|
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: 1799.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 391 PPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPD 470
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 471 GVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGY 550
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 551 PVLVRAAFALGGLGSGFASNREELSALVAPAFAHT--SQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHT 628
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 629 GESIVVAPSQTLNDREYQLLRQTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAK 708
Cdd:TIGR01369 244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 709 LALGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENC 787
Cdd:TIGR01369 324 LAVGYTLDELKNPVTGTTpASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 788 VGFDHT---VKPVSD--MELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDL 862
Cdd:TIGR01369 404 TGFDLPdreVEPDEDlwRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 863 LQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRT-PHVLVLGSG 941
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDkKKVLVLGSG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 942 VYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPN 1021
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1022 NMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVA 1101
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1102 YTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLER 1181
Cdd:TIGR01369 724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1182 IKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVG--LMTGSGVV 1259
Cdd:TIGR01369 804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1260 GVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLG 1339
Cdd:TIGR01369 884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1340 YSLYASLGTADFYTEHGVKVTAVDWHFEEAvdgecppqRSILEQLAEKNFELVINLSMRGAGgrrlssFVTKGYRTRRLA 1419
Cdd:TIGR01369 964 YKLYATEGTAKFLGEAGIKPELVLKVSEGR--------PNILDLIKNGEIELVINTTSKGAG------TATDGYKIRREA 1029
|
1050 1060
....*....|....*....|.
gi 18105007 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: 1430.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVL 473
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVL 553
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 554 VRAAFALGGLGSGFASNREELSALVAPAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGES 631
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 632 IVVAPSQTLNDREYQLLRQTAIKVTQHLGIV-GECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLA 710
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 711 LGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVG 789
Cdd:PRK05294 328 VGYTLDEIKNDITGKTpASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 790 FDHTVKPVSDME-----LETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHrGQPLPPDLLQ 864
Cdd:PRK05294 408 LDEDLFEEESLEelreeLKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEN-GLPLDAELLR 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 865 QAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYR 944
Cdd:PRK05294 487 EAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNR 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 945 IGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMA 1024
Cdd:PRK05294 567 IGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1025 MALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTD 1104
Cdd:PRK05294 647 KALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDE 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1105 GDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaSDGVVAAIA-ISEHVENAGVHSGDATLVTPPQDITAKTLERIK 1183
Cdd:PRK05294 727 EELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEDVLIGgIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIR 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1184 AIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTG--SGVVGV 1261
Cdd:PRK05294 806 EYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGliPPYVAV 885
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1262 KVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKK-NILLTIgSYKNKSELLPTVRLLESLGY 1340
Cdd:PRK05294 886 KEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLELGF 964
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1341 SLYASLGTADFYTEHGVKVTAVDWHFEEAVDgecppqrsILEQLAEKNFELVINlSMRGAGGRRlssfvtKGYRTRRLAA 1420
Cdd:PRK05294 965 KILATSGTAKFLREAGIPVELVNKVHEGRPH--------IVDLIKNGEIDLVIN-TPTGRQAIR------DGFSIRRAAL 1029
|
1050 1060
....*....|....*....|
gi 18105007 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: 1083.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVL 473
Cdd:PRK12815 8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVL 553
Cdd:PRK12815 88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 554 VRAAFALGGLGSGFASNREELSALVAPAFA--HTSQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGES 631
Cdd:PRK12815 168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQasPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 632 IVVAPSQTLNDREYQLLRQTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLAL 711
Cdd:PRK12815 248 IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 712 GIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALR--MVDENCV 788
Cdd:PRK12815 328 GYTLNELKNPVTGLTyASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRslEIKRNGL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 789 GFDHTVKPVSDMEL----ETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQpLPPDLLQ 864
Cdd:PRK12815 408 SLPIELSGKSDEELlqdlRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLD-LSADLLR 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 865 QAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTH-DLTFRTPHVLVLGSGVY 943
Cdd:PRK12815 487 KVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEaEPSSEKKKVLILGSGPI 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 944 RIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNM 1023
Cdd:PRK12815 567 RIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTAINL 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1024 AMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYT 1103
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYD 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1104 DGDLERFLssAAAVSKEHPVVISKFIqEAKEIDVDAVaSDGVVAAIA-ISEHVENAGVHSGDATLVTPPQDITAKTLERI 1182
Cdd:PRK12815 727 EPALEAYL--AENASQLYPILIDQFI-DGKEYEVDAI-SDGEDVTIPgIIEHIEQAGVHSGDSIAVLPPQSLSEEQQEKI 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1183 KAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMG----EEVEPVGLMTGSGV 1258
Cdd:PRK12815 803 RDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGkslaELGYPNGLWPGSPF 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1259 VGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESL 1338
Cdd:PRK12815 883 IHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLARRFAQL 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1339 GYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILEQLAEKNFELVINLSMRGAGGRrlssfvtKGYRTRRL 1418
Cdd:PRK12815 963 GFKLLATEGTANWLAEEGITTGVVEKVQEG--------SPSLLERIKQHRIVLVVNTSLSDSASE-------DAIKIRDE 1027
|
1050 1060 1070
....*....|....*....|....*....|
gi 18105007 1419 AADFSVPLIIDIKCTKLFVEALGQIGPAPP 1448
Cdd:PRK12815 1028 ALSTHIPVFTELETAQAFLQVLESLALTTQ 1057
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
394-1440 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 884.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVL 473
Cdd:PLN02735 24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLG-YPV 552
Cdd:PLN02735 104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 553 LVRAAFALGGLGSGFASNREELSALVAPAFA--HTSQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGE 630
Cdd:PLN02735 184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAasITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 631 SIVVAPSQTLNDREYQLLRQTAIKVTQHLGIvgEC---NVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAA 707
Cdd:PLN02735 264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 708 KLALGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDEN 786
Cdd:PLN02735 342 KLSVGYTLDQIPNDITLKTpASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 787 CVGFdhTVKPVSDME---------LETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQP 857
Cdd:PLN02735 422 FSGW--GCAKVKELDwdweqlkykLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLSE 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 858 LPPDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLV 937
Cdd:PLN02735 500 LSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLI 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 938 LGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGG 1017
Cdd:PLN02735 580 LGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGG 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1018 QLPNNMAMALHRQ-------------QCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYP 1084
Cdd:PLN02735 660 QTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYP 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1085 CVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVA-SDGVVAAIAISEHVENAGVHSG 1163
Cdd:PLN02735 740 VVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSG 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1164 DATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQL-IAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVI 1242
Cdd:PLN02735 820 DSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVM 899
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1243 MG---------EEVEPVGlmtgsgvVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKK 1313
Cdd:PLN02735 900 SGkslkdlgftEEVIPAH-------VSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLS 972
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1314 NILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAV-DWHfeeavdgECPPQrsILEQLAEKNFELV 1392
Cdd:PLN02735 973 GTVFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVlKLH-------EGRPH--AGDMLANGQIQLM 1043
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*...
gi 18105007 1393 INLSMRGAGGRRlssfvtKGYRTRRLAADFSVPLIIDIKCTKLFVEAL 1440
Cdd:PLN02735 1044 VITSSGDALDQK------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: 653.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 399 LGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGG 478
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 479 QTALNCGVELTKAGVLAryGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAF 558
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 559 ALGGLGSGFASNREELSALVAPAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAP 636
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVspDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 637 SQTLNDREYQLLRQTAIKVTQHLGIVGECNVQYALNpeSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 717 ELRNSvTGgtaaFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDencVGFDHTV-- 794
Cdd:COG0458 317 ELGND-TG----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLE---IGLPGTVll 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 795 KPVSD-----MELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHrgqPLPPDLLQQAKCL 869
Cdd:COG0458 389 SLVADddkeeALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEI---ILVINTLLGAKSL 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18105007 870 GFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGS 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: 631.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1460 KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1539
Cdd:cd01316 1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1540 ENAGTLGTVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKE 1619
Cdd:cd01316 81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1620 EILLIKAAKARGLPVTCEVAPHHLFLSHDDLERlgpGKGEVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSR 1699
Cdd:cd01316 161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPR---GQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1700 PPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKV 1779
Cdd:cd01316 238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317
|
330 340
....*....|....*....|....*..
gi 18105007 1780 KGTVRRVVLRGEVAYIDGQVLVPPGYG 1806
Cdd:cd01316 318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
938-1440 |
2.99e-175 |
|
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: 546.78 E-value: 2.99e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 938 LGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGG 1017
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1018 QLPNNMAMALHRQQ----CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVL 1093
Cdd:COG0458 81 QTALNLAVELEEAGilegVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1094 SGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaSDGV--VAAIAISEHVENAGVHSGDATLVTPP 1171
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVV-RDGEdnVIIVGIMEHIEPAGVHSGDSICVAPP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1172 QDITAKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVG 1251
Cdd:COG0458 240 QTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1252 LMTG----SGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKnILLTIGSYKNKSE 1327
Cdd:COG0458 320 NDTGfeptLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGT-VLLSLVADDDKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1328 LLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILEQLAEKNFELVINLSMRGAGGRRLSS 1407
Cdd:COG0458 399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEG--------RPIIVDEIELEEIILVINTLLGAKSLGDSDG 470
|
490 500 510
....*....|....*....|....*....|....*....
gi 18105007 1408 F------VTKGYRTRRLAADFSVPLIIDIKCTKLFVEAL 1440
Cdd:COG0458 471 IirralaAKVPYVTTLAAAAAAALAIKAVETEAGEFEEA 509
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-355 |
8.87e-160 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 496.52 E-value: 8.87e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1 MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSG 80
Cdd:PRK12564 4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 81 IHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLP-----FLDPNA 155
Cdd:PRK12564 75 PHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 156 RPLVPEVSIKTPRVFNTGGA---PRILALDCGLKYNQIRCLCQRGAEVTVVPWD---HALDSQEYEGLFLSNGPGDPASY 229
Cdd:PRK12564 155 LDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPAAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 230 PSVVSTLSRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWA 309
Cdd:PRK12564 235 DYAIEMIRELLEKK--IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 18105007 310 PLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLE 355
Cdd:PRK12564 313 VTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
2-359 |
3.84e-158 |
|
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: 491.76 E-value: 3.84e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:TIGR01368 1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDE---------DAESKGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVqngTEPSSLPFL------DPNA 155
Cdd:TIGR01368 72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVIS---TEDSNDEELvekarvSPDI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 156 RP--LVPEVSIKTPRVFN--TGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALDS-QEYE--GLFLSNGPGDPAS 228
Cdd:TIGR01368 149 TGinLVAEVSTKEPYTWGqrGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEiKKYNpdGIFLSNGPGDPAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 229 YPSVVSTLSRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPA-D 307
Cdd:TIGR01368 229 VEPAIETIRKLLEK---IPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgD 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 18105007 308 WAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKE 359
Cdd:TIGR01368 306 LEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
2-358 |
1.91e-154 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 481.83 E-value: 1.91e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:COG0505 5 ALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDE---------DFESDRP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSL-------PFLDPn 154
Cdd:COG0505 76 WVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELlekaraaPGMEG- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 155 aRPLVPEVSIKTPRVF--NTGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALD---SQEYEGLFLSNGPGDPASY 229
Cdd:COG0505 155 -LDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEeilALNPDGVFLSNGPGDPAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 230 PSVVSTLSRVLSEpnPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPA-DW 308
Cdd:COG0505 234 DYAIETIRELLGK--GIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 18105007 309 APLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVK 358
Cdd:COG0505 312 EVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| PyrB |
COG0540 |
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ... |
1919-2224 |
2.78e-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: 439.49 E-value: 2.78e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1919 HSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT 1998
Cdd:COG0540 1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1999 SSVQKGESLADSVQTMSCY-ADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2077
Cdd:COG0540 81 SSVSKGESLADTIRTLEAYgADAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2078 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPTVRAFVAsrgtkqEEFESIEEALPDTDVLYMTRIQKERFGSTQ- 2156
Cdd:COG0540 161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEIEELGV------EVTTDLDEALPDADVVYMLRIQKERFTDGLf 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18105007 2157 -EYEACFGQFILTPHIMTRAKKKMVVMH--PMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2224
Cdd:COG0540 234 pSYREYKRSYGLTAERLALAKPDAIVMHpgPRNRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
1461-1786 |
1.50e-128 |
|
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: 407.55 E-value: 1.50e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1461 LVRLPGLIDVHVHLREPGGT-HKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1539
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTtYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1540 EnaGTLGTVAGS----AAGLKLYLNETFSELRLDSVVQWMEHFETWPS-HLPIVAHAEqqtvaavlMVAQLTQ---RSVH 1611
Cdd:cd01302 81 G--DVTDELKKLfdagINSLKVFMNYYFGELFDVDDGTLMRTFLEIASrGGPVMVHAE--------RAAQLAEeagANVH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1612 ICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEVRPELGSRQDVEALWENMA--VIDCFASDHAP 1689
Cdd:cd01302 151 IAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGA-WGKVNPPLRSKEDREALWEGVKngKIDTIASDHAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1690 HTLEEKC----GSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQED---------TYVEVDLEH 1756
Cdd:cd01302 230 HSKEEKEsgkdIWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENPARIFGLYPKGTiavgydadlVIVDPKKEW 309
|
330 340 350
....*....|....*....|....*....|
gi 18105007 1757 EWTIPSHMpfSKAHWTPFEGQKVKGTVRRV 1786
Cdd:cd01302 310 KVTAEEIE--SKADWTPFEGMEVTGKPVST 337
|
|
| pyrB |
PRK00856 |
aspartate carbamoyltransferase catalytic subunit; |
1920-2224 |
1.01e-127 |
|
aspartate carbamoyltransferase catalytic subunit;
Pssm-ID: 234849 [Multi-domain] Cd Length: 305 Bit Score: 403.68 E-value: 1.01e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1920 SLVGQHILSVQQFTKDQMSHLFNVAHTLR-MMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT 1998
Cdd:PRK00856 2 PLKMKHLLSIEDLSREEIELLLDTAEEFKeVLRREVKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1999 SSVQKGESLADSVQTMSCY-ADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2077
