDKEEILGLLDRAKEVKALLKSgDRSFQPFKGKSMAMIFTKPSMRTRVSFETGFFLLGGHALYLGPDDIQL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2002 QKGESLADSVQTMSCYADVVVLR---HPQpgAVELaAKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMV 2078
Cdd:PLN02342 125 GKREETRDIARVLSRYNDIIMARvfaHQD--VLDL-AEYSSVPVINGLTDY-NHPCQIMADALTIIEHIGRLEGTKVVYV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2079 GDlkHGRTVHSLACLLTQYRVSLRYVAPPSLRMPSSVWDfvasrGTKQEEFESIE------EALPDTDVLY------MTr 2146
Cdd:PLN02342 201 GD--GNNIVHSWLLLAAVLPFHFVCACPKGYEPDAKTVE-----KARAAGISKIEitndpaEAVKGADVVYtdvwasMG- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2147 iQKErfgssqEYE---ACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATV 2221
Cdd:PLN02342 273 -QKE------EAEkrkKAFQGFQVNEALMKLAGPQAYFMHCLPaeRGVEVTDGVMEAPNSIVFPQAENRMHAQNAIMLHQ 345
|
..
gi 158534057 2222 LG 2223
Cdd:PLN02342 346 LG 347
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
1443-1794 |
5.97e-31 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 128.26 E-value: 5.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1443 IGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIiDAPALA----- 1517
Cdd:PRK07627 33 IGQAPAGFNADKTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAAVAGGVTSLVCPPDTDPVL-DEPGLVemlkf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1518 LAQKLAEA-----GArcdFTLFLGAS--SENAGTL--GAVAGSAAGLKLYLNE----------TFS-ELRLDSVAQWM-- 1575
Cdd:PRK07627 112 RARNLNQAhvyplGA---LTVGLKGEvlTEMVELTeaGCVGFSQANVPVVDTQvllralqyasTFGfTVWLRPLDAFLgr 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1576 ---EHFETWPSHL---PIVAHAERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNRED 1649
Cdd:PRK07627 189 ggvAASGAVASRLglsGVPVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1650 LERLGPgKGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCG--PKPPPGFPGLETMLPLLLTAVSEGRLSL 1725
Cdd:PRK07627 269 IGYFDS-QFRLDPPLRSQRDREAIRAALAdgTIDAICSDHTPVDDDEKLLpfAEATPGATGLELLLPLTLKWADEAKVPL 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158534057 1726 DDLLQRLHHNPRRIFHLP---LQEDTYVEV---DLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAY 1794
Cdd:PRK07627 348 ARALARITSAPARVLGLPagrLAEGAPADLcvfDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAF 422
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
1460-1811 |
1.23e-30 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 128.28 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1460 KLVrLPGLIDVHVHLREPGGT---HKEDFASGTAAALAGGVTMVC--AMPNTRPPIIDApaLALAQKLAEAGARCDFTLF 1534
Cdd:PRK13404 50 RLV-LPGGVDSHCHIDQPSGDgimMADDFYTGTVSAAFGGTTTVIpfAAQHRGQSLREA--VEDYHRRAAGKAVIDYAFH 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1535 LGASSENAGTLG-----AVAGSAAGLKLYLneTFSELRLD--------SVAQ-----------------WM-----EHFE 1579
Cdd:PRK13404 127 LIVADPTEEVLTeelpaLIAQGYTSFKVFM--TYDDLKLDdrqildvlAVARrhgamvmvhaenhdmiaWLtkrllAAGL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1580 TWPSH----LPIVAhaERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERlgP 1655
Cdd:PRK13404 205 TAPKYhaisRPMLA--EREATHRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDR--P 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1656 G----KGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKPPPGFPG----------LETMLPLLLTA-V 1718
Cdd:PRK13404 281 GmegaKYICSPPPRDKANQEAIWNGLAdgTFEVFSSDHAPFRFDDTDGKLAAGANPSfkaiangipgIETRLPLLFSEgV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1719 SEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYV---EVDL-----EHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRG 1790
Cdd:PRK13404 361 VKGRISLNRFVALTSTNPAKLYGLYPRKGAIAigaDADIaiwdpDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRG 440
|
410 420
....*....|....*....|.
gi 158534057 1791 EVAYIDGQVLVPPGYGQDVRK 1811
Cdd:PRK13404 441 RVVVEDGELVAERGSGQFLAR 461
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
1453-1794 |
7.85e-29 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 122.07 E-value: 7.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1453 VDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPpIIDAPAL---------------- 1516
Cdd:PRK09059 51 VDC---AGKAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMPDTDP-VIDDVALvefvkrtardtaivni 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1517 ----ALAQKLA-----------EAGARCdFTLflGASS-ENAGTLGAVAGSAAGLK-LYLNETFSElrlDSVAQWMEH-- 1577
Cdd:PRK09059 127 hpaaAITKGLAgeemtefgllrAAGAVA-FTD--GRRSvANTQVMRRALTYARDFDaVIVHETRDP---DLGGNGVMNeg 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1578 -FETWPSHLPIVAHAERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLerlgpg 1656
Cdd:PRK09059 201 lFASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVSINHLSLNENDI------ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1657 kGEVR------PELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCG--PKPPPGFPGLETMLPLLLTAVSEGRLSLD 1726
Cdd:PRK09059 275 -GEYRtffklsPPLRTEDDRVAMVEAVAsgTIDIIVSSHDPQDVDTKRLpfSEAAAGAIGLETLLAAALRLYHNGEVPLL 353
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158534057 1727 DLLQRLHHNPRRIFHLP---LQEDTYVE---VDLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAY 1794
Cdd:PRK09059 354 RLIEALSTRPAEIFGLPagtLKPGAPADiivIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVY 427
|
|
| PLN02795 |
PLN02795 |
allantoinase |
1462-1797 |
8.41e-29 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 123.35 E-value: 8.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1462 VRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSE 1540
Cdd:PLN02795 96 VVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1541 NAGTLGA----VAGSAAGLKLYL-NETFSELRLDSVAQWMEHFETWPSH-LPIVAHAERQS------------------- 1595
Cdd:PLN02795 176 NAHNASVleelLDAGALGLKSFMcPSGINDFPMTTATHIKAALPVLAKYgRPLLVHAEVVSpvesdsrldadprsystyl 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1596 -----------VAAVLMVAQLTRR-------SVHICHVARKEEIL-LIKTAKAQGLPVTCEVAPHHLFLNREDLerlgpG 1656
Cdd:PLN02795 256 ksrppsweqeaIRQLLEVAKDTRPggvaegaHVHIVHLSDAESSLeLIKEAKAKGDSVTVETCPHYLAFSAEEI-----P 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1657 KGEVR----PELGSREDMEALWENMA--VIDCFASDHAPHT-----LEEKCGPKPPPGFPGLETMLPLLLTAVSEGRLSL 1725
Cdd:PLN02795 331 DGDTRykcaPPIRDAANRELLWKALLdgDIDMLSSDHSPSPpdlklLEEGNFLRAWGGISSLQFVLPATWTAGRAYGLTL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1726 DDLLQRLHHNPRRIFHLPL--------QEDtYVEVDLEHEWTVPSHMPFSKAH--WTPFEGQKVKGTVRRVVLRGEVAYI 1795
Cdd:PLN02795 411 EQLARWWSERPAKLAGLDSkgaiapgkDAD-IVVWDPEAEFVLDESYPIYHKHksLSPYLGTKLSGKVIATFVRGNLVFL 489
|
..
gi 158534057 1796 DG 1797
Cdd:PLN02795 490 EG 491
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1454-1794 |
3.56e-26 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 114.57 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1454 DCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFT 1532
Cdd:PRK08044 42 EVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1533 LFLGASSENAGTLGAV-AGSAAGLKLYLnETFSELRLDS----VAQW----------------MEHFETWP--------- 1582
Cdd:PRK08044 122 QLGGLVSYNLDRLHELdEVGVVGFKCFV-ATCGDRGIDNdfrdVNDWqfykgaqklgelgqpvLVHCENALicdelgeea 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1583 -SHLPIVAHA---------ERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLER 1652
Cdd:PRK08044 201 kREGRVTAHDyvasrpvftEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1653 LGPgKGEVRPELGSREDMEALWENM--AVIDCFASDHAPHTLEEKCGPKPPP--GFPGLETMLPLLL-TAVSEGRLSLDD 1727
Cdd:PRK08044 281 IGT-LAKCSPPIRDLENQKGMWEKLfnGEIDCLVSDHSPCPPEMKAGNIMEAwgGIAGLQNCMDVMFdEAVQKRGMSLPM 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1728 LLQRLHHNPRRIFHLP---------------LQEDTYVEV---DLEHEWTVpshmpfskahwTPFEGQKVKGTVRRVVLR 1789
Cdd:PRK08044 360 FGKLMATNAADIFGLQqkgriapgkdadfvfIQPNSSYVLkneDLEYRHKV-----------SPYVGRTIGARITKTILR 428
|
....*
gi 158534057 1790 GEVAY 1794
Cdd:PRK08044 429 GDVIY 433
|
|
| PRK14805 |
PRK14805 |
ornithine carbamoyltransferase; Provisional |
1924-2223 |
6.00e-26 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 237819 [Multi-domain] Cd Length: 302 Bit Score: 110.55 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1924 QHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSldILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQK 2003
Cdd:PRK14805 2 KHLLSIKELTQQQLLDLLALAKTIKANPAEYRQ--ALAGKSVVMLFEKPSLRTRVSFDIGINKLGGHCLYLDQQNGALGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2004 GESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGDlkh 2083
Cdd:PRK14805 80 RESVADFAANLSCWADAIVARVFSHSTIEQLAEHGSVPVINALCDL-YHPCQALADFLTLAEQFGDVSKVKLAYVGD--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2084 GRTV-HSL----ACLLTQYRVslryVAP----PSLRMPSSVWDFVASRGTKQEEFESIeEALPDTDVLYM-TRIQKERFG 2153
Cdd:PRK14805 156 GNNVtHSLmygaAILGATMTV----ICPpghfPDGQIVAEAQELAAKSGGKLVLTSDI-EAIEGHDAIYTdTWISMGDDT 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158534057 2154 SSQEYEACFGQFILTPHIMTRAKKKMvVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2223
Cdd:PRK14805 231 PLAEIKAKFAPYQVNKALMEKAGATF-VMHCQPahRGVEITSEVMDGEGSLILQQAENRMHAQNAVLVTLLS 301
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
187-338 |
4.04e-25 |
|
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: 104.54 E-value: 4.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 187 YNQIRCLCQLGAEVTVVPWNH----ELDSRKYDGLFLSNGPGDPASYPGVVSTLNRVLSEpnpRPVFGICLGHQLLALAI 262
Cdd:cd01743 12 YNLVQYLRELGAEVVVVRNDEitleELELLNPDAIVISPGPGHPEDAGISLEIIRALAGK---VPILGVCLGHQAIAEAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 263 GAKTYKMRYGNRG------HNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWapLFTNANDcsnEGIV----HDNLPFFS 332
Cdd:cd01743 89 GGKVVRAPEPMHGktseihHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLL--EVTASTE---DGVImalrHRDLPIYG 163
|
....*.