Cdd:PRK00856 82 SSVSKGETLADTIRTLSAMgADAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2078 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPTVRAFvasrgtkqEEFESIEEALPDTDVLYMTRIQKERFG---- 2153
Cdd:PRK00856 162 VGDIKHSRVARSNIQALTRLGAEVRLIAPPTL-LPEGMPEY--------GVHTDLDEVIEDADVVMMLRVQKERMDggll 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18105007 2154 -STQEYeacFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2224
Cdd:PRK00856 233 pSYEEY---KRSYGLTAERLALAKPDAIVMHPGPvnRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLELLLGG 303
|
|
| PLN02527 |
PLN02527 |
aspartate carbamoyltransferase |
1924-2223 |
6.90e-127 |
|
aspartate carbamoyltransferase
Pssm-ID: 178142 [Multi-domain] Cd Length: 306 Bit Score: 401.43 E-value: 6.90e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1924 QHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEA--TSSV 2001
Cdd:PLN02527 1 SDVIEAQQFDREMLELLFEVAREMEKVERGSPGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENAgeFSSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2002 QKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDL 2081
Cdd:PLN02527 81 AKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATAEIPVINAGDGPGQHPTQALLDVYTIQREIGRLDGIKVGLVGDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2082 KHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFG-STQEYE 2159
Cdd:PLN02527 161 ANGRTVRSLAYLLAKYEdVKIYFVAPDVVKMKDDIKDYLTSKGVEWEESSDLMEVASKCDVLYQTRIQRERFGeRIDLYE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18105007 2160 ACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2223
Cdd:PLN02527 241 AARGKYIVDKKVMDVLPKHAVVMHPLPRLDEITTDVDSDPRAAYFRQAKNGLFIRMALLKLLLG 304
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
4-360 |
2.28e-126 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 401.96 E-value: 2.28e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 4 LVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEmdefglckwFESSGIHV 83
Cdd:PRK12838 5 LILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADD---------YESKQPQV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 84 AALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLPF----LDPNarpLV 159
Cdd:PRK12838 76 KGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDDAHAFDQIkalvLPKN---VV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 160 PEVSIKTPRVFNTGGaPRILALDCGLKYNQIRCLCQRGAEVTVVPWD---HALDSQEYEGLFLSNGPGDPASYPSVVSTL 236
Cdd:PRK12838 153 AQVSTKEPYTYGNGG-KHVALIDFGYKKSILRSLSKRGCKVTVLPYDtslEEIKNLNPDGIVLSNGPGDPKELQPYLPEI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 237 SRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSL-PADWAPLFTNA 315
Cdd:PRK12838 232 KKLISS---YPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRFFNV 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 18105007 316 NDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEA 360
Cdd:PRK12838 309 NDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKA 353
|
|
| asp_carb_tr |
TIGR00670 |
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ... |
1925-2223 |
6.24e-111 |
|
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: 355.51 E-value: 6.24e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1925 HILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEA-TSSVQK 2003
Cdd:TIGR00670 2 HLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFSDSeTSSVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2004 GESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKH 2083
Cdd:TIGR00670 82 GETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDLKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2084 GRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFG 2163
Cdd:TIGR00670 162 GRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEYEKVKG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2164 QFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2223
Cdd:TIGR00670 242 SYGITLERLEAAKKGVIIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
1437-1810 |
3.67e-105 |
|
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: 344.77 E-value: 3.67e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1437 VEALGQIGPAPPLKVHVDCmtSQKLVrLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPAL 1516
Cdd:COG0044 25 IAAIGPDLAAPEAAEVIDA--TGLLV-LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1517 ALAQKLAEAGARCDFALFLGASSENAGTL----GTVAGSAAGLKLYLNETFSELRLD----------------------- 1569
Cdd:COG0044 102 EFKLARAEEKALVDVGPHGALTKGLGENLaelgALAEAGAVAFKVFMGSDDGNPVLDdgllrraleyaaefgalvavhae 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1570 --SVVQWM---EHFETWPSHLPIV-AHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHL 1643
Cdd:COG0044 182 dpDLIRGGvmnEGKTSPRLGLKGRpAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1644 FLSHDDLERLGPgKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLT-AV 1718
Cdd:COG0044 262 TLTDEDLERYGT-NFKVNPPLRTEEDREALWEGLAdgTIDVIATDHAPHTLEEKELPFAeaPNGIPGLETALPLLLTeLV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1719 SEGRLSLDDLLQRLHHNPRRIFHLPP----QEDTY---VEVDLEHEWTI-PSHMpFSKAHWTPFEGQKVKGTVRRVVLRG 1790
Cdd:COG0044 341 HKGRLSLERLVELLSTNPARIFGLPRkgriAVGADadlVLFDPDAEWTVtAEDL-HSKSKNTPFEGRELTGRVVATIVRG 419
|
410 420
....*....|....*....|
gi 18105007 1791 EVAYIDGQVLVPPgYGQDVR 1810
Cdd:COG0044 420 RVVYEDGEVVGEP-RGRFLR 438
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
514-716 |
5.46e-103 |
|
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: 328.88 E-value: 5.46e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 514 DRRAFAARMAEIGEHVAPSEAA--NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHT------ 585
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 586 SQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLgiHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLGIVGEC 665
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18105007 666 NVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
178-354 |
1.47e-97 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 311.74 E-value: 1.47e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 178 ILALDCGLKYNQIRCLCQRGAEVTVVPWDHALD---SQEYEGLFLSNGPGDPASYPSVVSTLSRVLSEPnpRPVFGICLG 254
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEeilKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK--IPIFGICLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 255 HQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQ 334
Cdd:cd01744 79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158
|
170 180
....*....|....*....|
gi 18105007 335 FHPEHQAGPSDMELLFDIFL 354
Cdd:cd01744 159 FHPEASPGPHDTEYLFDEFL 178
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
1464-1790 |
4.52e-93 |
|
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: 306.57 E-value: 4.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGAS-SENA 1542
Cdd:cd01318 5 LPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTgSEDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1543 GTLgtVAGSAAGLKLYLNETFSELRLDsvvqwMEHFETWPSH--LPIVAHAEQQT------------------------- 1595
Cdd:cd01318 85 EEL--DKAPPAGYKIFMGDSTGDLLDD-----EETLERIFAEgsVLVTFHAEDEDrlrenrkelkgesahprirdaeaaa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1596 --VAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARglpVTCEVAPHHLFLSHDDLERLGpGKGEVRPELGSRQDVEAL 1673
Cdd:cd01318 158 vaTARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDRLG-TLGKVNPPLRSREDRKAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1674 WENMA--VIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP---PQE 1746
Cdd:cd01318 234 LQALAdgRIDVIASDHAPHTLEEKRKGYPaaPSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIFGIKnkgRIA 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 18105007 1747 DTY----VEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRG 1790
Cdd:cd01318 314 EGYdadlTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK08192 |
PRK08192 |
aspartate carbamoyltransferase; Provisional |
1923-2223 |
3.77e-92 |
|
aspartate carbamoyltransferase; Provisional
Pssm-ID: 169269 [Multi-domain] Cd Length: 338 Bit Score: 303.19 E-value: 3.77e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1923 GQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVL-SFSEATSSV 2001
Cdd:PRK08192 5 GSHILSVNQLDRDAIQRIFNVADRMEPYALREKRTRVLEGAILGNLFFEPSTRTRVSFGCAFNLLGGHVReTTGMASSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2002 QKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREEL----GTVNGMTITM 2077
Cdd:PRK08192 85 SKGESLYDTARVLSTYSDVIAMRHPDAGSVKEFAEGSRVPVINGGDGSNEHPTQALLDLFTIQKELahagRGIDGMHIAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2078 VGDLKHGRTVHSLACLLTQY-RVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQ 2156
Cdd:PRK08192 165 VGDLKFGRTVHSLSRLLCMYkNVSFTLVSPKELAMPDYVISDIENAGHKITITDQLEGNLDKADILYLTRIQEERFPSQE 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18105007 2157 EYEACFGQFILTPHIMTR-AKKKMVVMHPMPR-----VNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2223
Cdd:PRK08192 245 EANKYRGKFRLNQSIYTQhCKSNTVIMHPLPRdsraqANELDNDLNSHPNLAIFRQADNGLLIRMALFALTLG 317
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
1461-1796 |
5.42e-92 |
|
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: 305.52 E-value: 5.42e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSE 1540
Cdd:TIGR00857 35 LLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1541 NAGTLGT------VAGSAAGL----------KLYLNETfSELRLDSVVQWMEHFE---------------TWPSHLPIVA 1589
Cdd:TIGR00857 115 NQGKELTeayelkEAGAVGRMftddgsevqdILSMRRA-LEYAAIAGVPIALHAEdpdliyggvmhegpsAAQLGLPARP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1590 -HAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGpGKGEVRPELGSRQ 1668
Cdd:TIGR00857 194 pEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLD-GNGKVNPPLREKE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1669 DVEALWENMA--VIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP- 1743
Cdd:TIGR00857 273 DRLALIEGLKdgIIDIIATDHAPHTLEEKTKEFAaaPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPd 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 18105007 1744 --PQED----TYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYID 1796
Cdd:TIGR00857 353 kgTLEEgnpaDITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| PRK11891 |
PRK11891 |
aspartate carbamoyltransferase; Provisional |
1924-2223 |
5.52e-87 |
|
aspartate carbamoyltransferase; Provisional
Pssm-ID: 183362 [Multi-domain] Cd Length: 429 Bit Score: 291.77 E-value: 5.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1924 QHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT-SSVQ 2002
Cdd:PRK11891 88 PQLLSVDQFSRDSVEALFRVADVMQPIARRQKISRVLEGAVLGNLFFEASTRTRVSFGAAFCRLGGSVCDTTGFTfSSMA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2003 KGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREE---LG-TVNGMTITMV 2078
Cdd:PRK11891 168 KGESIYDTSRVMSGYVDALVIRHPEQGSVAEFARATNLPVINGGDGPGEHPSQALLDLYTIQREfsrLGkIVDGAHIALV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2079 GDLKHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGStQE 2157
Cdd:PRK11891 248 GDLKYGRTVHSLVKLLALYRgLKFTLVSPPTLEMPAYIVEQISRNGHVIEQTDDLAAGLRGADVVYATRIQKERFAD-ES 326
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18105007 2158 YEACFGQFILTPHIMTRA-KKKMVVMHPMPR-----VNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2223
Cdd:PRK11891 327 FEGYTPDFQINQALVDAVcKPDTLIMHPLPRdsrpgANDLSTDLNRDPRLAIFRQTDNGIPVRMAIFAVLLG 398
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1461-1796 |
7.56e-87 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 291.33 E-value: 7.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPA-----LALAQK-------------- 1521
Cdd:PRK09357 49 LVVAPGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVI-DTPEvveyvLDRAKEaglvdvlpvgaitk 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1522 ------------LAEAGARC---DfalflGASSENAGTLGTVAGSAAGLKLYLNETFSELRL-------DSVVQWMEHFE 1579
Cdd:PRK09357 128 glageeltefgaLKEAGVVAfsdD-----GIPVQDARLMRRALEYAKALDLLIAQHCEDPSLteggvmnEGEVSARLGLP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1580 TWPshlpivAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGE 1659
Cdd:PRK09357 203 GIP------AVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDP-NYK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1660 VRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCG--SRPPPGFPGLETMLPLLLTA-VSEGRLSLDDLLQRLHH 1734
Cdd:PRK09357 276 VNPPLRTEEDREALIEGLKdgTIDAIATDHAPHAREEKECefEAAPFGITGLETALSLLYTTlVKTGLLDLEQLLEKMTI 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18105007 1735 NPRRIFHLPP------QEDTYVEVDLEHEWTI-PSHMpFSKAHWTPFEGQKVKGTVRRVVLRGEVAYID 1796
Cdd:PRK09357 356 NPARILGLPAgplaegEPADLVIFDPEAEWTVdGEDF-ASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
2-358 |
2.94e-85 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 285.15 E-value: 2.94e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEmdefglckwFESSGI 81
Cdd:CHL00197 7 AILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLED---------IESVKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLG-------------KLVQNGTEPSSL 148
Cdd:CHL00197 78 QVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGcisnqnlnlsylrAKIKESPHMPSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 149 PFLDPNARPLVPEVSIKTPRVFN--------TGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALD---SQEYEGL 217
Cdd:CHL00197 158 DLIPRVTTSSYYEWDEKSHPSFYladnkrphSSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQdilSYQPDGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 218 FLSNGPGDPASYPSVVSTLSRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLvgSGRCFLTSQNHGF 297
Cdd:CHL00197 238 LLSNGPGDPSAIHYGIKTVKKLLKYN--IPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSGL--NQQVEITSQNHGF 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18105007 298 AVETDSLPADWAPL-FTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVK 358
Cdd:CHL00197 314 AVNLESLAKNKFYItHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIK 375
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
2-350 |
3.49e-76 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 260.30 E-value: 3.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemDEfglckwfESSGI 81
Cdd:PLN02771 57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFD--DE-------ESRQC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLV--QNGTEPSSLPF---LDPNAR 156
Cdd:PLN02771 128 FLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSteDSKTDEELLKMsrsWDIVGI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 157 PLVPEVSIKTPRV----------FNTGGAP----RILALDCGLKYNQIRCLCQRGAEVTVVP--WDhALDSQEY--EGLF 218
Cdd:PLN02771 208 DLISGVSCKSPYEwvdktnpewdFNTNSRDgesyHVIAYDFGIKHNILRRLASYGCKITVVPstWP-ASEALKMkpDGVL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 219 LSNGPGDPASYPSVVSTLSRVLSEPnprPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFA 298
Cdd:PLN02771 287 FSNGPGDPSAVPYAVETVKELLGKV---PVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYA 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 18105007 299 VETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLF 350
Cdd:PLN02771 364 VDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
1464-1803 |
6.45e-76 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 258.54 E-value: 6.45e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFAL-FLGASseNA 1542
Cdd:PRK04250 46 LPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALnFLIAG--NC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1543 GTLGTVagSAAGLKLYLNETFSELRLDSvvqWMEHFETWPSHLPIVAH--------------AEQQTVAAVLMVAQLTQR 1608
Cdd:PRK04250 124 EKAEEI--KADFYKIFMGASTGGIFSEN---FEVDYACAPGIVSVHAEdpelirefperppeAEVVAIERALEAGKKLKK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1609 SVHICHVARKEEILLIKaaKARGLPVTCEVAPHHLFLSHDDLERlGPgKGEVRPELGSRQDVEALWENMAVIDCFASDHA 1688
Cdd:PRK04250 199 PLHICHISTKDGLKLIL--KSNLPWVSFEVTPHHLFLTRKDYER-NP-LLKVYPPLRSEEDRKALWENFSKIPIIASDHA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1689 PHTLEEKcgSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPP------QEDTYVEVDLEHEWTIPS 1762
Cdd:PRK04250 275 PHTLEDK--EAGAAGIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIKNygieegNYANFAVFDMKKEWTIKA 352
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 18105007 1763 HMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1803
Cdd:PRK04250 353 EELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKP 393
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
4-138 |
1.83e-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: 246.47 E-value: 1.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 4 LVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEMdefglckwfESSGIHV 83
Cdd:pfam00988 1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDF---------ESDKIHV 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 18105007 84 AALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:pfam00988 72 AGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1464-1810 |
8.92e-73 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 251.11 E-value: 8.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGAS----- 1538
Cdd:PRK02382 53 LPGGIDVHVHFREPGYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTgnwdp 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1539 -----SENAGTLGTV--AGSAAGLKLYLnETFSEL-----RLDSVV--------------QWMEHFETWPSHLPI-VAHA 1591
Cdd:PRK02382 133 leslwERGVFALGEIfmADSTGGMGIDE-ELFEEAlaeaaRLGVLAtvhaededlfdelaKLLKGDADADAWSAYrPAAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1592 EQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKarglpVTCEVAPHHLFLSHDDLERLGPgKGEVRPELGSRQDVE 1671
Cdd:PRK02382 212 EAAAVERALEVASETGARIHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGT-FGKMNPPLRSEKRRE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1672 ALWE--NMAVIDCFASDHAPHTLEEKCGS--RPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQ-- 1745
Cdd:PRK02382 286 ALWErlNDGTIDVVASDHAPHTREEKDADiwDAPSGVPGVETMLPLLLAAVRKNRLPLERVRDVTAANPARIFGLDGKgr 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18105007 1746 -EDTY----VEVDLEHEWTIPSHMPFSKAHWTPFEGqkVKGTVRRVVL-RGEVAYIDGQVLVPPGYGQDVR 1810
Cdd:PRK02382 366 iAEGYdadlVLVDPDAAREIRGDDLHSKAGWTPFEG--MEGVFPELTMvRGTVVWDGDDINAKRGRGEFLR 434
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
2-138 |
1.92e-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: 234.96 E-value: 1.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:smart01097 3 AYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDE---------DFESDKI 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 18105007 82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:smart01097 74 QVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1442-1799 |
4.28e-71 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 246.12 E-value: 4.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1442 QIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPalALAQK 1521
Cdd:PRK07575 33 AIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRACAKGGVTSFLEMPNTKPLTTTQA--ALDDK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1522 LAEAGARC--DFALFLGASSENAGTLGTVAGsAAGLKLYLNETFSELRLDSVVQWMEHF-ETwpsHLPIVAHAEQQTV-- 1596
Cdd:PRK07575 111 LARAAEKCvvNYGFFIGATPDNLPELLTANP-TCGIKIFMGSSHGPLLVDEEAALERIFaEG---TRLIAVHAEDQARir 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1597 ---------------------AAVLMVAQLT-------QRSVHICHVARKEEILLIKAAKarGLPVTCEVAPHHLFLSHD 1648
Cdd:PRK07575 187 arraefagisdpadhsqiqdeEAALLATRLAlklskkyQRRLHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLNTD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1649 DLERLGPgKGEVRPELGSRQDVEALWENM--AVIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLS 1724
Cdd:PRK07575 265 AYERIGT-LAQMNPPLRSPEDNEALWQALrdGVIDFIATDHAPHTLEEKAQPYPnsPSGMPGVETSLPLMLTAAMRGKCT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1725 LDDLLQRLHHNPRRIFHLP------PQEDT-YVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDG 1797
Cdd:PRK07575 344 VAQVVRWMSTAVARAYGIPnkgriaPGYDAdLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRG 423
|
..