gi 158534057 333 VQFHPE 338
Cdd:cd01743 164 VQFHPE 169
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
1029-1247 |
1.87e-23 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 102.26 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1029 RQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLE 1108
Cdd:COG0439 36 AEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1109 RFL----SSAAAVSKEHPVVISKFIqEAKEIDVDAVACDGIVSAIAISEHvENAGVHSGDATLVTPPqDITPKTLERIKA 1184
Cdd:COG0439 116 AALaearAEAKAGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158534057 1185 IVHAVGQELQV-TGPFNLQ-LIAKDDQLKVIECNVRVS--RSFPFVSKTLGVDLVALATRIIMGEKV 1247
Cdd:COG0439 193 LVARALRALGYrRGAFHTEfLLTPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEPR 259
|
|
| PRK02102 |
PRK02102 |
ornithine carbamoyltransferase; Validated |
1921-2223 |
2.88e-23 |
|
ornithine carbamoyltransferase; Validated
Pssm-ID: 179366 [Multi-domain] Cd Length: 331 Bit Score: 103.43 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1921 LVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSS 2000
Cdd:PRK02102 5 LKGRSFLKLLDFTPEEIEYLIDLSIELKAAKKAGIEHQYLEGKNIALIFEKTSTRTRCAFEVAAIDLGAHVTYLGPNDSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2001 VQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGD 2080
Cdd:PRK02102 85 LGKKESIEDTARVLGRMYDGIEYRGFKQEIVEELAKYSGVPVWNGLTDE-WHPTQMLADFMTMKEHFGPLKGLKLAYVGD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2081 lkhGR--TVHSL---ACLLTqyrVSLRYVAPPSLRmPSS-----VWDFVASRGTKQEEFESIEEALPDTDVLYmTRI--- 2147
Cdd:PRK02102 164 ---GRnnMANSLmvgGAKLG---MDVRICAPKELW-PEEelvalAREIAKETGAKITITEDPEEAVKGADVIY-TDVwvs 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2148 ---QKERfgssQEYEACFGQFILTPHIMTR-AKKKMVVMHPMP-----------------RVNEISV--EVDSDPRAAYF 2204
Cdd:PRK02102 236 mgeEDEW----EERIKLLKPYQVNMDLMKAtGNPDVIFMHCLPafhdtetkvgkeiaekyGLKGLEVtdEVFESKYSIVF 311
|
330
....*....|....*....
gi 158534057 2205 RQAENGMYIRMALLATVLG 2223
Cdd:PRK02102 312 DEAENRMHTIKAVMVATLG 330
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
1048-1248 |
1.51e-22 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 97.76 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1048 RFKFSRLLDTIGISQPQW--RELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKE----H 1121
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgnP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1122 PVVISKFIQEAKEIDVDAVAcDGIVSAIAISEhVENA-GVHSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFN 1200
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLR-DAHGNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 158534057 1201 LQLI--AKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVE 1248
Cdd:pfam02786 160 VEFAldPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
460-714 |
1.80e-21 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 96.48 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 460 VTQVIRNERPDGILltfggqtALNCGVELTKAGVLARYGVRvlGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLE 539
Cdd:COG0439 9 AAELARETGIDAVL-------SESEFAVETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 540 QAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELSALV------APAFAHTSQVLIDKSLKGwKEIEYE-VVRDayGNC 612
Cdd:COG0439 80 EALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALaearaeAKAGSPNGEVLVEEFLEG-REYSVEgLVRD--GEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 613 VtVCNM---ENLDPLGIHTGEsivVAPSQtLNDREYQLLRRTAIKVTQHLGIV-GECNVQYALNPESEqYYIIEVNARLS 688
Cdd:COG0439 157 V-VCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGE-PYLIEINARLG 230
|
250 260
....*....|....*....|....*...
gi 158534057 689 --RSSALASKATGYPLAYVAAKLALGIP 714
Cdd:COG0439 231 geHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
1467-1739 |
2.75e-21 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 96.25 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1467 LIDVHVHLREPGGTH------------------KEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGAR 1528
Cdd:cd01292 1 FIDTHVHLDGSALRGtrlnlelkeaeelspedlYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1529 CDFTLFLGASSENAGTLG------------AVAGSAAGLKLYLNETFSELrldSVAQWMEHFETWPSH-LPIVAHAERQS 1595
Cdd:cd01292 81 IRVVLGLGIPGVPAAVDEdaealllellrrGLELGAVGLKLAGPYTATGL---SDESLRRVLEEARKLgLPVVIHAGELP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1596 VA--AVLMVAQLTRR--SVHICHVARKEEILLIKTAKAQglpVTCEVAPHHLFLNREDlerlgpgkgevrpelgsREDME 1671
Cdd:cd01292 158 DPtrALEDLVALLRLggRVVIGHVSHLDPELLELLKEAG---VSLEVCPLSNYLLGRD-----------------GEGAE 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158534057 1672 ALWENMA--VIDCFASDHAPHTLEekcgpkpppgfpglETMLPLLLTAVSEGRL--SLDDLLQRLHHNPRRI 1739
Cdd:cd01292 218 ALRRLLElgIRVTLGTDGPPHPLG--------------TDLLALLRLLLKVLRLglSLEEALRLATINPARA 275
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1327-1427 |
1.08e-19 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 85.62 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1327 ELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEA-VDGECppqrSILDQLAENHFELVINLSMRGAGGRRl 1405
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEGrPGGRV----QIGDLIKNGEIDLVINTLYPFKATVH- 75
|
90 100
....*....|....*....|..
gi 158534057 1406 ssfvtKGYRTRRLAADFSVPLI 1427
Cdd:pfam02142 76 -----DGYAIRRAAENIDIPGP 92
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
177-351 |
7.14e-19 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 87.69 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 177 RIFAVDCGLKYNQI-----RCLCQLGAEVTVV--------PWNHELDSrkYDGLFLSNGPG---DPASYPGVVSTLNRVL 240
Cdd:COG0518 1 KILILDHDPFGGQYpgliaRRLREAGIELDVLrvyageilPYDPDLED--PDGLILSGGPMsvyDEDPWLEDEPALIREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 241 SEPNpRPVFGICLGHQLLALAIGAKTYKMRYGNRG------HNQPCLLVGTGRCFLTSQNHGFAVDAdsLPAGWAPLFTN 314
Cdd:COG0518 79 FELG-KPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelTEADPLFAGLPDEFTVWMSHGDTVTE--LPEGAEVLASS 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 158534057 315 ANdCSNEGIVHDNlPFFSVQFHPEhrAGPSDMELLFD 351
Cdd:COG0518 156 DN-CPNQAFRYGR-RVYGVQFHPE--VTHTMMEAWLE 188
|
|
| PRK04284 |
PRK04284 |
ornithine carbamoyltransferase; Provisional |
1920-2224 |
1.38e-17 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 235269 [Multi-domain] Cd Length: 332 Bit Score: 86.34 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1920 SLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1999
Cdd:PRK04284 3 NLRNRSFLTLLDFTPKEIEYLLDLSEDLKRAKYAGIEVQKLKGKNIALIFEKDSTRTRCAFEVAAYDQGAHVTYLGPTGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2000 SVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINaGDGVGEHPTQALLDIFTIREEL-GTVNGMTITMV 2078
Cdd:PRK04284 83 QMGKKESTKDTARVLGGMYDGIEYRGFSQRTVETLAEYSGVPVWN-GLTDEDHPTQVLADFLTAKEHLkKPYKDIKFTYV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2079 GDlkhGRTVHSLACLLTQYRVSLRY--VAPPSLRMPSSVWD----FVASRGTKQEEFESIEEALPDTDVLYM-------- 2144
Cdd:PRK04284 162 GD---GRNNVANALMQGAAIMGMDFhlVCPKELNPDDELLNkckeIAAETGGKITITDDIDEGVKGSDVIYTdvwvsmge 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2145 -TRIQKERFGSSQEYEacfgqfiLTPHIMTRAKKKMVV-MHPMPRVN-------------------EISVEVDSDPRAAY 2203
Cdd:PRK04284 239 pDEVWEERIKLLKPYQ-------VNKEMMKKTGNPNAIfEHCLPSFHdldtkvgkeifekyglkemEVTDEVFESKASVV 311
|
330 340
....*....|....*....|.
gi 158534057 2204 FRQAENGMYIRMALLATVLGR 2224
Cdd:PRK04284 312 FDEAENRMHTIKAVMVATLGE 332
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
187-338 |
3.69e-17 |
|
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440278 [Multi-domain] Cd Length: 189 Bit Score: 81.62 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 187 YNQIRCLCQLGAEVTVVPWNH----ELDSRKYDGLFLSNGPGDPASyPGVvstLNRVLSEPNPR-PVFGICLGHQLLALA 261
Cdd:COG0512 12 YNLVQYLGELGAEVVVVRNDEitleEIEALAPDGIVLSPGPGTPEE-AGI---SLEVIRAFAGKiPILGVCLGHQAIGEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 262 IGAKTYKMRY------------GN---RGHNQPcLLVgtGRcfltsqNHGFAVDADSLPagwAPLFTNANDCSNE--GIV 324
Cdd:COG0512 88 FGGKVVRAPEpmhgktspithdGSglfAGLPNP-FTA--TR------YHSLVVDRETLP---DELEVTAWTEDGEimGIR 155
|
170
....*....|....
gi 158534057 325 HDNLPFFSVQFHPE 338
Cdd:COG0512 156 HRELPIEGVQFHPE 169
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
395-717 |
2.10e-16 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 82.62 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 395 KVLILGSGGlsigqagefdysGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLP-IT-PHYVTQVI---RNERP 469
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPkVTdPNYIDRLLdicKKEKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 470 DGILLTFGgqtalncgVELtkaGVLARY-------GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQ 542
Cdd:PRK12767 71 DLLIPLID--------PEL---PLLAQNrdrfeeiGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 543 AA--AERLGYPVLVRAAFALGGLGSGFASTKEELSalvaPAFAHTSQVLIDKSLKGwKEIEYEVVRDAYGNCVTVCNMEN 620
Cdd:PRK12767 140 AAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 621 LDPLGIHTGESIVVapsqtlndrEYQLLRRTAIKVTQHLGIVGECNVQYALNPesEQYYIIEVNARLSrssalaskaTGY 700
Cdd:PRK12767 215 IEVRAGETSKGVTV---------KDPELFKLAERLAEALGARGPLNIQCFVTD--GEPYLFEINPRFG---------GGY 274
|
330 340
....*....|....*....|....*.
gi 158534057 701 PLAYVA---------AKLALGIPLPE 717
Cdd:PRK12767 275 PLSYMAganepdwiiRNLLGGENEPI 300
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
178-349 |
8.81e-16 |
|
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: 77.74 E-value: 8.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 178 IFAVDCGLKYNQI--RCLCQLGAEVTVVPWN---HELDSRKYDGLFLSNGP-----GDPASYPGVVSTLNRvlsepnprP 247
Cdd:TIGR00888 1 ILVLDFGSQYTQLiaRRLRELGVYSELVPNTtplEEIREKNPKGIILSGGPssvyaENAPRADEKIFELGV--------P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 248 VFGICLGHQLLALAIG---AKTYKMRYGN---RGHNQPCLLVGTGRCFLTSQNHGFAVDAdsLPAGWAPLFTNANdCSNE 321
Cdd:TIGR00888 73 VLGICYGMQLMAKQLGgevGRAEKREYGKaelEILDEDDLFRGLPDESTVWMSHGDKVKE--LPEGFKVLATSDN-CPVA 149
|
170 180
....*....|....*....|....*...
gi 158534057 322 GIVHDNLPFFSVQFHPEHRAGPSDMELL 349
Cdd:TIGR00888 150 AMAHEEKPIYGVQFHPEVTHTEYGNELL 177
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
187-338 |
4.12e-15 |
|
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: 75.60 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 187 YNQIRCLCQLGAEVtVVPWNH-----ELDSRKYDGLFLSNGPGDPASyPGVVSTLNRVLSepNPRPVFGICLGHQLLALA 261
Cdd:TIGR00566 13 YNLVQYFCELGAEV-VVKRNDsltlqEIEALLPLLIVISPGPCTPNE-AGISLEAIRHFA--GKLPILGVCLGHQAMGQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 262 IGAKTYKMRYGNRG------HNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDNLPFFSVQF 335
Cdd:TIGR00566 89 FGGDVVRANTVMHGktseieHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQF 168
|
...
gi 158534057 336 HPE 338
Cdd:TIGR00566 169 HPE 171
|
|
| PRK03515 |
PRK03515 |
ornithine carbamoyltransferase subunit I; Provisional |
1914-2222 |
5.61e-15 |
|
ornithine carbamoyltransferase subunit I; Provisional
Pssm-ID: 179587 [Multi-domain] Cd Length: 336 Bit Score: 78.60 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1914 MSPLLHslvgQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLS 1993
Cdd:PRK03515 1 MNQFYQ----RHFLRLLDFTPAELNSLLQLAAKLKADKKNGKEEQKLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1994 FSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINagdGVGE--HPTQALLDIFTIREEL--GT 2069
Cdd:PRK03515 77 LGPSGSQIGHKESIKDTARVLGRMYDGIQYRGYGQEIVETLAEYAGVPVWN---GLTNefHPTQLLADLLTMQEHLpgKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2070 VNGMTITMVGDLKH--GRTVHSLACLLTqyrVSLRYVAP----PSLRMPSSVWDFVASRGTKQEEFESIEEALPDTDVLY 2143
Cdd:PRK03515 154 FNEMTLAYAGDARNnmGNSLLEAAALTG---LDLRLVAPkacwPEAALVTECRALAQKNGGNITLTEDIAEGVKGADFIY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2144 M---------TRIQKERFGSSQEYEACFGQFILT--PHI------------MTRAKKKMVVMHPMPRVNEISVEVDSDPR 2200
Cdd:PRK03515 231 TdvwvsmgepKEVWAERIALLRPYQVNSKMMQLTgnPQVkflhclpafhddQTTLGKKMAEEYGLHGGMEVTDEVFESAH 310
|
330 340
....*....|....*....|...
gi 158534057 2201 AAYFRQAENGMY-IRMALLATVL 2222
Cdd:PRK03515 311 SIVFDQAENRLHtIKAVMVATLS 333
|
|
| PRK12562 |
PRK12562 |
ornithine carbamoyltransferase subunit F; Provisional |
1914-2224 |
5.89e-15 |
|
ornithine carbamoyltransferase subunit F; Provisional
Pssm-ID: 105755 Cd Length: 334 Bit Score: 78.56 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1914 MSPLLHslvgQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLS 1993
Cdd:PRK12562 1 MSGFYK----KHFLKLLDFTPAELNSLLQLAAKLKADKKNGKEVARLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1994 FSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINaGDGVGEHPTQALLDIFTIREEL--GTVN 2071
Cdd:PRK12562 77 LGPSGSQIGHKESIKDTARVLGRMYDGIQYRGHGQEVVETLAEYAGVPVWN-GLTNEFHPTQLLADLLTMQEHLpgKAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2072 GMTITMVGDLKH--GRTVHSLACLLTqyrVSLRYVAP----PSLRMPSSVWDFVASRGTKQEEFESIEEALPDTDVLY-- 2143
Cdd:PRK12562 156 EMTLVYAGDARNnmGNSMLEAAALTG---LDLRLVAPqacwPEASLVAECSALAQKHGGKITLTEDIAAGVKGADFIYtd 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2144 ----MTRIQK---ERFGSSQEYEACFGQFILT--PHI------------MTRAKKKMVVMHPMPRVNEISVEVDSDPRAA 2202
Cdd:PRK12562 233 vwvsMGEPKEkwaERIALLRGYQVNSKMMALTgnPQVkflhclpafhddQTTLGKKMAKEFGLHGGMEVTDEVFESPASI 312
|
330 340
....*....|....*....|..
gi 158534057 2203 YFRQAENGMYIRMALLATVLGR 2224
Cdd:PRK12562 313 VFDQAENRMHTIKAVMVATLAK 334
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1026-1248 |
7.60e-15 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 78.00 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1026 ALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQT--VGYPCVVRPSYVLSGAAMNVAYT 1103
Cdd:PRK12767 90 RFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKgeLQFPLFVKPRDGSASIGVFKVND 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1104 DGDLERFLSSAAavskehPVVISKFIQEaKEIDVDA-VACDGIVSAIAISEHVEnagVHSGDATlvtppQDITPKTLERI 1182
Cdd:PRK12767 170 KEELEFLLEYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGETS-----KGVTVKDPELF 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158534057 1183 KAIVHaVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFvSKTLGVDLVALATRIIMGEKVE 1248
Cdd:PRK12767 235 KLAER-LAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL-SYMAGANEPDWIIRNLLGGENE 298
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
190-340 |
1.26e-14 |
|
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: 74.20 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 190 IRCLCQLGAEVTVVPWN---HELDSRKYDGLFLSNGPGDP--ASYPGVVST---LNRVLSEPnpRPVFGICLGHQLLALA 261
Cdd:cd01741 20 LREAGAETIEIDVVDVYageLLPDLDDYDGLVILGGPMSVdeDDYPWLKKLkelIRQALAAG--KPVLGICLGHQLLARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 262 IGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDA--------DSLPAGWAPLFTNAnDCSNEGI-VHDNlpFFS 332
Cdd:cd01741 98 LGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPVfhwhgdtvVELPPGAVLLASSE-ACPNQAFrYGDR--ALG 174
|
....*...
gi 158534057 333 VQFHPEHR 340
Cdd:cd01741 175 LQFHPEER 182
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
493-717 |
2.92e-14 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 77.48 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 493 VLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFAST 570
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDGAlKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 571 KEEL--SALVAPAFAHTS----QVLIDKSLKGWKEIEYEVVRDAYGNCVTV----CNMENldplgiHTGESIVVAPSQTL 640
Cdd:PRK08462 176 ESDLenLYLAAESEALSAfgdgTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVL 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158534057 641 NDREYQLLRRTAIKVTQHLGIVGECNVQYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPE 717
Cdd:PRK08462 250 DEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPS 325
|
|
| PRK14804 |
PRK14804 |
ornithine carbamoyltransferase; Provisional |
1924-2222 |
3.12e-14 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 173265 [Multi-domain] Cd Length: 311 Bit Score: 75.83 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1924 QHILSVKQFTKDQMSHLFNVAhtlrMMVQKERS--LDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSV 2001
Cdd:PRK14804 7 KHLISWEDWSDSEILDLLDFA----VHVKKNRVnyAGHMSGRSLAMLFQKTSTRTRVSFEVAMTEMGGHGIYLDWMASNF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2002 QkgesLAD---SVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGeHPTQALLDIFTIREELGTV--NGMTIT 2076
Cdd:PRK14804 83 Q----LSDidlEARYLSRNVSVIMARLKKHEDLLVMKNGSQVPVINGCDNMF-HPCQSLADIMTIALDSPEIplNQKQLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2077 MVGdlKHGRTVHSLACLLTQYRVSLRYVAPPSLR--MPSSVWDFVASRGTKQEEfESIEEALPDTDVLYMTRIQKERFGS 2154
Cdd:PRK14804 158 YIG--VHNNVVNSLIGITAALGIHLTLVTPIAAKenIHAQTVERAKKKGTLSWE-MNLHKAVSHADYVYTDTWLDMEFFN 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158534057 2155 SQEYEACFGQFI--LTPH-----IMTRAKKKmvVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVL 2222
Cdd:PRK14804 235 DPSYADKKKQRMelMMPYqinssLMEKTNAK--VMHDMPihAGYEITREVVLSDRSIIFQQAENRLDAQKAVILKLL 309
|
|
| PRK01713 |
PRK01713 |
ornithine carbamoyltransferase; Provisional |
1920-2222 |
1.10e-13 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 167263 [Multi-domain] Cd Length: 334 Bit Score: 74.64 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1920 SLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1999
Cdd:PRK01713 4 NLKNRHLLSLVNHTEREIKYLLDLSRDLKRAKYAGTEQQRLKGKNIALIFEKTSTRTRCAFEVAAYDQGAQVTYIDPNSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2000 SVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINagdGVGE--HPTQALLDIFTIREELGT-VNGMTIT 2076
Cdd:PRK01713 84 QIGHKESMKDTARVLGRMYDAIEYRGFKQSIVNELAEYAGVPVFN---GLTDefHPTQMLADVLTMIENCDKpLSEISYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2077 MVGDLKHGRTvHSLACLLTQYRVSLRYVAPPSL----RMPSSVWDFVASRGTKQEEFESIEEALPDTDVlymtrIQKERF 2152
Cdd:PRK01713 161 YIGDARNNMG-NSLLLIGAKLGMDVRICAPKALlpeaSLVEMCEKFAKESGARITVTDDIDKAVKGVDF-----VHTDVW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2153 GSSQEYEACFGQFI-------LTPHIMTR-AKKKMVVMHPMPRVN---------------------EISVEVDSDPRAAY 2203
Cdd:PRK01713 235 VSMGEPLETWGERIkllmpyqVTPELMKRtGNPKVKFMHCLPAFHnsetkvgrqiaekypelangiEVTEDVFESPMNIA 314
|
330
....*....|....*....