gi 18105007 1798 QV 1799
Cdd:PRK07575 424 QV 425
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1429-1810 |
3.49e-70 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 243.67 E-value: 3.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1429 DIKCTKLFVEALGQIGPAPPLKVhVDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRP 1508
Cdd:PRK09060 24 DIGIRDGRIAAIGDLSGASAGEV-IDC---RGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAAVLGGVTAVFEMPNTNP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1509 PIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTV--AGSAAGLKLYLNETFSELRLD---SVVQWME------- 1576
Cdd:PRK09060 100 LTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELerLPGCAGIKVFMGSSTGDLLVEddeGLRRILRngrrraa 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1577 -HFE---------------TWPSHlPIVAHAEqqtvAAVLM------VAQLTQRSVHICHVARKEEILLIKAAKARglpV 1634
Cdd:PRK09060 180 fHSEdeyrlrerkglrvegDPSSH-PVWRDEE----AALLAtrrlvrLARETGRRIHVLHVSTAEEIDFLADHKDV---A 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1635 TCEVAPHHLFLSHDDL-ERLGpGKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKcgSRP----PPGFPGL 1707
Cdd:PRK09060 252 TVEVTPHHLTLAAPECyERLG-TLAQMNPPIRDARHRDGLWRGVRqgVVDVLGSDHAPHTLEEK--AKPypasPSGMTGV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1708 ETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQ--------EDTYVeVDLEHEWTIPSHMPFSKAHWTPFEGQKV 1779
Cdd:PRK09060 329 QTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGIAGKgriavgydADFTI-VDLKRRETITNEWIASRCGWTPYDGKEV 407
|
410 420 430
....*....|....*....|....*....|.
gi 18105007 1780 KGTVRRVVLRGEVAYIDGQVLVPPGyGQDVR 1810
Cdd:PRK09060 408 TGWPVGTIVRGQRVMWDGELVGPPT-GEPVR 437
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
1453-1786 |
6.24e-70 |
|
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: 240.60 E-value: 6.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1453 VDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPAL--ALAQKLAEAGARCD 1530
Cdd:cd01317 5 IDA---EGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVI-DNPAVveLLKNRAKDVGIVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1531 FAL------FLGASSENAGTL---GTVAGSAAGLKLYLNETfselrLDSVVQWMEHFEtwpshLPIVAH----------- 1590
Cdd:cd01317 81 LPIgaltkgLKGEELTEIGELleaGAVGFSDDGKPIQDAEL-----LRRALEYAAMLD-----LPIIVHpedpslagggv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1591 ------------------AEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLER 1652
Cdd:cd01317 151 mnegkvasrlglpgippeAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALES 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1653 LGPGkGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCgsRP----PPGFPGLETMLPLLLT-AVSEGRLSL 1725
Cdd:cd01317 231 YDTN-AKVNPPLRSEEDREALIEALKdgTIDAIASDHAPHTDEEKD--LPfaeaPPGIIGLETALPLLWTlLVKGGLLTL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18105007 1726 DDLLQRLHHNPRRIFHLPPQEDTYVE------VDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRV 1786
Cdd:cd01317 308 PDLIRALSTNPAKILGLPPGRLEVGApadlvlFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
1461-1803 |
5.65e-64 |
|
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: 225.63 E-value: 5.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1539
Cdd:cd01315 48 LVVMPGLIDTHVHINEPGRTEWEGFETGTKAAAAGGITTIIDMPlNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1540 EN---------AGTLG---TVAGSAAGL-----KLYLNETFSEL-RLDSVVqwMEHFE------------------TWPS 1583
Cdd:cd01315 128 GNldqlrpldeAGVVGfkcFLCPSGVDEfpavdDEQLEEAMKELaKTGSVL--AVHAEnpeitealqeqakakgkrDYRD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1584 HL---PIVAhaEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEV 1660
Cdd:cd01315 206 YLasrPVFT--EVEAIQRILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGT-EFKC 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1661 RPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRPP-----PGFPGLETMLPLLLT-AVSEGRLSLDDLLQRL 1732
Cdd:cd01315 283 APPIRDAANQEQLWEALEngDIDMVVSDHSPCTPELKLLGKGDffkawGGISGLQLGLPVMLTeAVNKRGLSLEDIARLM 362
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18105007 1733 HHNPRRIFHLPPQEDT--------YVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1803
Cdd:cd01315 363 CENPAKLFGLSHQKGRiavgydadFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVGEP 441
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
179-355 |
7.66e-61 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 207.09 E-value: 7.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 179 LALDCGL--KYNQIRCLCQRGAEVTVVPWDH---ALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVLsePNPRPVFGICL 253
Cdd:pfam00117 1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTpaeEILEENPDGIILSGGPGSPGAAGGAIEAIREAR--ELKIPILGICL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 254 GHQLLALAIGAKTYKM-RYGNRGHNQPC------LLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHN 326
Cdd:pfam00117 79 GHQLLALAFGGKVVKAkKFGHHGKNSPVgddgcgLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHK 158
|
170 180
....*....|....*....|....*....
gi 18105007 327 SLPFFSVQFHPEHQAGPSDMELLFDIFLE 355
Cdd:pfam00117 159 KLPIFGVQFHPESILTPHGPEILFNFFIK 187
|
|
| ArgF |
COG0078 |
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine ... |
1920-2224 |
1.33e-56 |
|
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: 199.51 E-value: 1.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1920 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1999
Cdd:COG0078 2 NLKGRHFLSLLDLTPEELRALLDLAAELKAKRKAGIPHRPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIYLDPGDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2000 SVQKGESLADSVQTMSCYADVVVLR-HPQPGAVELaAKHCRRPVINA-GDgvGEHPTQALLDIFTIREELGTVNGMTITM 2077
Cdd:COG0078 82 QLGRGESIKDTARVLSRYVDGIMIRtFGHETLEEL-AKYAGVPVINGlTD--LFHPCQALADLLTIREHFGKLKGLKVAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2078 VGDlkhGRTV-HSLACLLTQYRVSLRYVAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLY------MTR 2146
Cdd:COG0078 159 VGD---GNNVaNSLLLAAAKLGMDVRIATPEGYEPDPEIvakaKEIAAESGGSITITHDPAEAVKGADVVYtdvwvsMGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2147 iQKERfgstQEYEACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEV-DSdPRAAYFRQAENGMYIRMALLATVLG 2223
Cdd:COG0078 236 -EEEA----EERIKAFKPYQVNEELMALAKPDAIFMHCLPahRGEEVTDEViDG-PQSVVFDEAENRLHAQKALLAWLLG 309
|
.
gi 18105007 2224 R 2224
Cdd:COG0078 310 G 310
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
799-921 |
3.91e-56 |
|
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: 190.74 E-value: 3.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 799 DMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIAL 878
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 18105007 879 AVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTY 921
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| OTCace_N |
pfam02729 |
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain; |
1925-2065 |
3.81e-55 |
|
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
Pssm-ID: 460665 [Multi-domain] Cd Length: 140 Bit Score: 188.79 E-value: 3.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1925 HILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKG 2004
Cdd:pfam02729 1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKLPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSSG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18105007 2005 ESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGdGVGEHPTQALLDIFTIRE 2065
Cdd:pfam02729 81 ESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1464-1799 |
1.61e-54 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 198.17 E-value: 1.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAG 1543
Cdd:PRK09236 53 LPGMIDDQVHFREPGLTHKGDIASESRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNLD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1544 TLGTV-AGSAAGLKLY---------------LNETFSELRL---------DSVVQWMEHF-ETWPSHLPIVAHAEQQTVA 1597
Cdd:PRK09236 133 EIKRLdPKRVCGVKVFmgastgnmlvdnpetLERIFRDAPTliathcedtPTIKANLAKYkEKYGDDIPAEMHPLIRSAE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1598 AVL----MVAQLTQRS---VHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGpGKGEVRPELGSRQDV 1670
Cdd:PRK09236 213 ACYksssLAVSLAKKHgtrLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLG-NLIKCNPAIKTASDR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1671 EALWENMA--VIDCFASDHAPHTLEEKCGS--RPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLppQE 1746
Cdd:PRK09236 292 EALRQALAddRIDVIATDHAPHTWEEKQGPyfQAPSGLPLVQHALPALLELVHEGKLSLEKVVEKTSHAPAILFDI--KE 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18105007 1747 DTY---------VEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQV 1799
Cdd:PRK09236 370 RGFiregywadlVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQL 431
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1464-1811 |
8.89e-53 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 193.38 E-value: 8.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENA 1542
Cdd:PRK06189 53 FPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1543 GTLGTVA-GSAAGLKLYLNETFSE-----------------LRLDSVVQWMEHFETWPSHLPIVAHAEQQT--------- 1595
Cdd:PRK06189 133 EHLRELAeAGVIGFKAFMSNSGTDefrssddltlyegmkeiAALGKILALHAESDALTRHLTTQARQQGKTdvrdylesr 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1596 -----VAAV---LMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEVRPELGSR 1667
Cdd:PRK06189 213 pvvaeLEAVqraLLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGA-VAKCAPPLRSR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1668 QDVEALWENMAV--IDCFASDHAPHTLEEKCGS---RPPPGFPGLETMLPLLLT-AVSEGRLSLDDLLQRLHHNPRRIFH 1741
Cdd:PRK06189 292 SQKEELWRGLLAgeIDMISSDHSPCPPELKEGDdffLVWGGISGGQSTLLVMLTeGYIERGIPLETIARLLATNPAKRFG 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18105007 1742 LPP-------QEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVlVPPGYGQDVRK 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 |
5.28e-48 |
|
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: 179.12 E-value: 5.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1461 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1539
Cdd:TIGR03178 47 LVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAAGGITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1540 ENAGTLGTVAGSAA-GLKLYLN----ETFSELRLDSVVQWME-----------HFETwPSHL-----------PIVAH-- 1590
Cdd:TIGR03178 127 YNLDDLRELDEAGVvGFKAFLSpsgdDEFPHVDDWQLYKGMRelarlgqlllvHAEN-PAITsalgeeappqgGVGADay 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1591 -------AEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEVRPE 1663
Cdd:TIGR03178 206 lasrpvfAEVEAIRRTLALAKVTGCRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGT-LAKCAPP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1664 LGSRQDVEALWENMA--VIDCFASDHAPHTLEEKC--------GsrpppGFPGLETMLPLLLTAVSEGR-LSLDDLLQRL 1732
Cdd:TIGR03178 285 IRDLANQEGLWEALLngLIDCVVSDHSPCTPDLKRagdffkawG-----GIAGLQSTLDVMFDEAVQKRgLPLEDIARLM 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18105007 1733 HHNPRRIFHLP------PQEDT-YVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1803
Cdd:TIGR03178 360 ATNPAKRFGLAqkgriaPGKDAdFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFIGAP 437
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