gi 158534057 2204 FRQAENGMYIRMALLATVL 2222
Cdd:PRK01713 315 FEQAENRMHTIKAVMVASL 333
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
391-724 |
1.20e-13 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 74.96 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 391 PPPRKVLILGS--GGLSIgqagefdysgsqaIKALKEENIQTLLInpniATVQTSQGL----ADKVYFLPITPH------ 458
Cdd:COG3919 3 TMRFRVVVLGGdiNALAV-------------ARSLGEAGVRVIVV----DRDPLGPAArsryVDEVVVVPDPGDdpeafv 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 459 -YVTQVIRNERPDgILLTFGGQTALncgveltkagVLARY------GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP 531
Cdd:COG3919 66 dALLELAERHGPD-VLIPTGDEYVE----------LLSRHrdeleeHYRLPYPDADLLDRLLDKERFYELAEELGVPVPK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 532 SEAANSLEQAQAAAERLGYPVLVRAA--------FALGGLGSGFASTKEELSALVAPAFAHTSQVLIDKSLKGWKEIEY- 602
Cdd:COG3919 135 TVVLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAGYELIVQEYIPGDDGEMRg 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 603 -EVVRDAYGNCVTVCNMENL--DPLGIhtGESIVVapsQTLNDREyqlLRRTAIKVTQHLGIVGECNVQYALNPESEQYY 679
Cdd:COG3919 215 lTAYVDRDGEVVATFTGRKLrhYPPAG--GNSAAR---ESVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYK 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 158534057 680 IIEVNARLSRSSALASKAtGYPLAYVAAKLALGIPLPELRNSVTG 724
Cdd:COG3919 287 LIEINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREG 330
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
187-355 |
1.85e-13 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 71.05 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 187 YNQIRCLCQLGAEVtVVPWNHELDSRKYDGL-----FLSNGPGDPaSYPGVvsTLNRVLSEPNPRPVFGICLGHQLLALA 261
Cdd:PRK06774 13 YNLYQYFCELGTEV-MVKRNDELQLTDIEQLapshlVISPGPCTP-NEAGI--SLAVIRHFADKLPILGVCLGHQALGQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 262 IGAKTYKMRYGNRG------HNQPCLLVGTGRCFLTSQNHGFAVDADSLPA-----GWAPLFTNANDCSneGIVHDNLPF 330
Cdd:PRK06774 89 FGARVVRARQVMHGktsaicHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGcfeltAWSERGGEMDEIM--GIRHRTLPL 166
|
170 180
....*....|....*....|....*
gi 158534057 331 FSVQFHPEHRAGPSDMELLfDVFLE 355
Cdd:PRK06774 167 EGVQFHPESILSEQGHQLL-DNFLK 190
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
498-716 |
2.38e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 74.68 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 498 GVRVLGTPVETIELTEDRraFAAR--MAEIGEHVAP--SEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEE 573
Cdd:PRK06111 99 GIVFIGPSADIIAKMGSK--IEARraMQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 574 LSAlvapAFAHTSQ----------VLIDKSLKGWKEIEYEVVRDAYGNCVtvcnmenldplgiHTGE---SI------VV 634
Cdd:PRK06111 177 LTK----AFESNKKraanffgngeMYIEKYIEDPRHIEIQLLADTHGNTV-------------YLWErecSVqrrhqkVI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 635 --APSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYaLNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALG 712
Cdd:PRK06111 240 eeAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEF-LVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAG 318
|
....
gi 158534057 713 IPLP 716
Cdd:PRK06111 319 EKLS 322
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1327-1427 |
2.46e-13 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 67.50 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1327 ELLPTVRLLESLGYSLYASLGTADFYTEHGVKV--TAVDWHFEEavdgecppQRSILDQLAENHFELVINLSMRGAggrr 1404
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVvkTLHPKVHGG--------IPQILDLIKNGEIDLVINTLYPFE---- 68
|
90 100
....*....|....*....|...
gi 158534057 1405 lSSFVTKGYRTRRLAADFSVPLI 1427
Cdd:smart00851 69 -AQAHEDGYSIRRAAENIDIPGP 90
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
491-716 |
2.49e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 74.75 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 491 AGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAAN--SLEQAQAAAERLGYPVLVRAAFALGGLGSGFA 568
Cdd:PRK07178 91 AEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNlaDLDEALAEAERIGYPVMLKATSGGGGRGIRRC 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 569 STKEELS-------ALVAPAFAhTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTV----CNMENldplgiHTGESIVVAPS 637
Cdd:PRK07178 171 NSREELEqnfprviSEATKAFG-SAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPS 243
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158534057 638 QTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEqYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:PRK07178 244 PQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGE-VYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLS 321
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
178-338 |
7.92e-13 |
|
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: 69.10 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 178 IFAVDCGLKYNQI--RCLCQLGAEVTVVPWN---HELDSRKYDGLFLSNGPgdpasypgvvstlNRVLSEPNPR------ 246
Cdd:cd01742 1 ILILDFGSQYTHLiaRRVRELGVYSEILPNTtplEEIKLKNPKGIILSGGP-------------SSVYEEDAPRvdpeif 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 247 ----PVFGICLGHQLLALAIGAKTYKMRYGNRGH------NQPCLLVGTGRCFLTSQNHGFAVDAdsLPAGWAPLFTNAN 316
Cdd:cd01742 68 elgvPVLGICYGMQLIAKALGGKVERGDKREYGKaeieidDSSPLFEGLPDEQTVWMSHGDEVVK--LPEGFKVIASSDN 145
|
170 180
....*....|....*....|..
gi 158534057 317 dCSNEGIVHDNLPFFSVQFHPE 338
Cdd:cd01742 146 -CPVAAIANEEKKIYGVQFHPE 166
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
929-1250 |
1.39e-12 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 71.88 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 929 DFRTPHVLVLGSgvyrigssvefDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLY------FDEISF-EVVMD 1001
Cdd:COG3919 2 MTMRFRVVVLGG-----------DINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVvvpdpgDDPEAFvDALLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1002 IYELENPEGVILSMGGQLpnnMAMALHRQQ----CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQF 1077
Cdd:COG3919 71 LAERHGPDVLIPTGDEYV---ELLSRHRDEleehYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1078 CQTVGYPCVVRPSYvlSGAAMNV----------AYTDGDLERFLSSAAAVskEHPVVISKFIQEAKEIDVDAVAC---DG 1144
Cdd:COG3919 148 AEDLGFPVVVKPAD--SVGYDELsfpgkkkvfyVDDREELLALLRRIAAA--GYELIVQEYIPGDDGEMRGLTAYvdrDG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1145 ----IVSAIAISEHVENAGVHSgdATLVTPPQDItpktLERIKAIVHAVGqelqVTGPFNLQLI--AKDDQLKVIECNVR 1218
Cdd:COG3919 224 evvaTFTGRKLRHYPPAGGNSA--ARESVDDPEL----EEAARRLLEALG----YHGFANVEFKrdPRDGEYKLIEINPR 293
|
330 340 350
....*....|....*....|....*....|..
gi 158534057 1219 VSRSFPFVSKTlGVDLVALATRIIMGEKVESV 1250
Cdd:COG3919 294 FWRSLYLATAA-GVNFPYLLYDDAVGRPLEPV 324
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
177-338 |
1.91e-12 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 68.54 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 177 RIFAVDC--GLKYNQIRCLCQLGAEVTVvpW-NHELD-------SRKYDGLFLSNGPGDPASyPGVVSTLNRVLSEPNpR 246
Cdd:PRK07765 2 RILVVDNydSFVFNLVQYLGQLGVEAEV--WrNDDPRladeaavAAQFDGVLLSPGPGTPER-AGASIDMVRACAAAG-T 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 247 PVFGICLGHQLLALAIGA-----------KTYKMRYGNRGhnqpcLLVGTGRCFLTSQNHGFAVDADSLPA-----GWAP 310
Cdd:PRK07765 78 PLLGVCLGHQAIGVAFGAtvdrapellhgKTSSVHHTGVG-----VLAGLPDPFTATRYHSLTILPETLPAelevtARTD 152
|
170 180 190
....*....|....*....|....*....|..
gi 158534057 311 lftnandcsnEGIV----HDNLPFFSVQFHPE 338
Cdd:PRK07765 153 ----------SGVImavrHRELPIHGVQFHPE 174
|
|
| PRK04523 |
PRK04523 |
N-acetylornithine carbamoyltransferase; Reviewed |
1924-2224 |
2.02e-12 |
|
N-acetylornithine carbamoyltransferase; Reviewed
Pssm-ID: 235304 [Multi-domain] Cd Length: 335 Bit Score: 70.93 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1924 QHILSVKQFTKDQMSHLFNVAHTLRmmvQKERSlDILKGKVMASMFYEVSTRTSSSFAAAMARLGG-AV----------L 1992
Cdd:PRK04523 4 KHFLNTQDWSRAELDALLTQAAAFK---RNKLG-SALKGKSIALVFFNPSLRTRTSFELGAFQLGGhAVvlqpgkdawpI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1993 SFSEATssVQKG---ESLADSVQTMSCYADVVVLR----------HPQPGAVELAAKHCRRPVINAGDGVgeHPTQALLD 2059
Cdd:PRK04523 80 EFELGA--VMDGeteEHIREVARVLSRYVDLIGVRafpkfvdwskDRQDQVLNSFAKYSTVPVINMETIT--HPCQELAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2060 IFTIREELG-TVNGMTI------------TMVGD------LKHGRTVhSLACLLTQYRVSLRYVAppslrmpsSVWDFVA 2120
Cdd:PRK04523 156 ALALQEHFGtTLRGKKYvltwtyhpkplnTAVANsalliaTRLGMDV-TLLCPTPDYILDERYMD--------WAEQNAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2121 SRGTKQEEFESIEEALPDTDVLYM----TRIQKERFGSSQEYEACFGQFILTPHIMTRAKKKmVVMH--PMPRVNEISVE 2194
Cdd:PRK04523 227 ESGGSLTVSHDIDSAYAGADVVYAkswgALPFFGNWEPEKPIRDQYQHFIVDERKMALTNNG-VFSHclPLRRNVKVTDA 305
|
330 340 350
....*....|....*....|....*....|
gi 158534057 2195 VDSDPRAAYFRQAENGMYIRMALLATVLGR 2224
Cdd:PRK04523 306 VMDSPNCIAIDEAENRLHVQKAIMAALASQ 335
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
159-338 |
2.90e-12 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 72.26 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 159 APEVSIKTPRVFNAGGA-PRIFAVDCGLKY-----NQIRclcQLGAEVTVVPWNH---ELDSRKYDGLFLSNGPGDPASY 229
Cdd:PRK13566 509 KPKNLSAEEPDAAAVGEgKRVLLVDHEDSFvhtlaNYFR---QTGAEVTTVRYGFaeeMLDRVNPDLVVLSPGPGRPSDF 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 230 pGVVSTLNRVLSepnpR--PVFGICLGHQLLALAIGAKTYKMRYGNRG------HNQPC-LLVGTGRCFLTSQNHGFAVD 300
Cdd:PRK13566 586 -DCKATIDAALA----RnlPIFGVCLGLQAIVEAFGGELGQLAYPMHGkpsrirVRGPGrLFSGLPEEFTVGRYHSLFAD 660
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 158534057 301 ADSLPAGwapLFTNANdcSNEGIV----HDNLPFFSVQFHPE 338
Cdd:PRK13566 661 PETLPDE---LLVTAE--TEDGVImaieHKTLPVAAVQFHPE 697
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
177-338 |
4.27e-12 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 66.80 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 177 RIFAVDCGLKYNQI--RCLCQLGAEVTVVPwNH----ELDSRKyDGLFLSNGP-----GDPASYpgvVSTLNRvlsepnp 245
Cdd:PRK00758 1 KIVVVDNGGQYNHLihRTLRYLGVDAKIIP-NTtpveEIKAFE-DGLILSGGPdieraGNCPEY---LKELDV------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 246 rPVFGICLGHQLLALAIGAKTYKMRYGNRG--------HNQPclLVGTGRCFLTSQNHgfavdAD---SLPAGWAPLFTN 314
Cdd:PRK00758 69 -PILGICLGHQLIAKAFGGEVGRGEYGEYAlveveildEDDI--LKGLPPEIRVWASH-----ADevkELPDGFEILARS 140
|
170 180
....*....|....*....|....
gi 158534057 315 ANdCSNEGIVHDNLPFFSVQFHPE 338
Cdd:PRK00758 141 DI-CEVEAMKHKEKPIYGVQFHPE 163
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
1464-1778 |
7.64e-12 |
|
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.
Pssm-ID: 238619 Cd Length: 335 Bit Score: 69.23 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1464 LPGLIDVHVHLREpgGTHKEDFASGTAAALAGGVTMvcamPNTRPPIIDAP-ALALAQKLAEAGARCDF----TLFLGAS 1538
Cdd:cd01294 3 IPRPDDMHLHLRD--GAMLKLVLPYTARGFSRAIVM----PNLKPPVTTTAdALAYRERILAADPGPNFtplmTLYLTEN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1539 -SENAGTLGAVAGSAAGLKLYLN--ETFSELRLDSVAQWMEHFETWPSH-LPIVAHAERQSVAAVLMVAQ---------- 1604
Cdd:cd01294 77 tTPEELREAKKKGGIRGVKLYPAgaTTNSQGGVTDLEKIYPVLEAMQKLgMPLLVHGEVPDFKIDVLDREakfipvlepl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1605 ---LTRRSVHICHVARKEEILLIKTAKAqglPVTCEVAPHHLFLNREDLerLGPGKGEV---RPELGSREDMEALwENMA 1678
Cdd:cd01294 157 aqrFPKLKIVLEHITTADAVEYVKSCNE---NVAATITPHHLLLTRDDL--LGGGLNPHlycKPVAKRPEDREAL-RKAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1679 VIDC----FASDHAPHTLEEKCGPKPPPGFPGLETMLPLLLTAVSEGRlSLDDLLQRLHHNPRRIFHLPLQEDTYVEVdl 1754
Cdd:cd01294 231 TSGHpkffLGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHN-ALDKLEAFASDNGPNFYGLPPNKKTITLV-- 307
|
330 340
....*....|....*....|....
gi 158534057 1755 EHEWTVPSHMPFSKAHWTPFEGQK 1778
Cdd:cd01294 308 KEPWKVPEKIPFGNNGVVPFRAGE 331
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
187-338 |
1.34e-11 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 65.54 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 187 YNQIRCLCQLGAEVTVVPwNH-----ELDSRKYDGLFLSNGPGDPA---SYPGVVSTLNRVLsepnprPVFGICLGHQLL 258
Cdd:PRK05670 13 YNLVQYLGELGAEVVVYR-NDeitleEIEALNPDAIVLSPGPGTPAeagISLELIREFAGKV------PILGVCLGHQAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 259 ALAIGA-----------KTYKMRygnrgHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGwapLFTNANDCSNE--GIVH 325
Cdd:PRK05670 86 GEAFGGkvvrakeimhgKTSPIE-----HDGSGIFAGLPNPFTVTRYHSLVVDRESLPDC---LEVTAWTDDGEimGVRH 157
|
170
....*....|...
gi 158534057 326 DNLPFFSVQFHPE 338
Cdd:PRK05670 158 KELPIYGVQFHPE 170
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
187-338 |
2.05e-11 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 65.28 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 187 YNQIRCLCQLGAEVTVVPwNHELDSRKYDGL-----FLSNGPGDPASyPGVvsTLNRVLSEPNPRPVFGICLGHQLLALA 261
Cdd:PRK08857 13 YNLYQYFCELGAQVKVVR-NDEIDIDGIEALnpthlVISPGPCTPNE-AGI--SLQAIEHFAGKLPILGVCLGHQAIAQV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 262 IGAKTYKMRYGNRGHNQPclLVGTGRCFLTSQN--------HGFAVDADSLPA-----GWAPLFTNANDcSNEGIVHDNL 328
Cdd:PRK08857 89 FGGQVVRARQVMHGKTSP--IRHTGRSVFKGLNnpltvtryHSLVVKNDTLPEcfeltAWTELEDGSMD-EIMGFQHKTL 165
|
170
....*....|
gi 158534057 329 PFFSVQFHPE 338
Cdd:PRK08857 166 PIEAVQFHPE 175
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
1314-1427 |
6.05e-11 |
|
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.
Pssm-ID: 238712 [Multi-domain] Cd Length: 110 Bit Score: 61.34 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1314 NILLTIgSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILDQLAENHFELVI 1393
Cdd:cd01424 2 TVFISV-ADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEG--------RPNIVDLIKNGEIQLVI 72
|
90 100 110
....*....|....*....|....*....|....
gi 158534057 1394 NlsmrGAGGRRlssFVTKGYRTRRLAADFSVPLI 1427
Cdd:cd01424 73 N----TPSGKR---AIRDGFSIRRAALEYKVPYF 99
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
1059-1219 |
6.59e-11 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 63.04 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1059 GISQPQWRELSDLESARQFCQTVGYPCVV---RPSYvlSGAAMNVAYTDGDLERFLSSAAAVskehPVVISKFIQEAKEI 1135
Cdd:pfam02222 4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEELGDG----PVIVEEFVPFDREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1136 DVDAV-ACDGIVSAIAISEHVEnagvHSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFNLQL-IAKDDQLKVI 1213
Cdd:pfam02222 78 SVLVVrSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELfVTEDGDLLIN 153
|
....*.
gi 158534057 1214 ECNVRV 1219
Cdd:pfam02222 154 ELAPRP 159
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
187-338 |
6.86e-11 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 63.60 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 187 YNQIRCLCQLGAEVTVVPwNHELD---SRKYDGLFLSNGPGDPASYPGVVSTLNRVLSEpnpRPVFGICLGHQLLALAIG 263
Cdd:PRK06895 15 FNLVDLIRKLGVPMQVVN-VEDLDldeVENFSHILISPGPDVPRAYPQLFAMLERYHQH---KSILGVCLGHQTLCEFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 264 AKTYKMRYGNRGHNQPCLLVGTGRCF--LTSQ-----NHGFAVDADSLPAgwaPLFTNANdCSNEGIV---HDNLPFFSV 333
Cdd:PRK06895 91 GELYNLNNVRHGQQRPLKVRSNSPLFdgLPEEfniglYHSWAVSEENFPT---PLEITAV-CDENVVMamqHKTLPIYGV 166
|
....*
gi 158534057 334 QFHPE 338
Cdd:PRK06895 167 QFHPE 171
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
498-716 |
9.15e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 66.93 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 498 GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP--SEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEEL- 574
Cdd:PRK08654 99 GIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELe 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 575 ------SALVAPAFAhTSQVLIDKSLKGWKEIEYEVVRDAYGNCvtvcnmenldplgIHTGES-----------IVVAPS 637
Cdd:PRK08654 179 daiestQSIAQSAFG-DSTVFIEKYLEKPRHIEIQILADKHGNV-------------IHLGDRecsiqrrhqklIEEAPS 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158534057 638 QTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALnpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:PRK08654 245 PIMTPELRERMGEAAVKAAKAINYENAGTVEFLY--SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELS 321
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
1464-1794 |
1.83e-10 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 65.11 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1464 LPGLIDVHVHLREPGGTHKeDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLgASSENaG 1543
Cdd:PRK08417 29 LPALVDLNVSLKNDSLSSK-NLKSLENECLKGGVGSIVLYPDSTPAIDNEIALELINSAQRELPMQIFPSIR-ALDED-G 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1544 TLGAVA-----GSAAglkLYLNETFSELRLDSVAQWMEHFETwpshlPIVAHAERQSV---------------------- 1596
Cdd:PRK08417 106 KLSNIAtllkkGAKA---LELSSDLDANLLKVIAQYAKMLDV-----PIFCRCEDSSFddsgvmndgelsfelglpgips 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1597 -AAVLMVAQLTRRSVHIC------HVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPgKGEVRPELGSRED 1669
Cdd:PRK08417 178 iAETKEVAKMKELAKFYKnkvlfdTLALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSACENFNT-AAKLNPPLRSKED 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1670 MEALWENM--AVIDCFASDHAPHTLEEK--CGPKPPPGFPGLETMLPLLLT-AVSEGRLSLDDLLQRLHHNPRRIFHLPL 1744
Cdd:PRK08417 257 RLALLEALkeGKIDFLTSLHSAKSNSKKdlAFDEAAFGIDSICEYFSLCYTyLVKEGIITWSELSRFTSYNPAQFLGLNS 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 158534057 1745 QEDT------YVEVDLEHEWTVPSHMPfskahwtPFEGQKVKGTVRRVVLRGEVAY 1794
Cdd:PRK08417 337 GEIEvgkeadLVLFDPNESTIIDDNFS-------LYSGDELYGKIEAVIIKGKLYL 385
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
498-716 |
2.09e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 65.55 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 498 GVRVLGTPVETIELTEDRrAFAARMA-EIGEHVAPSEAA--NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEEL 574
Cdd:PRK12833 102 GLIFVGPDAQTIRTMGDK-ARARRTArRAGVPTVPGSDGvvASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 575 SALV------APAFAHTSQVLIDKSLKGWKEIEYEVVRDayGNCVTVCnMENLDPLGIHTGESIVVAPSQTLNDREYQLL 648
Cdd:PRK12833 181 AAELplaqreAQAAFGDGGVYLERFIARARHIEVQILGD--GERVVHL-FERECSLQRRRQKILEEAPSPSLTPAQRDAL 257
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158534057 649 RRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:PRK12833 258 CASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLR 325
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
987-1237 |
3.60e-10 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 63.42 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 987 DRLYFDEISFEVVMDIYELENPEGVILsmgGQLPNNMAMA----LHRQQCRVLGtSPEAIDSAENRFKFSRLLDTIGISQ 1062
Cdd:COG0189 36 DDLTLDLGRAPELYRGEDLSEFDAVLP---RIDPPFYGLAllrqLEAAGVPVVN-DPEAIRRARDKLFTLQLLARAGIPV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1063 PQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEhPVVISKFIQEAKEIDVDAVAC 1142
Cdd:COG0189 112 PPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELGSE-PVLVQEFIPEEDGRDIRVLVV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1143 DG-IVSAIA-ISEHVENAG-VHSGDATLvtpPQDITPKTLERIKAIVHAVGqeLQVTGpfnLQLIAKDDQLKVIECNVRV 1219
Cdd:COG0189 191 GGePVAAIRrIPAEGEFRTnLARGGRAE---PVELTDEERELALRAAPALG--LDFAG---VDLIEDDDGPLVLEVNVTP 262
|
250
....*....|....*...