1464-1804 |
2.07e-47 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 175.72 E-value: 2.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPAlALAQKLAE--AGARCDFALFLGA--SS 1539
Cdd:PRK00369 46 LPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPL-NTPE-AITEKLAEleYYSRVDYFVYSGVtkDP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1540 ENAGTLGTvagsaAGLKLYLNETfseLRLDSVVQWMEhfetwpSHLPIVAHAEQQTV--------------AAVLMVAQL 1605
Cdd:PRK00369 124 EKVDKLPI-----AGYKIFPEDL---EREETFRVLLK------SRKLKILHPEVPLAlksnrklrrncwyeIAALYYVKD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1606 TQRsVHICHVARKEEILLikaAKARGLpvTCEVAPHHLFLshddlERLGPGKGEVRPELGSRQDVEALWENMAVIDCFAS 1685
Cdd:PRK00369 190 YQN-VHITHASNPRTVRL---AKELGF--TVDITPHHLLV-----NGEKDCLTKVNPPIRDINERLWLLQALSEVDAIAS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1686 DHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPpqeDTYVEVDLEHEWTIPS- 1762
Cdd:PRK00369 259 DHAPHSSFEKLQPYEvcPPGIAALSFTPPFIYTLVSKGILSIDRAVELISTNPARILGIP---YGEIKEGYRANFTVIQf 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 18105007 1763 -----HMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPG 1804
Cdd:PRK00369 336 edwrySTKYSKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKG 382
|
|
| pyrB |
PRK13814 |
aspartate carbamoyltransferase; |
1925-2224 |
4.29e-46 |
|
aspartate carbamoyltransferase;
Pssm-ID: 139876 [Multi-domain] Cd Length: 310 Bit Score: 169.51 E-value: 4.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1925 HILSVQQFTKDQMSHLFNVA-HTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQK 2003
Cdd:PRK13814 7 HLLNMRSLTRDHIEKLIQRAnYFLTQGMEKNSVFETLKGHVVANLFFEPSTRTRNSFEIAAKRLGAMVLNPNLKISAISK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2004 GESLADSVQTMSCYA-DVVVLRHPQPGAVELAAKHCRRPV-INAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDL 2081
Cdd:PRK13814 87 GETLFDTIKTLEAMGvYFFIVRHSENETPEQIAKQLSSGVvINAGDGNHQHPSQALIDLMTIKQHKPHWNKLCVTIIGDI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2082 KHGRTVHSLA-CLLTQYRVSLRYVAPPSLrMPPTVrafvasRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEA 2160
Cdd:PRK13814 167 RHSRVANSLMdGLVTMGVPEIRLVGPSSL-LPDKV------GNDSIKKFTELKPSLLNSDVIVTLRLQKERHDNSVDIDA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18105007 2161 CFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2224
Cdd:PRK13814 240 FRGSFRLTPEKLYSAKPDAIVMHPGPvnREVEINSDVADNQQSVILQQVRNGVAMRMAVLELFLLR 305
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
1464-1811 |
5.79e-46 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 171.96 E-value: 5.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1464 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAG 1543
Cdd:PRK01211 45 LPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1544 TLGTVagsAAGLKLYLNETFSELRLDSVVQWMEHFETwpSHLPIVAHAEQQ------------------------TVAAV 1599
Cdd:PRK01211 125 ILDER---SIGLKVYMGGTTNTNGTDIEGGEIKKINE--ANIPVFFHAELSeclrkhqfesknlrdhdlarpiecEIKAV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1600 LMVAQLTQRSVHICHVARKEEIllikaakargLPVTCEVAPHHLFLsHDDLErLGpGKGEVRPELGSRQDVEALWENM-- 1677
Cdd:PRK01211 200 KYVKNLDLKTKIIAHVSSIDVI----------GRFLREVTPHHLLL-NDDMP-LG-SYGKVNPPLRDRWTQERLLEEYis 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1678 AVIDCFASDHAPHTLEEKCG-SRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQ--EDTY----V 1750
Cdd:PRK01211 267 GRFDILSSDHAPHTEEDKQEfEYAKSGIIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGIKKGkiEEGYdadfM 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18105007 1751 EVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTvRRVVLRGEVAyIDGQVLVPPGYGQDVRK 1811
Cdd:PRK01211 347 AFDFTNIKKINDKRLHSKCPVSPFNGFDAIFP-SHVIMRGEVV-IDNYELISERTGKFVPK 405
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
1439-1806 |
1.57e-44 |
|
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: 168.94 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1439 ALGQ-IGPAPPLKVhVDCmtSQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPA 1515
Cdd:cd01314 28 AIGPnLEAPGGVEV-IDA--TGKYV-LPGGIDPHTHLELPfmGTVTADDFESGTRAAAAGGTTTIIDFAIPNKGQSLLEA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1516 LALAQKLAEAGARCDFALFLGASSENAGT---LGTVAgsAAGL---KLYLneTFSELRLDSVVQWMEHFETWPSH--LPI 1587
Cdd:cd01314 104 VEKWRGKADGKSVIDYGFHMIITDWTDSVieeLPELV--KKGIssfKVFM--AYKGLLMVDDEELLDVLKRAKELgaLVM 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1588 VaHAEQQTVAAVL--------------------------------MVAQLTQRSVHICHVARKEEILLIKAAKARGLPVT 1635
Cdd:cd01314 180 V-HAENGDVIAELqkkllaqgktgpeyhalsrppeveaeataraiRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1636 CEVAPHHLFLSHDDLERLGP-GKGEV-RPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP-----PPGFPG 1706
Cdd:cd01314 259 GETCPQYLLLDDSDYWKDWFeGAKYVcSPPLRPKEDQEALWDGLSsgTLQTVGSDHCPFNFAQKARGKDdftkiPNGVPG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1707 LETMLPLLLTA-VSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVE--------VDLEHEWTIPSHMPFSKAHWTPFEGQ 1777
Cdd:cd01314 339 VETRMPLLWSEgVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVgsdadlviWDPNAEKTISADTHHHNVDYNIFEGM 418
|
410 420
....*....|....*....|....*....
gi 18105007 1778 KVKGTVRRVVLRGEVAYIDGQVLVPPGYG 1806
Cdd:cd01314 419 KVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| PRK00779 |
PRK00779 |
ornithine carbamoyltransferase; Provisional |
1920-2222 |
1.49e-43 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 234835 [Multi-domain] Cd Length: 304 Bit Score: 161.80 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1920 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1999
Cdd:PRK00779 1 MLMGRHFLSLDDLSPEELEELLDLAAELKKKRKAGEPHPPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIFLSPRDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2000 SVQKGESLADSVQTMSCYADVVVLR-HPQPGAVELaAKHCRRPVINA-GDgvGEHPTQALLDIFTIREELGTVNGMTITM 2077
Cdd:PRK00779 81 QLGRGEPIEDTARVLSRYVDAIMIRtFEHETLEEL-AEYSTVPVINGlTD--LSHPCQILADLLTIYEHRGSLKGLKVAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2078 VGDlkhGRTV-HSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVA-SRGTKQEEFESIEEALPDTDVLY------Mtriqk 2149
Cdd:PRK00779 158 VGD---GNNVaNSLLLAAALLGFDLRVATPKGYEPDPEIVEKIAkETGASIEVTHDPKEAVKGADVVYtdvwvsM----- 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18105007 2150 erfGSTQEYE---ACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVL 2222
Cdd:PRK00779 230 ---GQEAEAEerlKAFAPYQVNEELMALAKPDAIFMHCLPahRGEEVTDEVIDGPQSVVWDEAENRLHAQKALLAWLL 304
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1313-1438 |
6.23e-43 |
|
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: 152.84 E-value: 6.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1313 KNILLTIGSYkNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGEcppqRSILEQLAEKNFELV 1392
Cdd:cd01423 1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK----PSLRELLAEGKIDLV 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 18105007 1393 INLSMRGAGGRRLSsfvtkGYRTRRLAADFSVPLIIDIKCTKLFVE 1438
Cdd:cd01423 76 INLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
1442-1811 |
2.42e-42 |
|
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: 162.94 E-value: 2.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1442 QIGP--APPLKVHV-DCmtSQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPAL 1516
Cdd:TIGR02033 28 AVGDnlIPPDAVEViDA--TGKYV-LPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAAGGTTTIIDFVVPEKGSSLTEAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1517 ALAQKLAEAGARCDFALFLGASSENAGTLG-----TVAGSAAGLKLY-------------LNETFSELR----------- 1567
Cdd:TIGR02033 105 ETWHEKAEGKSVIDYGFHMDITHWNDSVLEehipeVKEEGINSFKVFmayknllmvddeeLFEILKRLKelgallqvhae 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1568 ----LDSVVQWM-EHFETWPSHLPIV--AHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAP 1640
Cdd:TIGR02033 185 ngdiIAELQARMlAQGITGPEYHALSrpPELEAEAVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1641 HHLFLSHDDLERLG--PGKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCG------SRPPPGFPGLETM 1710
Cdd:TIGR02033 265 QYLVLDDTHYDKPGfeGAKYVCSPPLREPEDQDALWSALSsgALQTVGSDHCTFNFAQKKAigkddfTKIPNGGPGVEER 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1711 LPLLLTA-VSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVE--------VDLEHEWTIPSHMPFSKAHWTPFEGQKVKG 1781
Cdd:TIGR02033 345 MSLLFDEgVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVgsdadiviWDPNRTTVISAETHHSNADYNPFEGFKVRG 424
|
410 420 430
....*....|....*....|....*....|
gi 18105007 1782 TVRRVVLRGEVAYIDGQVLVPPGYGQDVRK 1811
Cdd:TIGR02033 425 APVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
1442-1783 |
3.80e-41 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 158.23 E-value: 3.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1442 QIGPAPPLKVHVDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPAL--ALA 1519
Cdd:PRK07369 37 HIDPIPPDTQIIDA---SGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPPL-DNPATlaRLQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1520 QKLAE-AGARCDF--ALFLGASSENAGTLGT-----VAGSAAGLKLylnETFSELR--LDSVVQWMEHFETWPSHL---- 1585
Cdd:PRK07369 113 QQAQQiPPVQLHFwgALTLGGQGKQLTELAElaaagVVGFTDGQPL---ENLALLRrlLEYLKPLGKPVALWPCDRslag 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1586 ----------------PIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDD 1649
Cdd:PRK07369 190 ngvmregllalrlglpGDPASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1650 LERLGPgkgEVR--PELGSRQDVEALWENM--AVIDCFASDHAPHTLEEKCG--SRPPPGFPGLETMLPLLL-TAVSEGR 1722
Cdd:PRK07369 270 LASYDP---NLRldPPLGNPSDRQALIEGVrtGVIDAIAIDHAPYTYEEKTVafAEAPPGAIGLELALPLLWqNLVETGE 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18105007 1723 LSLDDLLQRLHHNPRRIFHLPP------QEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTV 1783
Cdd:PRK07369 347 LSALQLWQALSTNPARCLGQEPpslapgQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRV 413
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1460-1817 |
6.52e-41 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 158.80 E-value: 6.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1460 KLVrLPGLIDVHVHLREP-GGTH-KEDFASGTAAALAGGITMVC--AMPNTRPPIIDApaLALAQKLAEAGARCD--FAL 1533
Cdd:PRK08323 45 KYV-MPGGIDPHTHMEMPfGGTVsSDDFETGTRAAACGGTTTIIdfALQPKGQSLREA--LEAWHGKAAGKAVIDygFHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1534 FLGASSENAGT-LGTVAgsAAG---LKLYLN-------------ETFSELR-LDSVVqwMEHFE---------------- 1579
Cdd:PRK08323 122 IITDWNEVVLDeMPELV--EEGitsFKLFMAykgalmldddellRALQRAAeLGALP--MVHAEngdaiaylqakllaeg 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1580 -TWPSHLPIV--AHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPG 1656
Cdd:PRK08323 198 kTGPEYHALSrpPEVEGEATNRAIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWF 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1657 KGEVR---PELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCG------SRPPPGFPGLETMLPLLLTA-VSEGRLS 1724
Cdd:PRK08323 278 EGAKYvmsPPLRDKEHQDALWRGLQdgDLQVVATDHCPFCFEQKKQlgrgdfTKIPNGTPGVEDRMPLLFSEgVMTGRIT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1725 LDDLLQRLHHNPRRIFHLPPQEDTyVEV---------DLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYI 1795
Cdd:PRK08323 358 LNRFVELTSTNPAKIFGLYPRKGT-IAVgadadiviwDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVE 436
|
410 420
....*....|....*....|..