gi 158534057 1220 srSFPFVSKTLGVDLVAL 1237
Cdd:COG0189 263 --GFRGLERATGVDIAEA 278
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
498-687 |
1.99e-09 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 63.23 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 498 GVRVLGTPVETIELTEDRraFAARMA--EIGEHVAPS--EAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEE 573
Cdd:PRK12999 103 GITFIGPTAEVLRLLGDK--VAARNAaiKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 574 LSALVAPA-------FAhTSQVLIDKSLKGWKEIEYEVVRDAYGNCVtvcnmenldplgiHTGE---SI------VV--A 635
Cdd:PRK12999 181 LEEAFERAkreakaaFG-NDEVYLEKYVENPRHIEVQILGDKHGNVV-------------HLYErdcSVqrrhqkVVeiA 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 158534057 636 PSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESeQYYIIEVNARL 687
Cdd:PRK12999 247 PAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADG-NFYFIEVNPRI 297
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
498-712 |
3.62e-09 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 61.75 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 498 GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAAN--SLEQAQAAAERLGYPVLVRAAFALGGLG---------- 564
Cdd:PRK08463 98 GIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPgTEKLNseSMEEIKIFARKIGYPVILKASGGGGGRGirvvhkeedl 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 565 -SGFASTKEElsalvAPAFAHTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCnmENLDPLGIHTGESIVVAPSQTLNDR 643
Cdd:PRK08463 178 eNAFESCKRE-----ALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLC--ERDCSIQRRHQKVIEIAPCPSISDN 250
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158534057 644 EYQLLRRTAIKVTQHLGIVGECNVQYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALG 712
Cdd:PRK08463 251 LRKTMGVTAVAAAKAVGYTNAGTIEFLLD-DYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
187-338 |
4.53e-09 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 58.20 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 187 YNQIRCLCQLGAEVTVVPwNHELDSRKYD-----GLFLSNGPGDPASYP---GVVSTL-NRVlsepnprPVFGICLGHQL 257
Cdd:CHL00101 13 YNLVQSLGELNSDVLVCR-NDEIDLSKIKnlnirHIIISPGPGHPRDSGislDVISSYaPYI-------PILGVCLGHQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 258 LALAIGAKTYKMRYGNRG------HNQPCLLVGTGRCFLTSQNHGFAVDADSLPagwAPLFTNANdcSNEGIV----HDN 327
Cdd:CHL00101 85 IGYLFGGKIIKAPKPMHGktskiyHNHDDLFQGLPNPFTATRYHSLIIDPLNLP---SPLEITAW--TEDGLImacrHKK 159
|
170
....*....|..
gi 158534057 328 LPF-FSVQFHPE 338
Cdd:CHL00101 160 YKMlRGIQFHPE 171
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
187-362 |
8.01e-09 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 57.51 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 187 YNQIRCLCQLGAEVtVVPWN-----HELDSRKYDGLFLSNGPGDPaSYPGVvsTLNRVLSEPNPRPVFGICLGHQLLALA 261
Cdd:PRK07649 13 FNLVQFLGELGQEL-VVKRNdevtiSDIENMKPDFLMISPGPCSP-NEAGI--SMEVIRYFAGKIPIFGVCLGHQSIAQV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 262 IGA---KTYKMRYGNRG---HNQPCLLVGTGRCFLTSQNHGFAVDADSLPagwaplftnanDC------SNEG----IVH 325
Cdd:PRK07649 89 FGGevvRAERLMHGKTSlmhHDGKTIFSDIPNPFTATRYHSLIVKKETLP-----------DClevtswTEEGeimaIRH 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 158534057 326 DNLPFFSVQFHPEHRAGPSDMELLFDvFLETVRDTVA 362
Cdd:PRK07649 158 KTLPIEGVQFHPESIMTSHGKELLQN-FIRKYSPSVT 193
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
187-338 |
1.73e-08 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 59.73 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 187 YNQIRCLCQLGAEVTVVPWN-----HELDSRKYDGLFLSNGPGDP----------ASYPGVVstlnrvlsepnprPVFGI 251
Cdd:PRK14607 13 YNIYQYIGELGPEEIEVVRNdeitiEEIEALNPSHIVISPGPGRPeeagisveviRHFSGKV-------------PILGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 252 CLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTG------RCFLTSQNHGFAVDADSLPAGWAPLfTNANDCSNEGIVH 325
Cdd:PRK14607 80 CLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGlfrgipNPTVATRYHSLVVEEASLPECLEVT-AKSDDGEIMGIRH 158
|
170
....*....|...
gi 158534057 326 DNLPFFSVQFHPE 338
Cdd:PRK14607 159 KEHPIFGVQFHPE 171
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
190-263 |
1.82e-08 |
|
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: 54.53 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 190 IRCLCQLGAEVTVVPWNH-----ELDSRKYDGLFLSNGPGDP---ASYPGVVSTLNRVLSepNPRPVFGICLGHQLLALA 261
Cdd:cd01653 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPddlARDEALLALLREAAA--AGKPILGICLGAQLLVLG 95
|
..
gi 158534057 262 IG 263
Cdd:cd01653 96 VQ 97
|
|
| PRK07200 |
PRK07200 |
aspartate/ornithine carbamoyltransferase family protein; Validated |
1933-2077 |
2.04e-08 |
|
aspartate/ornithine carbamoyltransferase family protein; Validated
Pssm-ID: 235961 [Multi-domain] Cd Length: 395 Bit Score: 58.98 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1933 TKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQ 2012
Cdd:PRK07200 30 TPDELKAVLDVADALRALREENISTKVFNSGLGISVFRDNSTRTRFSYASACNLLGLEVQDLDEGKSQIAHGETVRETAN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 2013 TMSCYADVVVLR------------HPQPGAVELAAKHC---RRP-VINAGDGVgEHPTQALLDIFTIREELGTVN---GM 2073
Cdd:PRK07200 110 MISFMADVIGIRddmyigkgnaymREVGAAVDDGYKQGvlpQRPtLVNLQCDI-DHPTQSMADLLHLIEHFGGLEnlkGK 188
|
....
gi 158534057 2074 TITM 2077
Cdd:PRK07200 189 KIAM 192
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
502-715 |
2.29e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 58.96 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 502 LGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLG-----------SGFA 568
Cdd:PRK05586 103 IGPDSETIELMGNKSNAREIMIKAGVPVVPgSEGEiENEEEALEIAKEIGYPVMVKASAGGGGRGirivrseeeliKAFN 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 569 STKEELSAlvapAFAHTSqVLIDKSLKGWKEIEYEVVRDAYGNCVTV----CNMENldplgiHTGESIVVAPSQTLNDRE 644
Cdd:PRK05586 183 TAKSEAKA----AFGDDS-MYIEKFIENPKHIEFQILGDNYGNVVHLgerdCSLQR------RNQKVLEEAPSPVMTEEL 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158534057 645 YQLLRRTAIKVTQHLGIVGECNVQYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPL 715
Cdd:PRK05586 252 RKKMGEIAVKAAKAVNYKNAGTIEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
507-687 |
7.74e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 57.12 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 507 ETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELsalvAPAFAH 584
Cdd:PRK08591 108 ETIRLMGDKVTAKATMKKAGVPVVPgSDGPvDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAEL----EKAFSM 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 585 TSQ----------VLIDKSLKGWKEIEYEVVRDAYGNcvtvcnmenldplGIHTGE---SI------VV--APSQTLNDR 643
Cdd:PRK08591 184 ARAeakaafgnpgVYMEKYLENPRHIEIQVLADGHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEE 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 158534057 644 EYQLLRRTAIKVTQHLGIVGECNVQYaLNPESEQYYIIEVNARL 687
Cdd:PRK08591 251 LRRKIGEAAVKAAKAIGYRGAGTIEF-LYEKNGEFYFIEMNTRI 293
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
187-338 |
1.42e-07 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 53.77 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 187 YNQIRCLCQLGAEVtVVPWNHELDSRKYDGL-----FLSNGPGDPaSYPGVvsTLNRVLSEPNPRPVFGICLGHQLLALA 261
Cdd:PRK08007 13 WNLYQYFCELGADV-LVKRNDALTLADIDALkpqkiVISPGPCTP-DEAGI--SLDVIRHYAGRLPILGVCLGHQAMAQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 262 IGAKTYKMRYGNRGHNQPCLLVGTG------RCFLTSQNHGFAVDADSLPAGWAplfTNANDCSNE--GIVHDNLPFFSV 333
Cdd:PRK08007 89 FGGKVVRAAKVMHGKTSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLEGV 165
|
....*
gi 158534057 334 QFHPE 338
Cdd:PRK08007 166 QFHPE 170
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
190-258 |
1.49e-07 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 51.05 E-value: 1.49e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158534057 190 IRCLCQLGAEVTVVPWNH-----ELDSRKYDGLFLSNGPGDP---ASYPGVVSTLNRVLSepNPRPVFGICLGHQLL 258
Cdd:cd03128 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPddlAWDEALLALLREAAA--AGKPVLGICLGAQLL 92
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
498-686 |
1.55e-07 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 57.01 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 498 GVRVLGTPVETIELTEDRRAfAARMA-EIGEHVAPS--EAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEEL 574
Cdd:COG1038 102 GITFIGPSPEVLEMLGDKVA-ARAAAiEAGVPVIPGteGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEEL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 575 SALVAPAF--AHTS----QVLIDKSLKGWKEIEYEVVRDAYGNCVtvcnmenldplgiHTGE---SI------VV--APS 637
Cdd:COG1038 181 EEAFESARreAKAAfgddEVFLEKYIERPKHIEVQILGDKHGNIV-------------HLFErdcSVqrrhqkVVeiAPA 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 158534057 638 QTLNDREYQLLRRTAIKVTQHLGIVGECNVQYaLNPESEQYYIIEVNAR 686
Cdd:COG1038 248 PNLDEELREAICEAAVKLAKAVGYVNAGTVEF-LVDDDGNFYFIEVNPR 295
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
215-353 |
7.20e-07 |
|
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: 51.81 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 215 DGLFLSNGPG-DPASYPGVVSTlnrVLSEPNPR-----------------PVFGICLGHQLLALAIGAKTYKMRYGNRGH 276
Cdd:cd01745 55 DGLLLTGGGDvDPPLYGEEPHP---ELGPIDPErdafelallraalergkPILGICRGMQLLNVALGGTLYQDIRVNSLH 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158534057 277 NQpcllvgtgrcfltsqnhgfAVDAdsLPAGWAPLFTnANDCSNEGIVHDNLPF-FSVQFHPE-HRAGPSDMELLFDVF 353
Cdd:cd01745 132 HQ-------------------AIKR--LADGLRVEAR-APDGVIEAIESPDRPFvLGVQWHPEwLADTDPDSLKLFEAF 188
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
177-338 |
7.80e-07 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 54.28 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 177 RIFAVDCGLKYNQ-----IRclcQLGAEVTVVPWNH---ELDSRKYDGLFLSNGPgdpASypgvvstlnrVLSEPNPR-- 246
Cdd:PRK00074 5 KILILDFGSQYTQliarrVR---ELGVYSEIVPYDIsaeEIRAFNPKGIILSGGP---AS----------VYEEGAPRad 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 247 --------PVFGICLGHQLLALAIGAK---TYKMRYGN---RGHNQPCLLVGTGRCFLTSQNHGFAVDAdsLPAGWAPLF 312
Cdd:PRK00074 69 peifelgvPVLGICYGMQLMAHQLGGKverAGKREYGRaelEVDNDSPLFKGLPEEQDVWMSHGDKVTE--LPEGFKVIA 146
|
170 180
....*....|....*....|....*.