gi 18105007 1796 DGQVLVPPGYGQDVRKWPQGAV 1817
Cdd:PRK08323 437 DGEFRGKAGHGRFLKRKPFQAV 458
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
1460-1846 |
1.68e-38 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 151.77 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1460 KLVrLPGLIDVHVHLREPGGT---HKEDFASGTAAALAGGITMVC--AMPNTRPPIIDApaLALAQKLAEAGARCDFALF 1534
Cdd:PRK13404 50 RLV-LPGGVDSHCHIDQPSGDgimMADDFYTGTVSAAFGGTTTVIpfAAQHRGQSLREA--VEDYHRRAAGKAVIDYAFH 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1535 LGASSENAGTLG-----TVAGSAAGLKLYLneTFSELRLDS-------------------------VVQWM-----EHFE 1579
Cdd:PRK13404 127 LIVADPTEEVLTeelpaLIAQGYTSFKVFM--TYDDLKLDDrqildvlavarrhgamvmvhaenhdMIAWLtkrllAAGL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1580 TWPSH----LPIVAHAEQQTVAAVLmvAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERlgP 1655
Cdd:PRK13404 205 TAPKYhaisRPMLAEREATHRAIAL--AELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDR--P 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1656 G----KGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP----------PPGFPGLETMLPLLLTA-V 1718
Cdd:PRK13404 281 GmegaKYICSPPPRDKANQEAIWNGLAdgTFEVFSSDHAPFRFDDTDGKLAaganpsfkaiANGIPGIETRLPLLFSEgV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1719 SEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYV---EVDL-----EHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRG 1790
Cdd:PRK13404 361 VKGRISLNRFVALTSTNPAKLYGLYPRKGAIAigaDADIaiwdpDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRG 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 18105007 1791 EVAYIDGQVLVPPGYGQDVRKwpqgavpqlppsapatsemtTTPERPRRGIPGLPD 1846
Cdd:PRK13404 441 RVVVEDGELVAERGSGQFLAR--------------------SLPDRARPNGRLEPE 476
|
|
| OTCace |
pfam00185 |
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain; |
2074-2221 |
3.08e-38 |
|
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;
Pssm-ID: 425511 [Multi-domain] Cd Length: 154 Bit Score: 140.82 E-value: 3.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2074 TITMVGDlKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLYMTRIQ- 2148
Cdd:pfam00185 1 KIAYVGD-GHNNVAHSLIIAAAKLGMDVRLATPKGYPPDPEVldkaKKIAEKSGGSIEITDDPAEAVKGADVVYTDVWQs 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18105007 2149 ----KERFgstQEYEAcFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATV 2221
Cdd:pfam00185 80 mgqeKERE---ERLKA-FKPYQVNEELMKLAKKDAIFMHCLPahRGEEVTDDVFDGPRSVVFDQAENRLHAQKALLALL 154
|
|
| pyrB |
PRK13376 |
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase ... |
1920-2223 |
7.88e-35 |
|
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase regulatory subunit; Provisional
Pssm-ID: 237369 [Multi-domain] Cd Length: 525 Bit Score: 141.82 E-value: 7.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1920 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLD---ILKGKV-MASMFYEVSTRTSSSFA-AAMARLGGAVLSF 1994
Cdd:PRK13376 4 DFLGRTLAVIEDLSVEEQLFLYEKTRELKQRWYEGEDVSefrIKKRDVgIYIVFVEPSTRTKESFInAAKFHKNVKVNIF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1995 SEATSSVQKGESLADSVQTMSCYAD--VVVLRHPQPG--------AVELAAKH-CRRPV-INAGDGVGEHPTQALLDIFT 2062
Cdd:PRK13376 84 DSEHSSFNKQESYTDTFNMLTGYSDysIFIVRTRLEGvcrlleekVSEFASRNgIEVPAfINAGDGKHEHPTQELLDEFT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2063 IREELGTVNG-MTITMVGDLKHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTD 2140
Cdd:PRK13376 164 FLEQNNFDNSfIHIALVGDLLHGRTVHSKVNGLKIFKnVKVDLIAPEELAMPEHYVEKMKKNGFEVRIFSSIEEYLSQKD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2141 VL---YMTRIQKERFGStqeyeacfgQFILTPHIMTRA---KKKMV--------VMHPMPRVN---EISVEVDSDPRAAY 2203
Cdd:PRK13376 244 VAkiwYFTRLQLERMGE---------DILEKEHILRKAvtfRKEFLdklpegvkFYHPLPRHKvypTIPTFLDTLPLNGW 314
|
330 340
....*....|....*....|
gi 18105007 2204 FRQAENGMYIRMALLATVLG 2223
Cdd:PRK13376 315 ETQAINGYWVRIVLLSMLGG 334
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
801-877 |
2.82e-33 |
|
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: 124.03 E-value: 2.82e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18105007 801 ELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHrGQPLPPDLLQQAKCLGFSDKQIA 877
Cdd:pfam02787 2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEA-GLDLDAELLREAKRLGFSDRQIA 77
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
1443-1794 |
5.03e-33 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 134.42 E-value: 5.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1443 IGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPALA----- 1517
Cdd:PRK07627 33 IGQAPAGFNADKTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAAVAGGVTSLVCPPDTDPVL-DEPGLVemlkf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1518 LAQKLAEAGARCDFALFLGASSENAGTL------GTVAGSAAGLKLylnetfselrLDSVVQW--MEH-----FETWPSH 1584
Cdd:PRK07627 112 RARNLNQAHVYPLGALTVGLKGEVLTEMvelteaGCVGFSQANVPV----------VDTQVLLraLQYastfgFTVWLRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1585 LPI------VAH----------------AEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHH 1642
Cdd:PRK07627 182 LDAflgrggVAAsgavasrlglsgvpvaAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNH 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1643 LFLSHDDLERLGPgKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKC--GSRPPPGFPGLETMLPLLLTAV 1718
Cdd:PRK07627 262 VHLIDVDIGYFDS-QFRLDPPLRSQRDREAIRAALAdgTIDAICSDHTPVDDDEKLlpFAEATPGATGLELLLPLTLKWA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1719 SEGRLSLDDLLQRLHHNPRRIFHLPPQE-------DTYVeVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGE 1791
Cdd:PRK07627 341 DEAKVPLARALARITSAPARVLGLPAGRlaegapaDLCV-FDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQ 419
|
...
gi 18105007 1792 VAY 1794
Cdd:PRK07627 420 VAF 422
|
|
| PLN02342 |
PLN02342 |
ornithine carbamoyltransferase |
1882-2223 |
1.70e-32 |
|
ornithine carbamoyltransferase
Pssm-ID: 177976 [Multi-domain] Cd Length: 348 Bit Score: 131.07 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1882 MGTPDGTCYPPPPVPRQASPQNlGTPGLLHPQTSPLLHSLVG----QHILSVQQFTKDQMSHLFNVAHTLRMMVQK-ERS 1956
Cdd:PLN02342 1 MFFSLRRARSPSAVSSSSRARR-GLVVCAASSSAAAPSPIKGkskpKHFLHIDDFDKEEILGLLDRAKEVKALLKSgDRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1957 LDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLR---HPQpgAVEL 2033
Cdd:PLN02342 80 FQPFKGKSMAMIFTKPSMRTRVSFETGFFLLGGHALYLGPDDIQLGKREETRDIARVLSRYNDIIMARvfaHQD--VLDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2034 aAKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGDlkHGRTVHSLACLLTQYRVSLRYVAPPSLRMPP 2113
Cdd:PLN02342 158 -AEYSSVPVINGLTDY-NHPCQIMADALTIIEHIGRLEGTKVVYVGD--GNNIVHSWLLLAAVLPFHFVCACPKGYEPDA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2114 TVrafvaSRGTKQEEFESIE------EALPDTDVLY------MTriQKErfgstqEYE---ACFGQFILTPHIMTRAKKK 2178
Cdd:PLN02342 234 KT-----VEKARAAGISKIEitndpaEAVKGADVVYtdvwasMG--QKE------EAEkrkKAFQGFQVNEALMKLAGPQ 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 18105007 2179 MVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2223
Cdd:PLN02342 301 AYFMHCLPaeRGVEVTDGVMEAPNSIVFPQAENRMHAQNAIMLHQLG 347
|
|
| PLN02795 |
PLN02795 |
allantoinase |
1462-1797 |
5.15e-31 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 129.90 E-value: 5.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1462 VRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFALFLGASSE 1540
Cdd:PLN02795 96 VVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1541 NA------------GTLG----------------TVAGSAAGLK---------LYLNETFSELRLDSVVQ-----WMEHF 1578
Cdd:PLN02795 176 NAhnasvleelldaGALGlksfmcpsgindfpmtTATHIKAALPvlakygrplLVHAEVVSPVESDSRLDadprsYSTYL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1579 ETWPshlpivAHAEQQTVAAVLMVAQLTQR-------SVHICHVARKEEIL-LIKAAKARGLPVTCEVAPHHLFLSHDDL 1650
Cdd:PLN02795 256 KSRP------PSWEQEAIRQLLEVAKDTRPggvaegaHVHIVHLSDAESSLeLIKEAKAKGDSVTVETCPHYLAFSAEEI 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1651 erlgpGKGEVR----PELGSRQDVEALWENMA--VIDCFASDHAPHT-----LEEKCGSRPPPGFPGLETMLPLLLTAVS 1719
Cdd:PLN02795 330 -----PDGDTRykcaPPIRDAANRELLWKALLdgDIDMLSSDHSPSPpdlklLEEGNFLRAWGGISSLQFVLPATWTAGR 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1720 EGRLSLDDLLQRLHHNPRRIFHLP------PQEDTYVEV-DLEHEWTIPSHMPFSKAH--WTPFEGQKVKGTVRRVVLRG 1790
Cdd:PLN02795 405 AYGLTLEQLARWWSERPAKLAGLDskgaiaPGKDADIVVwDPEAEFVLDESYPIYHKHksLSPYLGTKLSGKVIATFVRG 484
|
....*..
gi 18105007 1791 EVAYIDG 1797
Cdd:PLN02795 485 NLVFLEG 491
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
1446-1794 |
5.25e-30 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 125.53 E-value: 5.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1446 APPLKVHVDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPpIIDAPAL--------- 1516
Cdd:PRK09059 44 APEGAEIVDC---AGKAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMPDTDP-VIDDVALvefvkrtar 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1517 -----------ALAQKLA-----------EAGARC----------------------DFALFLGASSENAgTLGtvagsA 1552
Cdd:PRK09059 120 dtaivnihpaaAITKGLAgeemtefgllrAAGAVAftdgrrsvantqvmrraltyarDFDAVIVHETRDP-DLG-----G 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1553 AGLklyLNETFselrldsvvqwmehFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGL 1632
Cdd:PRK09059 194 NGV---MNEGL--------------FASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQISCAESAEALRRAKDRGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1633 PVTCEVAPHHLFLSHDDLerlgpgkGEVR------PELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKcgsRPP--- 1701
Cdd:PRK09059 257 KVTAGVSINHLSLNENDI-------GEYRtffklsPPLRTEDDRVAMVEAVAsgTIDIIVSSHDPQDVDTK---RLPfse 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1702 --PGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP-------PQEDTYVeVDLEHEWTIPSHMPFSKAHWT 1772
Cdd:PRK09059 327 aaAGAIGLETLLAAALRLYHNGEVPLLRLIEALSTRPAEIFGLPagtlkpgAPADIIV-IDLDEPWVVDPEDLKSRSKNT 405
|
410 420
....*....|....*....|..
gi 18105007 1773 PFEGQKVKGTVRRVVLRGEVAY 1794
Cdd:PRK09059 406 PFEEARFQGRVVRTIVAGKTVY 427
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1454-1794 |
1.97e-29 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 124.20 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1454 DCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFA 1532
Cdd:PRK08044 42 EVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1533 LFLGASSENAGTLGTV-AGSAAGLKLYL--------NETFSELRLDSVVQWME-----------HFETWP--SHLPIVAH 1590
Cdd:PRK08044 122 QLGGLVSYNLDRLHELdEVGVVGFKCFVatcgdrgiDNDFRDVNDWQFYKGAQklgelgqpvlvHCENALicDELGEEAK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1591 AEQQTVAA-----------------VLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERL 1653
Cdd:PRK08044 202 REGRVTAHdyvasrpvfteveairrVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1654 GPgKGEVRPELGSRQDVEALWENM--AVIDCFASDHAPHTLEEKCGS--RPPPGFPGLETMLPLLL-TAVSEGRLSLDDL 1728
Cdd:PRK08044 282 GT-LAKCSPPIRDLENQKGMWEKLfnGEIDCLVSDHSPCPPEMKAGNimEAWGGIAGLQNCMDVMFdEAVQKRGMSLPMF 360
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18105007 1729 LQRLHHNPRRIFHL-------PPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAY 1794
Cdd:PRK08044 361 GKLMATNAADIFGLqqkgriaPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIY 433
|
|
| PRK14805 |
PRK14805 |
ornithine carbamoyltransferase; Provisional |
1924-2223 |
3.50e-26 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 237819 [Multi-domain] Cd Length: 302 Bit Score: 111.32 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1924 QHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSldILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQK 2003
Cdd:PRK14805 2 KHLLSIKELTQQQLLDLLALAKTIKANPAEYRQ--ALAGKSVVMLFEKPSLRTRVSFDIGINKLGGHCLYLDQQNGALGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2004 GESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGDlkh 2083
Cdd:PRK14805 80 RESVADFAANLSCWADAIVARVFSHSTIEQLAEHGSVPVINALCDL-YHPCQALADFLTLAEQFGDVSKVKLAYVGD--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2084 GRTV-HSL----ACLLTQYRVslryVAPPSLRMPPTV----RAFVASRGTKQEEFESIeEALPDTDVLYM-TRIQKERFG 2153
Cdd:PRK14805 156 GNNVtHSLmygaAILGATMTV----ICPPGHFPDGQIvaeaQELAAKSGGKLVLTSDI-EAIEGHDAIYTdTWISMGDDT 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18105007 2154 STQEYEACFGQFILTPHIMTRAKKKMvVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2223
Cdd:PRK14805 231 PLAEIKAKFAPYQVNKALMEKAGATF-VMHCQPahRGVEITSEVMDGEGSLILQQAENRMHAQNAVLVTLLS 301
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
1029-1247 |
8.82e-24 |
|
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: 103.03 E-value: 8.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1029 RQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLE 1108
Cdd:COG0439 36 AEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1109 RFL----SSAAAVSKEHPVVISKFIqEAKEIDVDAVASDGVVAAIAISEHvENAGVHSGDATLVTPPqDITAKTLERIKA 1184
Cdd:COG0439 116 AALaearAEAKAGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18105007 1185 IVHAVGQELQV-TGPFNLQ-LIAKDDQLKVIECNVRVS--RSFPFVSKTLGVDLVALATRVIMGEEV 1247
Cdd:COG0439 193 LVARALRALGYrRGAFHTEfLLTPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEPR 259
|
|
| PRK02102 |
PRK02102 |
ornithine carbamoyltransferase; Validated |
1921-2223 |
1.67e-23 |
|
ornithine carbamoyltransferase; Validated
Pssm-ID: 179366 [Multi-domain] Cd Length: 331 Bit Score: 104.20 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1921 LVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSS 2000
Cdd:PRK02102 5 LKGRSFLKLLDFTPEEIEYLIDLSIELKAAKKAGIEHQYLEGKNIALIFEKTSTRTRCAFEVAAIDLGAHVTYLGPNDSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2001 VQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGD 2080
Cdd:PRK02102 85 LGKKESIEDTARVLGRMYDGIEYRGFKQEIVEELAKYSGVPVWNGLTDE-WHPTQMLADFMTMKEHFGPLKGLKLAYVGD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2081 lkhGR--TVHSL---ACLLTqyrVSLRYVAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLYmTRI---- 2147
Cdd:PRK02102 164 ---GRnnMANSLmvgGAKLG---MDVRICAPKELWPEEELvalaREIAKETGAKITITEDPEEAVKGADVIY-TDVwvsm 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2148 --QKERfgstQEYEACFGQFILTPHIMTR-AKKKMVVMHPMP-----------------RVNEISV--EVDSDPRAAYFR 2205
Cdd:PRK02102 237 geEDEW----EERIKLLKPYQVNMDLMKAtGNPDVIFMHCLPafhdtetkvgkeiaekyGLKGLEVtdEVFESKYSIVFD 312
|
330
....*....|....*...
gi 18105007 2206 QAENGMYIRMALLATVLG 2223
Cdd:PRK02102 313 EAENRMHTIKAVMVATLG 330
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
187-338 |
8.11e-23 |
|
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: 97.99 E-value: 8.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 187 YNQIRCLCQRGAEVTVVPWDHALDSQE----YEGLFLSNGPGDPASYPSVVSTLSRVLSEpnpRPVFGICLGHQLLALAI 262
Cdd:cd01743 12 YNLVQYLRELGAEVVVVRNDEITLEELellnPDAIVISPGPGHPEDAGISLEIIRALAGK---VPILGVCLGHQAIAEAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 263 GAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWapLFTNANDgsnEGIV----HNSLPFFS 332
Cdd:cd01743 89 GGKVVRAPEPMHGktseihHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLL--EVTASTE---DGVImalrHRDLPIYG 163
|
....*.
gi 18105007 333 VQFHPE 338
Cdd:cd01743 164 VQFHPE 169
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
1467-1739 |
4.69e-22 |
|
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: 98.56 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1467 LIDVHVHLREPGGTH------------------KEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGAR 1528
Cdd:cd01292 1 FIDTHVHLDGSALRGtrlnlelkeaeelspedlYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1529 CDFALFLGASSENAGTLGTV------------AGSAAGLKLYLNETFSELRLDSVvqwMEHFETWPSH-LPIVAHAEQQT 1595
Cdd:cd01292 81 IRVVLGLGIPGVPAAVDEDAealllellrrglELGAVGLKLAGPYTATGLSDESL---RRVLEEARKLgLPVVIHAGELP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1596 VA--AVLMVAQLTQR--SVHICHVARKEEILLIKAAKArglPVTCEVAPHHLFLSHDDlerlgpgkgevrpelgsRQDVE 1671
Cdd:cd01292 158 DPtrALEDLVALLRLggRVVIGHVSHLDPELLELLKEA---GVSLEVCPLSNYLLGRD-----------------GEGAE 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18105007 1672 ALWENMA--VIDCFASDHAPHTLEekcgsrpppgfpglETMLPLLLTAVSEGRL--SLDDLLQRLHHNPRRI 1739
Cdd:cd01292 218 ALRRLLElgIRVTLGTDGPPHPLG--------------TDLLALLRLLLKVLRLglSLEEALRLATINPARA 275
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
460-714 |
4.72e-22 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 98.02 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 460 VTQVIRNERPDGVLltfggqtALNCGVELTKAGVLARYGVRvlGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLE 539
Cdd:COG0439 9 AAELARETGIDAVL-------SESEFAVETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 540 QAQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVA------PAFAHTSQVLVDKSLKGwKEIEYE-VVRDayGNC 612
Cdd:COG0439 80 EALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAearaeaKAGSPNGEVLVEEFLEG-REYSVEgLVRD--GEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 613 VtVCNM---ENLDPLGIHTGEsivVAPSQtLNDREYQLLRQTAIKVTQHLGIV-GECNVQYALNPESEqYYIIEVNARLS 688
Cdd:COG0439 157 V-VCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGE-PYLIEINARLG 230
|
250 260
....*....|....*....|....*...
gi 18105007 689 --RSSALASKATGYPLAYVAAKLALGIP 714
Cdd:COG0439 231 geHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
1048-1245 |
2.25e-21 |
|
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: 94.68 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1048 RFKFSRLLDTIGISQPQW--RELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKE----H 1121
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgnP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1122 PVVISKFIQEAKEIDVDAVAsDGVVAAIAISEhVENA-GVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFN 1200
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLR-DAHGNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18105007 1201 LQLI--AKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGE 1245
Cdd:pfam02786 160 VEFAldPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGY 206
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1327-1427 |
9.24e-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: 82.92 E-value: 9.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1327 ELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEA-VDGECppqrSILEQLAEKNFELVINLSMRGAGGRRl 1405
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEGrPGGRV----QIGDLIKNGEIDLVINTLYPFKATVH- 75
|
90 100
....*....|....*....|..
gi 18105007 1406 ssfvtKGYRTRRLAADFSVPLI 1427
Cdd:pfam02142 76 -----DGYAIRRAAENIDIPGP 92
|
|
| PRK04284 |
PRK04284 |
ornithine carbamoyltransferase; Provisional |
1920-2224 |
9.59e-19 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 235269 [Multi-domain] Cd Length: 332 Bit Score: 89.80 E-value: 9.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1920 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1999
Cdd:PRK04284 3 NLRNRSFLTLLDFTPKEIEYLLDLSEDLKRAKYAGIEVQKLKGKNIALIFEKDSTRTRCAFEVAAYDQGAHVTYLGPTGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2000 SVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINaGDGVGEHPTQALLDIFTIREEL-GTVNGMTITMV 2078
Cdd:PRK04284 83 QMGKKESTKDTARVLGGMYDGIEYRGFSQRTVETLAEYSGVPVWN-GLTDEDHPTQVLADFLTAKEHLkKPYKDIKFTYV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2079 GDlkhGRTVHSLACLLTQYRVSLRY--VAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLYM-------- 2144
Cdd:PRK04284 162 GD---GRNNVANALMQGAAIMGMDFhlVCPKELNPDDELlnkcKEIAAETGGKITITDDIDEGVKGSDVIYTdvwvsmge 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2145 -TRIQKERFGSTQEYEacfgqfiLTPHIMTRAKKKMVV-MHPMPRVN-------------------EISVEVDSDPRAAY 2203
Cdd:PRK04284 239 pDEVWEERIKLLKPYQ-------VNKEMMKKTGNPNAIfEHCLPSFHdldtkvgkeifekyglkemEVTDEVFESKASVV 311
|
330 340
....*....|....*....|.
gi 18105007 2204 FRQAENGMYIRMALLATVLGR 2224
Cdd:PRK04284 312 FDEAENRMHTIKAVMVATLGE 332
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
395-717 |
6.10e-17 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 84.55 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 395 KVLILGSGGlsigqagefdysGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLP-IT-PHYVTQVI---RNERP 469
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPkVTdPNYIDRLLdicKKEKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 470 DGVLLTFGgqtalncgVELtkaGVLARY-------GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQ 542
Cdd:PRK12767 71 DLLIPLID--------PEL---PLLAQNrdrfeeiGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 543 AA--AERLGYPVLVRAAFALGGLGSGFASNREELSalvaPAFAHTSQVLVDKSLKGwKEIEYEVVRDAYGNCVTVCNMEN 620
Cdd:PRK12767 140 AAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 621 LDPLGIHTGESIVVapsqtlndrEYQLLRQTAIKVTQHLGIVGECNVQYALNPesEQYYIIEVNARLSrssalaskaTGY 700
Cdd:PRK12767 215 IEVRAGETSKGVTV---------KDPELFKLAERLAEALGARGPLNIQCFVTD--GEPYLFEINPRFG---------GGY 274
|
330 340
....*....|....*....|....*.
gi 18105007 701 PLAYVA---------AKLALGIPLPE 717
Cdd:PRK12767 275 PLSYMAganepdwiiRNLLGGENEPI 300
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
177-351 |
8.02e-17 |
|
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: 81.92 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 177 RILALDCGLKYNQI-----RCLCQRGAEVTVV--------PWDHALDsqEYEGLFLSNGPG---DPASYPSVVSTLSRVL 240
Cdd:COG0518 1 KILILDHDPFGGQYpgliaRRLREAGIELDVLrvyageilPYDPDLE--DPDGLILSGGPMsvyDEDPWLEDEPALIREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 241 SEPNpRPVFGICLGHQLLALAIGAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVetDSLPADWAPLFTN 314
Cdd:COG0518 79 FELG-KPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelTEADPLFAGLPDEFTVWMSHGDTV--TELPEGAEVLASS 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 18105007 315 ANDgSNEGIVHNSlPFFSVQFHPEhqAGPSDMELLFD 351
Cdd:COG0518 156 DNC-PNQAFRYGR-RVYGVQFHPE--VTHTMMEAWLE 188
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1026-1249 |
3.90e-16 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 81.85 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1026 ALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQT--VGYPCVVRPSYVLSGAAMNVAYT 1103
Cdd:PRK12767 90 RFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKgeLQFPLFVKPRDGSASIGVFKVND 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1104 DGDLERFLSSAAavskehPVVISKFIQEaKEIDVDA-VASDGVVAAIAISEHVEnagVHSGDATlvtppQDITAKTLERI 1182
Cdd:PRK12767 170 KEELEFLLEYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGETS-----KGVTVKDPELF 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18105007 1183 KAIVHaVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFvSKTLGVDLVALATRVIMGEEVEP 1249
Cdd:PRK12767 235 KLAER-LAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL-SYMAGANEPDWIIRNLLGGENEP 299
|
|
| PRK12562 |
PRK12562 |
ornithine carbamoyltransferase subunit F; Provisional |
1918-2224 |
4.82e-16 |
|
ornithine carbamoyltransferase subunit F; Provisional
Pssm-ID: 105755 Cd Length: 334 Bit Score: 82.03 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1918 LHSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEA 1997
Cdd:PRK12562 1 MSGFYKKHFLKLLDFTPAELNSLLQLAAKLKADKKNGKEVARLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1998 TSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINaGDGVGEHPTQALLDIFTIREEL--GTVNGMTI 2075
Cdd:PRK12562 81 GSQIGHKESIKDTARVLGRMYDGIQYRGHGQEVVETLAEYAGVPVWN-GLTNEFHPTQLLADLLTMQEHLpgKAFNEMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2076 TMVGDLKH--GRTVHSLACLLTqyrVSLRYVAP----PSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLY------ 2143
Cdd:PRK12562 160 VYAGDARNnmGNSMLEAAALTG---LDLRLVAPqacwPEASLVAECSALAQKHGGKITLTEDIAAGVKGADFIYtdvwvs 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2144 MTRIQK---ERFGSTQEYEACFGQFILT--PHI------------MTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQ 2206
Cdd:PRK12562 237 MGEPKEkwaERIALLRGYQVNSKMMALTgnPQVkflhclpafhddQTTLGKKMAKEFGLHGGMEVTDEVFESPASIVFDQ 316
|
330
....*....|....*...
gi 18105007 2207 AENGMYIRMALLATVLGR 2224
Cdd:PRK12562 317 AENRMHTIKAVMVATLAK 334
|
|
| PRK03515 |
PRK03515 |
ornithine carbamoyltransferase subunit I; Provisional |
1924-2222 |
2.07e-15 |
|
ornithine carbamoyltransferase subunit I; Provisional
Pssm-ID: 179587 [Multi-domain] Cd Length: 336 Bit Score: 79.76 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1924 QHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQK 2003
Cdd:PRK03515 7 RHFLRLLDFTPAELNSLLQLAAKLKADKKNGKEEQKLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSGSQIGH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2004 GESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINagdGVGE--HPTQALLDIFTIREEL--GTVNGMTITMVG 2079
Cdd:PRK03515 87 KESIKDTARVLGRMYDGIQYRGYGQEIVETLAEYAGVPVWN---GLTNefHPTQLLADLLTMQEHLpgKAFNEMTLAYAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2080 DLKH--GRTVHSLACLLTqyrVSLRYVAP----PSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYM--------- 2144
Cdd:PRK03515 164 DARNnmGNSLLEAAALTG---LDLRLVAPkacwPEAALVTECRALAQKNGGNITLTEDIAEGVKGADFIYTdvwvsmgep 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2145 TRIQKERFGSTQEYEACFGQFILT--PHI------------MTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENG 2210
Cdd:PRK03515 241 KEVWAERIALLRPYQVNSKMMQLTgnPQVkflhclpafhddQTTLGKKMAEEYGLHGGMEVTDEVFESAHSIVFDQAENR 320
|
330
....*....|...
gi 18105007 2211 MY-IRMALLATVL 2222
Cdd:PRK03515 321 LHtIKAVMVATLS 333
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
187-338 |
2.17e-15 |
|
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: 76.62 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 187 YNQIRCLCQRGAEVTVVPWDH----ALDSQEYEGLFLSNGPGDPASYP---SVVSTLSRVLsepnprPVFGICLGHQLLA 259
Cdd:COG0512 12 YNLVQYLGELGAEVVVVRNDEitleEIEALAPDGIVLSPGPGTPEEAGislEVIRAFAGKI------PILGVCLGHQAIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 260 LAIGAKTYKMRY------------GN---RGHNQPcLLVgsGRcfltsqNHGFAVETDSLPAD-----WAPlftnanDGS 319
Cdd:COG0512 86 EAFGGKVVRAPEpmhgktspithdGSglfAGLPNP-FTA--TR------YHSLVVDRETLPDElevtaWTE------DGE 150
|
170
....*....|....*....
gi 18105007 320 NEGIVHNSLPFFSVQFHPE 338
Cdd:COG0512 151 IMGIRHRELPIEGVQFHPE 169
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
391-724 |
1.74e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 77.66 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 391 PPPRKVLILGS--GGLSIgqagefdysgsqaIKALKEENIQTLLInpniATVQTSQGL----ADKVYFLPITPH------ 458
Cdd:COG3919 3 TMRFRVVVLGGdiNALAV-------------ARSLGEAGVRVIVV----DRDPLGPAArsryVDEVVVVPDPGDdpeafv 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 459 -YVTQVIRNERPDgVLLTFGGQTALncgveltkagVLARY------GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP 531
Cdd:COG3919 66 dALLELAERHGPD-VLIPTGDEYVE----------LLSRHrdeleeHYRLPYPDADLLDRLLDKERFYELAEELGVPVPK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 532 SEAANSLEQAQAAAERLGYPVLVRAA--------FALGGLGSGFASNREELSALVAPAFAHTSQVLVDKSLKGWKEIEY- 602
Cdd:COG3919 135 TVVLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAGYELIVQEYIPGDDGEMRg 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 603 -EVVRDAYGNCVTVCNMENL--DPLGIhtGESIVVapsQTLNDREyqlLRQTAIKVTQHLGIVGECNVQYALNPESEQYY 679
Cdd:COG3919 215 lTAYVDRDGEVVATFTGRKLrhYPPAG--GNSAAR---ESVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYK 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 18105007 680 IIEVNARLSRSSALASKAtGYPLAYVAAKLALGIPLPELRNSVTG 724
Cdd:COG3919 287 LIEINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREG 330
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
493-717 |
3.49e-14 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 77.48 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 493 VLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASN 570
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDGAlKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 571 REEL--SALVAPAFAHTS----QVLVDKSLKGWKEIEYEVVRDAYGNCVTV----CNMENldplgiHTGESIVVAPSQTL 640
Cdd:PRK08462 176 ESDLenLYLAAESEALSAfgdgTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVL 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18105007 641 NDREYQLLRQTAIKVTQHLGIVGECNVQYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPE 717
Cdd:PRK08462 250 DEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPS 325
|
|
| PRK01713 |
PRK01713 |
ornithine carbamoyltransferase; Provisional |
1920-2222 |
3.82e-14 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 167263 [Multi-domain] Cd Length: 334 Bit Score: 76.18 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1920 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1999
Cdd:PRK01713 4 NLKNRHLLSLVNHTEREIKYLLDLSRDLKRAKYAGTEQQRLKGKNIALIFEKTSTRTRCAFEVAAYDQGAQVTYIDPNSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2000 SVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINagdGVGE--HPTQALLDIFTIREELGT-VNGMTIT 2076
Cdd:PRK01713 84 QIGHKESMKDTARVLGRMYDAIEYRGFKQSIVNELAEYAGVPVFN---GLTDefHPTQMLADVLTMIENCDKpLSEISYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2077 MVGDLKHGRTvHSLACLLTQYRVSLRYVAPPSL----RMPPTVRAFVASRGTKQEEFESIEEALPDTDVlymtrIQKERF 2152
Cdd:PRK01713 161 YIGDARNNMG-NSLLLIGAKLGMDVRICAPKALlpeaSLVEMCEKFAKESGARITVTDDIDKAVKGVDF-----VHTDVW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2153 GSTQEYEACFGQFI-------LTPHIMTR-AKKKMVVMHPMPRVN---------------------EISVEVDSDPRAAY 2203
Cdd:PRK01713 235 VSMGEPLETWGERIkllmpyqVTPELMKRtGNPKVKFMHCLPAFHnsetkvgrqiaekypelangiEVTEDVFESPMNIA 314
|
330
....*....|....*....
gi 18105007 2204 FRQAENGMYIRMALLATVL 2222
Cdd:PRK01713 315 FEQAENRMHTIKAVMVASL 333
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
929-1250 |
3.84e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 76.51 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 929 TFRTPHVLVLGSgvyrigssvefDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLY------FDEISF-EVVMD 1001
Cdd:COG3919 2 MTMRFRVVVLGG-----------DINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVvvpdpgDDPEAFvDALLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1002 IYELENPEGVILSMGGQLpnnMAMALHRQQ----CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQF 1077
Cdd:COG3919 71 LAERHGPDVLIPTGDEYV---ELLSRHRDEleehYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1078 CQTVGYPCVVRPSYvlSGAAMNV----------AYTDGDLERFLSSAAAVskEHPVVISKFI--QEAKEIDVDA-VASDG 1144
Cdd:COG3919 148 AEDLGFPVVVKPAD--SVGYDELsfpgkkkvfyVDDREELLALLRRIAAA--GYELIVQEYIpgDDGEMRGLTAyVDRDG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1145 VVAAIAISEHV----ENAGVHSgdATLVTPPQDItaktLERIKAIVHAVGqelqVTGPFNLQLI--AKDDQLKVIECNVR 1218
Cdd:COG3919 224 EVVATFTGRKLrhypPAGGNSA--ARESVDDPEL----EEAARRLLEALG----YHGFANVEFKrdPRDGEYKLIEINPR 293
|
330 340 350
....*....|....*....|....*....|..
gi 18105007 1219 VSRSFPFVSKTlGVDLVALATRVIMGEEVEPV 1250
Cdd:COG3919 294 FWRSLYLATAA-GVNFPYLLYDDAVGRPLEPV 324
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
187-338 |
3.90e-14 |
|
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.
Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 72.90 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 187 YNQIRCLCQRGAEVtVVPWDHALDSQEYEGL---FLSNGPGdpASYPSVVSTLSRVLSEPNPR-PVFGICLGHQLLALAI 262
Cdd:TIGR00566 13 YNLVQYFCELGAEV-VVKRNDSLTLQEIEALlplLIVISPG--PCTPNEAGISLEAIRHFAGKlPILGVCLGHQAMGQAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 263 GAKTYKMRYGNRGHNQPCLLVGSGRC------FLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFH 336
Cdd:TIGR00566 90 GGDVVRANTVMHGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFH 169
|
..
gi 18105007 337 PE 338
Cdd:TIGR00566 170 PE 171
|
|
| PRK04523 |
PRK04523 |
N-acetylornithine carbamoyltransferase; Reviewed |
1924-2224 |
7.32e-14 |
|
N-acetylornithine carbamoyltransferase; Reviewed
Pssm-ID: 235304 [Multi-domain] Cd Length: 335 Bit Score: 75.17 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1924 QHILSVQQFTKDQMSHLFNVAHTLRmmvQKERSlDILKGKVMASMFYEVSTRTSSSFAAAMARLGG-AV----------L 1992
Cdd:PRK04523 4 KHFLNTQDWSRAELDALLTQAAAFK---RNKLG-SALKGKSIALVFFNPSLRTRTSFELGAFQLGGhAVvlqpgkdawpI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1993 SFSEATssVQKG---ESLADSVQTMSCYADVVVLR----------HPQPGAVELAAKHCRRPVINAGDGVgeHPTQALLD 2059
Cdd:PRK04523 80 EFELGA--VMDGeteEHIREVARVLSRYVDLIGVRafpkfvdwskDRQDQVLNSFAKYSTVPVINMETIT--HPCQELAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2060 IFTIREELG-TVNGMTI------------TMVGD------LKHGRTVhSLACLLTQYRVSLRYVAppslrmppTVRAFVA 2120
Cdd:PRK04523 156 ALALQEHFGtTLRGKKYvltwtyhpkplnTAVANsalliaTRLGMDV-TLLCPTPDYILDERYMD--------WAEQNAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2121 SRGTKQEEFESIEEALPDTDVLYM----TRIQKERFGSTQEYEACFGQFILTPHIMTRAKKKmVVMH--PMPRVNEISVE 2194
Cdd:PRK04523 227 ESGGSLTVSHDIDSAYAGADVVYAkswgALPFFGNWEPEKPIRDQYQHFIVDERKMALTNNG-VFSHclPLRRNVKVTDA 305
|
330 340 350
....*....|....*....|....*....|
gi 18105007 2195 VDSDPRAAYFRQAENGMYIRMALLATVLGR 2224
Cdd:PRK04523 306 VMDSPNCIAIDEAENRLHVQKAIMAALASQ 335
|
|
| PRK14804 |
PRK14804 |
ornithine carbamoyltransferase; Provisional |
1924-2222 |
8.65e-14 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 173265 [Multi-domain] Cd Length: 311 Bit Score: 74.68 E-value: 8.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1924 QHILSVQQFTKDQMSHLFNVAhtlrMMVQKERS--LDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSV 2001
Cdd:PRK14804 7 KHLISWEDWSDSEILDLLDFA----VHVKKNRVnyAGHMSGRSLAMLFQKTSTRTRVSFEVAMTEMGGHGIYLDWMASNF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2002 QkgesLAD---SVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGeHPTQALLDIFTIREELGTV--NGMTIT 2076
Cdd:PRK14804 83 Q----LSDidlEARYLSRNVSVIMARLKKHEDLLVMKNGSQVPVINGCDNMF-HPCQSLADIMTIALDSPEIplNQKQLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2077 MVGdlKHGRTVHSLACLLTQYRVSLRYVAPPSLR---MPPTV-RAfvASRGTKQEEfESIEEALPDTDVLYMTRIQKERF 2152
Cdd:PRK14804 158 YIG--VHNNVVNSLIGITAALGIHLTLVTPIAAKeniHAQTVeRA--KKKGTLSWE-MNLHKAVSHADYVYTDTWLDMEF 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18105007 2153 GSTQEYEACFGQFI--LTPH-----IMTRAKKKmvVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVL 2222
Cdd:PRK14804 233 FNDPSYADKKKQRMelMMPYqinssLMEKTNAK--VMHDMPihAGYEITREVVLSDRSIIFQQAENRLDAQKAVILKLL 309
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
498-785 |
9.11e-14 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 76.22 E-value: 9.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 498 GVRVLGTPVETIELTEDRraFAAR--MAEIGEHVAP--SEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREE 573
Cdd:PRK06111 99 GIVFIGPSADIIAKMGSK--IEARraMQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 574 LSAlvapAFAHTSQ----------VLVDKSLKGWKEIEYEVVRDAYGNCVtvcnmenldplgiHTGE---SI------VV 634
Cdd:PRK06111 177 LTK----AFESNKKraanffgngeMYIEKYIEDPRHIEIQLLADTHGNTV-------------YLWErecSVqrrhqkVI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 635 --APSQTLNDREYQLLRQTAIKVTQHLGIVGECNVQYaLNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALG 712
Cdd:PRK06111 240 eeAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEF-LVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 713 IPLPELRNSVTGGTAAFE------------PSVDycvvKIPRWDLSK--FLRVSTKIGSCMK-------SVGEVMGIGRS 771
Cdd:PRK06111 319 EKLSFTQDDIKRSGHAIEvriyaedpktffPSPG----KITDLTLPGgeGVRHDHAVENGVTvtpfydpMIAKLIAHGET 394
|
330
....*....|....
gi 18105007 772 FEEAFQKALRMVDE 785
Cdd:PRK06111 395 REEAISRLHDALEE 408
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
491-716 |
2.04e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 75.14 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 491 AGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAAN--SLEQAQAAAERLGYPVLVRAAFALGGLGSGFA 568
Cdd:PRK07178 91 AEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNlaDLDEALAEAERIGYPVMLKATSGGGGRGIRRC 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 569 SNREELS-------ALVAPAFAhTSQVLVDKSLKGWKEIEYEVVRDAYGNCVTV----CNMENldplgiHTGESIVVAPS 637
Cdd:PRK07178 171 NSREELEqnfprviSEATKAFG-SAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPS 243
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18105007 638 QTLNDREYQLLRQTAIKVTQHLGIVGECNVQYALNPESEqYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:PRK07178 244 PQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGE-VYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLS 321
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
177-338 |
9.48e-13 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 69.69 E-value: 9.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 177 RILALDC--GLKYNQIRCLCQRGAEVTVV------PWDHALDSQEYEGLFLSNGPGDP----ASYPSVVSTLSRVLsepn 244
Cdd:PRK07765 2 RILVVDNydSFVFNLVQYLGQLGVEAEVWrnddprLADEAAVAAQFDGVLLSPGPGTPeragASIDMVRACAAAGT---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 245 prPVFGICLGHQLLALAIGA-----------KTYKMRYGNRGhnqpcLLVGSGRCFLTSQNHGFAVETDSLPADwapLFT 313
Cdd:PRK07765 78 --PLLGVCLGHQAIGVAFGAtvdrapellhgKTSSVHHTGVG-----VLAGLPDPFTATRYHSLTILPETLPAE---LEV 147
|
170 180
....*....|....*....|....*....
gi 18105007 314 NANDGSneGIV----HNSLPFFSVQFHPE 338
Cdd:PRK07765 148 TARTDS--GVImavrHRELPIHGVQFHPE 174
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
187-338 |
1.37e-12 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 68.62 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 187 YN---QIRCLcqrGAEVTVVPWDhALDSQEYE-----GLFLSNGPGDPA---SYPSVVSTLSRVLsepnprPVFGICLGH 255
Cdd:PRK05670 13 YNlvqYLGEL---GAEVVVYRND-EITLEEIEalnpdAIVLSPGPGTPAeagISLELIREFAGKV------PILGVCLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 256 QLLALAIGA-----------KTYKMRygnrgHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADwapLFTNA--NDGSNEG 322
Cdd:PRK05670 83 QAIGEAFGGkvvrakeimhgKTSPIE-----HDGSGIFAGLPNPFTVTRYHSLVVDRESLPDC---LEVTAwtDDGEIMG 154
|
170
....*....|....*.
gi 18105007 323 IVHNSLPFFSVQFHPE 338
Cdd:PRK05670 155 VRHKELPIYGVQFHPE 170
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
187-355 |
1.41e-12 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 68.35 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 187 YNQIRCLCQRGAEVtVVPWDHALDSQEYEGL-----FLSNGPGDPASYPSVVSTLSRVLSEpnpRPVFGICLGHQLLALA 261
Cdd:PRK06774 13 YNLYQYFCELGTEV-MVKRNDELQLTDIEQLapshlVISPGPCTPNEAGISLAVIRHFADK---LPILGVCLGHQALGQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 262 IGAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNE---GIVHNSLPFFS 332
Cdd:PRK06774 89 FGARVVRARQVMHGktsaicHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSERGGEMDeimGIRHRTLPLEG 168
|
170 180
....*....|....*....|...
gi 18105007 333 VQFHPEHQAGPSDMELLfDIFLE 355
Cdd:PRK06774 169 VQFHPESILSEQGHQLL-DNFLK 190
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
1464-1778 |
1.50e-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: 71.16 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1464 LPGLIDVHVHLREpgGTHKEDFASGTAAALAGGITMvcamPNTRPPIIDAP-ALALAQKLAEAGARCDF----ALFLGAS 1538
Cdd:cd01294 3 IPRPDDMHLHLRD--GAMLKLVLPYTARGFSRAIVM----PNLKPPVTTTAdALAYRERILAADPGPNFtplmTLYLTEN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1539 -SENAGTLGTVAGSAAGLKLYLN--ETFSELRLDSVVQWMEHFETWPSH-LPIVAHAEQQTVAAVLM---------VAQL 1605
Cdd:cd01294 77 tTPEELREAKKKGGIRGVKLYPAgaTTNSQGGVTDLEKIYPVLEAMQKLgMPLLVHGEVPDFKIDVLdreakfipvLEPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1606 TQR----SVHICHVARKEEILLIKAAKARglpVTCEVAPHHLFLSHDDLerLGPGKGEV---RPELGSRQDVEALwENMA 1678
Cdd:cd01294 157 AQRfpklKIVLEHITTADAVEYVKSCNEN---VAATITPHHLLLTRDDL--LGGGLNPHlycKPVAKRPEDREAL-RKAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1679 VIDC----FASDHAPHTLEEKcgsRPPPGFPGLET---MLPLLLTAVSEGRlSLDDLLQRLHHNPRRIFHLPPQEDTYVE 1751
Cdd:cd01294 231 TSGHpkffLGSDSAPHPKSNK---ESSCGCAGIFSapiALPYLAEVFEEHN-ALDKLEAFASDNGPNFYGLPPNKKTITL 306
|
330 340
....*....|....*....|....*..
gi 18105007 1752 VdlEHEWTIPSHMPFSKAHWTPFEGQK 1778
Cdd:cd01294 307 V--KEPWKVPEKIPFGNNGVVPFRAGE 331
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1327-1427 |
1.54e-12 |
|
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: 65.19 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1327 ELLPTVRLLESLGYSLYASLGTADFYTEHGVKV--TAVDWHFEEavdgecppQRSILEQLAEKNFELVINLSMRGAggrr 1404
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVvkTLHPKVHGG--------IPQILDLIKNGEIDLVINTLYPFE---- 68
|
90 100
....*....|....*....|...
gi 18105007 1405 lSSFVTKGYRTRRLAADFSVPLI 1427
Cdd:smart00851 69 -AQAHEDGYSIRRAAENIDIPGP 90
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
178-338 |
1.89e-12 |
|
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: 68.11 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 178 ILALDCGLKYNQI--RCLCQRGAEVTVVPWDHALD---SQEYEGLFLSNGPGdpasypsvvSTLSRVLSEPNPR------ 246
Cdd:TIGR00888 1 ILVLDFGSQYTQLiaRRLRELGVYSELVPNTTPLEeirEKNPKGIILSGGPS---------SVYAENAPRADEKifelgv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 247 PVFGICLGHQLLALAIG---AKTYKMRYGN---RGHNQPCLLVGSGRCFLTSQNHGFAVEtdSLPADWAPLFTNANdGSN 320
Cdd:TIGR00888 72 PVLGICYGMQLMAKQLGgevGRAEKREYGKaelEILDEDDLFRGLPDESTVWMSHGDKVK--ELPEGFKVLATSDN-CPV 148
|
170
....*....|....*...