gi 158534057 313 TNANdCSNEGIVHDNLPFFSVQFHPE 338
Cdd:PRK00074 147 STEN-CPIAAIANEERKFYGVQFHPE 171
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
1464-1730 |
1.76e-06 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 52.50 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1464 LPGLIDVHVHLR--------EPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDApalalaqkLAEAgarcdftlfl 1535
Cdd:pfam01979 3 LPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEA--------LLEA---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1536 gASSENAGtLGAVAGSAAGLKLYLNETFSELRLDSVAQWM-EHFETWPSHLPIVAHAERQSV--AAVLMVAQLTRR---S 1609
Cdd:pfam01979 65 -AEELPLG-LRFLGPGCSLDTDGELEGRKALREKLKAGAEfIKGMADGVVFVGLAPHGAPTFsdDELKAALEEAKKyglP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1610 VHIcHVARKEEILLIKTAKAQG----------------LPVTCEVAPHHLFLNREDLERLGPGKGEVR------PELGSR 1667
Cdd:pfam01979 143 VAI-HALETKGEVEDAIAAFGGgiehgthlevaesgglLDIIKLILAHGVHLSPTEANLLAEHLKGAGvahcpfSNSKLR 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158534057 1668 EDMEALWE--NMAVIDCFASDHAPHTleekcgpkpPPGFPGLETMLPLLLTAVSEGRLSLDDLLQ 1730
Cdd:pfam01979 222 SGRIALRKalEDGVKVGLGTDGAGSG---------NSLNMLEELRLALELQFDPEGGLSPLEALR 277
|
|
| PRK06849 |
PRK06849 |
hypothetical protein; Provisional |
1032-1219 |
4.26e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235876 [Multi-domain] Cd Length: 389 Bit Score: 51.59 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1032 CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQF-CQTVGYPCVVRPSYVLSGAAMNVAYTdgdlERF 1110
Cdd:PRK06849 101 CEVLHFDFELLLLLHNKWEFAEQARSLGLSVPKTYLITDPEAIRNFmFKTPHTPYVLKPIYSRFVRRVDLLPK----EAA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1111 LSSaAAVSKEHPVVISKFIQeAKEIDVDAVACDGIVSAIAISEHVENAGVHSGDATlvtppQDITPktlERIKAIVHAVG 1190
Cdd:PRK06849 177 LKE-LPISKDNPWVMQEFIQ-GKEYCSYSIVRSGELRAHSCYKPEYCAGSGAQIAF-----QPINH---PRIEEFVTHFV 246
|
170 180 190
....*....|....*....|....*....|
gi 158534057 1191 QELQVTGPFNLQLI-AKDDQLKVIECNVRV 1219
Cdd:PRK06849 247 KELNYTGQISFDFIeTENGDAYPIECNPRT 276
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
536-684 |
1.32e-05 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 48.47 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 536 NSLEQAQAAAERLGYPVLVRAAfalgGLGSGFASTK----EELSALVAPAFAHTSQVLIDKSLKGwKEIEyevvrdaygn 611
Cdd:pfam07478 23 NPKEWCAQVEEALGYPVFVKPA----RLGSSVGVSKvesrEELQAAIEEAFQYDEKVLVEEGIEG-REIE---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 612 cVTVCNMENLDPLGIH------------------TGESIVVAPsqtLNDREYQLLRRTAIKVTQHLGIVGECNVQYALnP 673
Cdd:pfam07478 88 -CAVLGNEDPEVSPVGeivpsggfydyeakyiddSAQIVVPAD---LEEEQEEQIQELALKAYKALGCRGLARVDFFL-T 162
|
170
....*....|.
gi 158534057 674 ESEQYYIIEVN 684
Cdd:pfam07478 163 EDGEIVLNEVN 173
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
1054-1242 |
1.94e-05 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 47.70 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1054 LLDTIGISQPQW-------RELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLssAAAVSKEHPVVIS 1126
Cdd:pfam07478 1 LLKAAGLPVVPFvtftradWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAI--EEAFQYDEKVLVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1127 KFIqEAKEIDVdAVACDGIVSAIAISEHVENAGV------HSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTG--- 1197
Cdd:pfam07478 79 EGI-EGREIEC-AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGlar 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 158534057 1198 -PFNLQliaKDDQLKVIECN-----VRVSRsFPFVSKTLGVDLVALATRII 1242
Cdd:pfam07478 157 vDFFLT---EDGEIVLNEVNtipgfTSISM-FPKLAAAAGVSFPDLVDQLI 203
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
187-338 |
3.63e-05 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 47.10 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 187 YNQIRCLCQLGA--------EVTVvpwnHELDSRKYDGLFLSNGPGDPASyPGVvsTLNRVLSEPNPRPVFGICLGHQLL 258
Cdd:PLN02335 32 YNLCQYMGELGChfevyrndELTV----EELKRKNPRGVLISPGPGTPQD-SGI--SLQTVLELGPLVPLFGVCMGLQCI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 259 ALAIGAKTYKMRYG-NRGHNQPC---------LLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDNL 328
Cdd:PLN02335 105 GEAFGGKIVRSPFGvMHGKSSPVhydekgeegLFSGLPNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKY 184
|
170
....*....|.
gi 158534057 329 PFFS-VQFHPE 338
Cdd:PLN02335 185 KHIQgVQFHPE 195
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
247-338 |
3.70e-05 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 47.25 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 247 PVFGICLGHQLLALAIGAKTY---KMRYGNRGHNQPC----------LLVGTGRCF--LTSQN-------HGFAVDAdsL 304
Cdd:pfam07722 107 PILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapshaVNVEPGSLLasLLGSEefrvnslHHQAIDR--L 184
|
90 100 110
....*....|....*....|....*....|....*.
gi 158534057 305 PAGWAPLFTnANDCSNEGIVHDNLPFF--SVQFHPE 338
Cdd:pfam07722 185 APGLRVEAV-APDGTIEAIESPNAKGFalGVQWHPE 219
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
1053-1185 |
5.82e-05 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 47.41 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1053 RLLDTIGISQPQWRELS--DLESARQFCQTVGYPCVVRPsyVLSGAA--MNVAYTDGDLERFLSSAAAVSkeHPVVISKF 1128
Cdd:COG1181 101 RVLAAAGLPTPPYVVLRrgELADLEAIEEELGLPLFVKP--AREGSSvgVSKVKNAEELAAALEEAFKYD--DKVLVEEF 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158534057 1129 IqEAKEIDVdAVACDGIVSAIAISEHVENAGV-------HSGDATLVTPPqDITPKTLERIKAI 1185
Cdd:COG1181 177 I-DGREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPA-RLPEELEERIQEL 237
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
529-684 |
7.81e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 47.03 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 529 VAPSEAANSLEQAQAAAERLGYPVLVRAafALGG--LGSGFASTKEELSALVAPAFAHTSQVLIDKSLKGwkeIEYevvr 606
Cdd:PRK01372 113 TPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGssVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKG---REL---- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 607 daygncvTVCNMEN--LDPLGI-------------HTGESIVVAPSQtLNDREYQLLRRTAIKVTQHLGIVGECNVQYAL 671
Cdd:PRK01372 184 -------TVAVLGGkaLPVIEIvpagefydyeakyLAGGTQYICPAG-LPAEIEAELQELALKAYRALGCRGWGRVDFML 255
|
170
....*....|...
gi 158534057 672 NpESEQYYIIEVN 684
Cdd:PRK01372 256 D-EDGKPYLLEVN 267
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
1446-1813 |
1.28e-04 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 47.15 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1446 APPLKVHVDCMT---SQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGVTMvcampntrppIID-------- 1512
Cdd:PLN02942 36 APNLKVPDDVRVidaTGKFV-MPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTTM----------HIDfvipvngn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1513 -APALALAQKLAEAGArCDFTLFLGAS------SENAGTLGAVAGSAAgLKLYLNETFS-----ELRLDSVAQW------ 1574
Cdd:PLN02942 105 lLAGYEAYEKKAEKSC-MDYGFHMAITkwddtvSRDMETLVKEKGINS-FKFFMAYKGSlmvtdELLLEGFKRCkslgal 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1575 -MEHFE-----------------TWP-----SHLPIVahaERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQG 1631
Cdd:PLN02942 183 aMVHAEngdavfegqkrmielgiTGPeghalSRPPLL---EGEATARAIRLAKFVNTPLYVVHVMSIDAMEEIARARKSG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1632 LPVTCEVAPHHLFLNRE---DLERLGPGKGEVRPELGSREDMEALWENMA--VIDCFASDHAPHTLEEKCGPKP------ 1700
Cdd:PLN02942 260 QRVIGEPVVSGLVLDDSklwDPDFTIASKYVMSPPIRPAGHGKALQAALSsgILQLVGTDHCPFNSTQKAFGKDdfrkip 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1701 PPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFH--------LPLQEDTYVEVDLEHEWTVPSHMPFSKAHWT 1772
Cdd:PLN02942 340 NGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNiyprkgaiLAGSDADIIILNPNSTFTISAKTHHSRIDTN 419
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 158534057 1773 PFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWP 1813
Cdd:PLN02942 420 VYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPP 460
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
395-718 |
1.57e-04 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 46.25 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 395 KVLILgSGGLSigqaGEFD---YSGSQAIKALKEENIQtllinpniatvqtsqgladkVYFLPITPHYVTQVIRNERPDG 471
Cdd:COG1181 2 RVAVL-FGGRS----AEREvslKSGRAVAAALDKAGYD--------------------VVPIGIDVEDLPAALKELKPDV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 472 ILLtfggqtALNC--GVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANS--LEQAQAAAER 547
Cdd:COG1181 57 VFP------ALHGrgGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRgeLADLEAIEEE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 548 LGYPVLVRAAFAlgglGSGF----ASTKEELSALVAPAFAHTSQVLIDKSLKGwKEIEyevvrdaygncVTVCNMENLDP 623
Cdd:COG1181 131 LGLPLFVKPARE----GSSVgvskVKNAEELAAALEEAFKYDDKVLVEEFIDG-REVT-----------VGVLGNGGPRA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 624 LGI----------------HTGESIVVAPSQtLNDREYQLLRRTAIKVTQHLGIVGecnvqYA-----LNPEsEQYYIIE 682
Cdd:COG1181 195 LPPieivpengfydyeakyTDGGTEYICPAR-LPEELEERIQELALKAFRALGCRG-----YArvdfrLDED-GEPYLLE 267
|
330 340 350
....*....|....*....|....*....|....*...
gi 158534057 683 VNAR--LSRSSalaskatGYPLAYVAAklalGIPLPEL 718
Cdd:COG1181 268 VNTLpgMTPTS-------LLPKAAAAA----GISYEEL 294
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
522-601 |
5.42e-04 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 44.73 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 522 MAEIGEHVAPSEAANSLEQA----QAAAERLGYPVLVRAAfalgGLGSGF----ASTKEELSALVAPAFAHTSQVLIDKS 593
Cdd:PRK01966 131 LAAAGIPVAPYVVLTRGDWEeaslAEIEAKLGLPVFVKPA----NLGSSVgiskVKNEEELAAALDLAFEYDRKVLVEQG 206
|
....*...
gi 158534057 594 LKGwKEIE 601
Cdd:PRK01966 207 IKG-REIE 213
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
210-359 |
5.64e-04 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 45.22 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 210 DSRKYDGLFLSNGPGDPASyPGVVSTLNRVLSEPNPRPVFGICLGHQLLALAIGAKTYKM------RYGNRGHNQpCLL- 282
Cdd:PLN02889 128 EEKAFDNIVISPGPGSPTC-PADIGICLRLLLECRDIPILGVCLGHQALGYVHGARIVHApepvhgRLSEIEHNG-CRLf 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 283 --VGTGR--CFLTSQNHGFAVDADSLPAGWAPL-FTNAND----------------CSNE-------------------- 321
Cdd:PLN02889 206 ddIPSGRnsGFKVVRYHSLVIDAESLPKELVPIaWTSSSDtlsflesqksglvpdaYESQigqsgssdpfssklkngtsw 285
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 158534057 322 ---------------GIVHDNLPFFSVQFHPEhRAGPSDMELLFDVFLETVRD 359
Cdd:PLN02889 286 psshsermqngkilmGIMHSTRPHYGLQFHPE-SIATCYGRQIFKNFREITQD 337
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1035-1141 |
5.66e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 44.97 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1035 LGTSPEAIDSAENRFKFSRLLDTIGISQPQWRE--LSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLS 1112
Cdd:PRK08654 103 IGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEegIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIE 182
|
90 100 110
....*....|....*....|....*....|...
gi 158534057 1113 S----AAAVSKEHPVVISKFIQEAKEIDVDAVA 1141
Cdd:PRK08654 183 StqsiAQSAFGDSTVFIEKYLEKPRHIEIQILA 215
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
1079-1145 |
6.11e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 44.44 E-value: 6.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158534057 1079 QTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVskEHPVVISKFIqEAKEIDVDAVACDGI 1145
Cdd:PRK14570 168 EVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKY--DLTVVIEKFI-EAREIECSVIGNEQI 231
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1068-1249 |
7.67e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 44.35 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1068 LSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLER-FL---SSAAAVSKEHPVVISKFIQEAKEIDVDAVAcD 1143
Cdd:PRK08462 140 LKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENlYLaaeSEALSAFGDGTMYMEKFINNPRHIEVQILG-D 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1144 GIVSAIAISEhvENAGVHSGDATLV--TPPQDITPKTLER-----IKAiVHAVGQELQVTGPFnlqLIAKDDQLKVIECN 1216
Cdd:PRK08462 219 KHGNVIHVGE--RDCSLQRRHQKLIeeSPAVVLDEKTRERlhetaIKA-AKAIGYEGAGTFEF---LLDSNLDFYFMEMN 292
|
170 180 190
....*....|....*....|....*....|...
gi 158534057 1217 VRVSRSFPFVSKTLGVDLVALATRIIMGEKVES 1249
Cdd:PRK08462 293 TRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPS 325
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
507-663 |
8.94e-04 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 43.91 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 507 ETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFalGGL-GSG--FASTKEELSALVApafA 583
Cdd:COG0026 82 EALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRR--GGYdGKGqvVIKSAADLEAAWA---A 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 584 HTSQVLIdksLKGWKEIEYE----VVRDAYGNCVT--VCnmENldplgIHTG----ESIVVAP-SQTLNDReyqlLRRTA 652
Cdd:COG0026 157 LGGGPCI---LEEFVPFERElsviVARSPDGEVATypVV--EN-----VHRNgildESIAPARiSEALAAE----AEEIA 222
|
170
....*....|.
gi 158534057 653 IKVTQHLGIVG 663
Cdd:COG0026 223 KRIAEALDYVG 233
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
191-349 |
2.32e-03 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 41.33 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 191 RCLCQLGAEVTVVPWNHELdsRKYDGLFLsngPGDpASYPGVVSTLNRV-LSEP------NPRPVFGICLGHQLLalaig 263
Cdd:cd01748 16 NALERLGAEVIITSDPEEI--LSADKLIL---PGV-GAFGDAMANLRERgLIEAlkeaiaSGKPFLGICLGMQLL----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 264 aktykMRYGNRGHNQPCL--LVGTGRCFLTSQNHgfavdadSLP-AGW--------APLFTNAND-------------CS 319
Cdd:cd01748 85 -----FESSEEGGGTKGLglIPGKVVRFPASEGL-------KVPhMGWnqleitkeSPLFKGIPDgsyfyfvhsyyapPD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 158534057 320 NEGIV---------------HDNlpFFSVQFHPE--HRAGpsdMELL 349
Cdd:cd01748 153 DPDYIlattdyggkfpaaveKDN--IFGTQFHPEksGKAG---LKLL 194
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1443-1595 |
3.00e-03 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 42.26 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1443 IGPAPPLKV-----HVDCmtSQKLVrLPGLIDVHVHLREPGGTHKEDFASGT---------------AAALAGGVTMVCA 1502
Cdd:COG1228 41 VGPAADLAVpagaeVIDA--TGKTV-LPGLIDAHTHLGLGGGRAVEFEAGGGitptvdlvnpadkrlRRALAAGVTTVRD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1503 MPNTRPPIIDAPA------LALAQKLAEAGArcdFTLFLGASSENAGTLGAV-----AGSAAGLKLYLNETFSELRLDSV 1571
Cdd:COG1228 118 LPGGPLGLRDAIIagesklLPGPRVLAAGPA---LSLTGGAHARGPEEARAAlrellAEGADYIKVFAEGGAPDFSLEEL 194
|
170 180
....*....|....*....|....
gi 158534057 1572 AQWMEhfETWPSHLPIVAHAERQS 1595
Cdd:COG1228 195 RAILE--AAHALGLPVAAHAHQAD 216
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
507-663 |
5.61e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 41.29 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 507 ETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFaLG--GLGSGFASTKEELSALVApafAH 584
Cdd:PRK06019 93 DALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTRR-GGydGKGQWVIRSAEDLEAAWA---LL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 585 TSQVLIdksLKGWKEIEYE----VVRDAYGNCVT---VcnmENLDPLGI-HTgesiVVAPSQtLNDREYQLLRRTAIKVT 656
Cdd:PRK06019 169 GSVPCI---LEEFVPFEREvsviVARGRDGEVVFyplV---ENVHRNGIlRT----SIAPAR-ISAELQAQAEEIASRIA 237
|
....*..
gi 158534057 657 QHLGIVG 663
Cdd:PRK06019 238 EELDYVG 244
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
1038-1212 |
7.15e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 41.29 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1038 SPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVV---RPSY------VLSGAAmnvaytdgDLE 1108
Cdd:PRK06019 91 GPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLktrRGGYdgkgqwVIRSAE--------DLE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1109 RFLSSAAAVskehPVVISKFIQEAKEIDVDAV-ACDGIVSAIAIsehVENagVHSG---DATLVtpPQDITPKTLERIKA 1184
Cdd:PRK06019 163 AAWALLGSV----PCILEEFVPFEREVSVIVArGRDGEVVFYPL---VEN--VHRNgilRTSIA--PARISAELQAQAEE 231
|
170 180
....*....|....*....|....*....
gi 158534057 1185 IVHAVGQELQVTGPFNLQL-IAKDDQLKV 1212
Cdd:PRK06019 232 IASRIAEELDYVGVLAVEFfVTGDGELLV 260
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1067-1246 |
7.74e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 41.33 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1067 ELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSA---AAVSKEHPVV-ISKFIQEAKEIDVDAVAc 1142
Cdd:PRK08591 137 PVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMAraeAKAAFGNPGVyMEKYLENPRHIEIQVLA- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158534057 1143 DGIVSAIAISE--------H---VENAgvhsgdatlvtPPQDITPKTLERIKAIVHAVGQELQVTGPFNLQ-LIAKDDQL 1210
Cdd:PRK08591 216 DGHGNAIHLGErdcslqrrHqkvLEEA-----------PSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEfLYEKNGEF 284
|
170 180 190
....*....|....*....|....*....|....*.
gi 158534057 1211 KVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEK 1246
Cdd:PRK08591 285 YFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
|
| |