gi 18105007 321 EGIVHNSLPFFSVQFHPE 338
Cdd:TIGR00888 149 AAMAHEEKPIYGVQFHPE 166
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
172-338 |
2.45e-12 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 72.26 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 172 TGGAPRILALDCGLKY-----NQIRclcQRGAEVTVVPWDHA---LDSQEYEGLFLSNGPGDPASY--PSVVST-LSRVL 240
Cdd:PRK13566 523 VGEGKRVLLVDHEDSFvhtlaNYFR---QTGAEVTTVRYGFAeemLDRVNPDLVVLSPGPGRPSDFdcKATIDAaLARNL 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 241 sepnprPVFGICLGHQLLALAIGAKTYKMRYGNRG------HNQPC-LLVGSGRCFLTSQNHGFAVETDSLPADwaplFT 313
Cdd:PRK13566 600 ------PIFGVCLGLQAIVEAFGGELGQLAYPMHGkpsrirVRGPGrLFSGLPEEFTVGRYHSLFADPETLPDE----LL 669
|
170 180
....*....|....*....|....*...
gi 18105007 314 N---ANDGSNEGIVHNSLPFFSVQFHPE 338
Cdd:PRK13566 670 VtaeTEDGVIMAIEHKTLPVAAVQFHPE 697
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
1059-1219 |
7.34e-12 |
|
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: 65.74 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1059 GISQPQWRELSDLESARQFCQTVGYPCVV---RPSYvlSGAAMNVAYTDGDLERFLSSAAAVskehPVVISKFIQEAKEI 1135
Cdd:pfam02222 4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEELGDG----PVIVEEFVPFDREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1136 DVDAVAS-DGVVAAIAISEHVEnagvHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQL-IAKDDQLKVI 1213
Cdd:pfam02222 78 SVLVVRSvDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELfVTEDGDLLIN 153
|
....*.
gi 18105007 1214 ECNVRV 1219
Cdd:pfam02222 154 ELAPRP 159
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
190-340 |
3.24e-11 |
|
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: 64.57 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 190 IRCLCQRGAEVTVVPW---DHALDSQEYEGLFLSNGPGDP--ASYPSVVST---LSRVLSEPnpRPVFGICLGHQLLALA 261
Cdd:cd01741 20 LREAGAETIEIDVVDVyagELLPDLDDYDGLVILGGPMSVdeDDYPWLKKLkelIRQALAAG--KPVLGICLGHQLLARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 262 IGAKTYKMRYG----------NRGHNQPCLLVGSGRCFLTSQNHGFAVEtdSLPADWAPLFTNAnDGSNEGIVHNSLpFF 331
Cdd:cd01741 98 LGGKVGRNPKGweigwfpvtlTEAGKADPLFAGLPDEFPVFHWHGDTVV--ELPPGAVLLASSE-ACPNQAFRYGDR-AL 173
|
....*....
gi 18105007 332 SVQFHPEHQ 340
Cdd:cd01741 174 GLQFHPEER 182
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
209-338 |
4.60e-11 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 63.99 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 209 LDSQE-YEGLFLSNGPGDPASYPSVVSTLSRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGR 287
Cdd:PRK06895 38 LDEVEnFSHILISPGPDVPRAYPQLFAMLERYHQH---KSILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSP 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18105007 288 CF--LTSQ-----NHGFAVETDSLPAdwaPLFTNANdgSNEGIV----HNSLPFFSVQFHPE 338
Cdd:PRK06895 115 LFdgLPEEfniglYHSWAVSEENFPT---PLEITAV--CDENVVmamqHKTLPIYGVQFHPE 171
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
187-338 |
5.73e-11 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 63.74 E-value: 5.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 187 YNQIRCLCQRGAEVTVVPWDHaLDSQEYEGL-----FLSNGPGDPASYPSVVSTLSRVLSEpnpRPVFGICLGHQLLALA 261
Cdd:PRK08857 13 YNLYQYFCELGAQVKVVRNDE-IDIDGIEALnpthlVISPGPCTPNEAGISLQAIEHFAGK---LPILGVCLGHQAIAQV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 262 IGAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWA-PLFTNANDGSNE---GIVHNSLPFF 331
Cdd:PRK08857 89 FGGQVVRARQVMHGktspirHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFElTAWTELEDGSMDeimGFQHKTLPIE 168
|
....*..
gi 18105007 332 SVQFHPE 338
Cdd:PRK08857 169 AVQFHPE 175
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
178-338 |
7.20e-11 |
|
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: 63.32 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 178 ILALDCGLKYNQ-----IRCLcqrGAEVTVVPWDHALDS---QEYEGLFLSNGPgdpasypsvvstlSRVLSEPNPR--- 246
Cdd:cd01742 1 ILILDFGSQYTHliarrVREL---GVYSEILPNTTPLEEiklKNPKGIILSGGP-------------SSVYEEDAPRvdp 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 247 -------PVFGICLGHQLLALAIGAKTYKMRYGNRGHNQpCLLVGSGRCF--LTSQ-----NHGFAVETdsLPADWAPLF 312
Cdd:cd01742 65 eifelgvPVLGICYGMQLIAKALGGKVERGDKREYGKAE-IEIDDSSPLFegLPDEqtvwmSHGDEVVK--LPEGFKVIA 141
|
170 180
....*....|....*....|....*.
gi 18105007 313 TNANDGsNEGIVHNSLPFFSVQFHPE 338
Cdd:cd01742 142 SSDNCP-VAAIANEEKKIYGVQFHPE 166
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
498-716 |
9.31e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 66.93 E-value: 9.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 498 GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP--SEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREEL- 574
Cdd:PRK08654 99 GIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELe 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 575 ------SALVAPAFAhTSQVLVDKSLKGWKEIEYEVVRDAYGNCvtvcnmenldplgIHTGES-----------IVVAPS 637
Cdd:PRK08654 179 daiestQSIAQSAFG-DSTVFIEKYLEKPRHIEIQILADKHGNV-------------IHLGDRecsiqrrhqklIEEAPS 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18105007 638 QTLNDREYQLLRQTAIKVTQHLGIVGECNVQYALnpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:PRK08654 245 PIMTPELRERMGEAAVKAAKAINYENAGTVEFLY--SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELS 321
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
987-1237 |
1.35e-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: 64.58 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 987 DRLYFDEISFEVVMDIYELENPEGVILsmgGQLPNNMAMA----LHRQQCRVLGtSPEAIDSAENRFKFSRLLDTIGISQ 1062
Cdd:COG0189 36 DDLTLDLGRAPELYRGEDLSEFDAVLP---RIDPPFYGLAllrqLEAAGVPVVN-DPEAIRRARDKLFTLQLLARAGIPV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1063 PQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEhPVVISKFIQEAKEIDVDAVAS 1142
Cdd:COG0189 112 PPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELGSE-PVLVQEFIPEEDGRDIRVLVV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1143 DG-VVAAIA-ISEHVENAG-VHSGDATLvtpPQDITAKTLERIKAIVHAVGqeLQVTGpfnLQLIAKDDQLKVIECNVRV 1219
Cdd:COG0189 191 GGePVAAIRrIPAEGEFRTnLARGGRAE---PVELTDEERELALRAAPALG--LDFAG---VDLIEDDDGPLVLEVNVTP 262
|
250
....*....|....*...
gi 18105007 1220 srSFPFVSKTLGVDLVAL 1237
Cdd:COG0189 263 --GFRGLERATGVDIAEA 278
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
498-716 |
2.14e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 65.55 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 498 GVRVLGTPVETIELTEDRrAFAARMA-EIGEHVAPSEAA--NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREEL 574
Cdd:PRK12833 102 GLIFVGPDAQTIRTMGDK-ARARRTArRAGVPTVPGSDGvvASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 575 SALV------APAFAHTSQVLVDKSLKGWKEIEYEVVRDayGNCVTVCnMENLDPLGIHTGESIVVAPSQTLNDREYQLL 648
Cdd:PRK12833 181 AAELplaqreAQAAFGDGGVYLERFIARARHIEVQILGD--GERVVHL-FERECSLQRRRQKILEEAPSPSLTPAQRDAL 257
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18105007 649 RQTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 716
Cdd:PRK12833 258 CASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLR 325
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
498-687 |
7.04e-10 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 64.77 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 498 GVRVLGTPVETIELTEDRraFAARMA--EIGEHVAPS--EAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREE 573
Cdd:PRK12999 103 GITFIGPTAEVLRLLGDK--VAARNAaiKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 574 LSALVAPA-------FAhTSQVLVDKSLKGWKEIEYEVVRDAYGNCVtvcnmenldplgiHTGE---SI------VV--A 635
Cdd:PRK12999 181 LEEAFERAkreakaaFG-NDEVYLEKYVENPRHIEVQILGDKHGNVV-------------HLYErdcSVqrrhqkVVeiA 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18105007 636 PSQTLNDREYQLLRQTAIKVTQHLGIVGECNVQYALNPESeQYYIIEVNARL 687
Cdd:PRK12999 247 PAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADG-NFYFIEVNPRI 297
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
1464-1794 |
9.55e-10 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 63.18 E-value: 9.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1464 LPGLIDVHVHLREPGGTHKeDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQK---------------LAEAGAR 1528
Cdd:PRK08417 29 LPALVDLNVSLKNDSLSSK-NLKSLENECLKGGVGSIVLYPDSTPAIDNEIALELINSaqrelpmqifpsiraLDEDGKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1529 CDFALFL--GA------SSENAGTLGTVAGSAAGLK--LYLNETFSELRlDSVVqwMEHFETWPS-HLP-IVAHAEQQTV 1596
Cdd:PRK08417 108 SNIATLLkkGAkalelsSDLDANLLKVIAQYAKMLDvpIFCRCEDSSFD-DSGV--MNDGELSFElGLPgIPSIAETKEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1597 AAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEVRPELGSRQDVEALWEN 1676
Cdd:PRK08417 185 AKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSACENFNT-AAKLNPPLRSKEDRLALLEA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1677 M--AVIDCFASDHAPHTLEEKCGS--RPPPGFPGLETMLPLLLT-AVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDT--- 1748
Cdd:PRK08417 264 LkeGKIDFLTSLHSAKSNSKKDLAfdEAAFGIDSICEYFSLCYTyLVKEGIITWSELSRFTSYNPAQFLGLNSGEIEvgk 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 18105007 1749 ---YVEVDLEHEWTIPSHMPfskahwtPFEGQKVKGTVRRVVLRGEVAY 1794
Cdd:PRK08417 344 eadLVLFDPNESTIIDDNFS-------LYSGDELYGKIEAVIIKGKLYL 385
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
247-338 |
1.50e-09 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 63.20 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 247 PVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSG------RCFLTSQNHGFAVETDSLPADWAPLfTNANDGSN 320
Cdd:PRK14607 75 PILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGlfrgipNPTVATRYHSLVVEEASLPECLEVT-AKSDDGEI 153
|
90
....*....|....*...
gi 18105007 321 EGIVHNSLPFFSVQFHPE 338
Cdd:PRK14607 154 MGIRHKEHPIFGVQFHPE 171
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
1314-1427 |
3.04e-09 |
|
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: 56.33 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1314 NILLTIgSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILEQLAEKNFELVI 1393
Cdd:cd01424 2 TVFISV-ADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEG--------RPNIVDLIKNGEIQLVI 72
|
90 100 110
....*....|....*....|....*....|....
gi 18105007 1394 NlsmrGAGGRRlssFVTKGYRTRRLAADFSVPLI 1427
Cdd:cd01424 73 N----TPSGKR---AIRDGFSIRRAALEYKVPYF 99
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
1446-1813 |
6.78e-09 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 60.63 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1446 APPLKVHVDCMT---SQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGITMvcampntrppIID-------- 1512
Cdd:PLN02942 36 APNLKVPDDVRVidaTGKFV-MPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTTM----------HIDfvipvngn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1513 -APALALAQKLAEAGArCDFALFLGAS------SENAGTLGTVAGSAAgLKLYLNETFSELRLDSVVqwMEHFETWPS-- 1583
Cdd:PLN02942 105 lLAGYEAYEKKAEKSC-MDYGFHMAITkwddtvSRDMETLVKEKGINS-FKFFMAYKGSLMVTDELL--LEGFKRCKSlg 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1584 HLPIVaHAEQ--------------------------------QTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARG 1631
Cdd:PLN02942 181 ALAMV-HAENgdavfegqkrmielgitgpeghalsrppllegEATARAIRLAKFVNTPLYVVHVMSIDAMEEIARARKSG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1632 LPVTCEVAPHHLFLshDDLERLGP-----GKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP---- 1700
Cdd:PLN02942 260 QRVIGEPVVSGLVL--DDSKLWDPdftiaSKYVMSPPIRPAGHGKALQAALSsgILQLVGTDHCPFNSTQKAFGKDdfrk 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1701 -PPGFPGLETMLPLLL-TAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVE--------VDLEHEWTIPSHMPFSKAH 1770
Cdd:PLN02942 338 iPNGVNGIEERMHLVWdTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAgsdadiiiLNPNSTFTISAKTHHSRID 417
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 18105007 1771 WTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWP 1813
Cdd:PLN02942 418 TNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPP 460
|
|
| PRK07200 |
PRK07200 |
aspartate/ornithine carbamoyltransferase family protein; Validated |
1933-2143 |
8.42e-09 |
|
aspartate/ornithine carbamoyltransferase family protein; Validated
Pssm-ID: 235961 [Multi-domain] Cd Length: 395 Bit Score: 60.14 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1933 TKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQ 2012
Cdd:PRK07200 30 TPDELKAVLDVADALRALREENISTKVFNSGLGISVFRDNSTRTRFSYASACNLLGLEVQDLDEGKSQIAHGETVRETAN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 2013 TMSCYADVVVLR------------HPQPGAVELAAKHC---RRP-VINAGDGVgEHPTQALLDIFTIREELGTVN---GM 2073
Cdd:PRK07200 110 MISFMADVIGIRddmyigkgnaymREVGAAVDDGYKQGvlpQRPtLVNLQCDI-DHPTQSMADLLHLIEHFGGLEnlkGK 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18105007 2074 TITMVGDL--KHGRTV---HSLACLLTQYRVSLRYVAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLY 2143
Cdd:PRK07200 189 KIAMTWAYspSYGKPLsvpQGIIGLMTRFGMDVTLAHPEGYDLMPEVvevaKKNAKASGGSFRQVNSMEEAFKDADIVY 267
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
187-362 |
1.30e-08 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 57.12 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 187 YNQIRCLCQRGAEVtVVPWDHALDSQEYEGL---FLSNGPGdPASYPSVVSTLSRVLSEPNPRPVFGICLGHQLLALAIG 263
Cdd:PRK07649 13 FNLVQFLGELGQEL-VVKRNDEVTISDIENMkpdFLMISPG-PCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 264 A---KTYKMRYGNRG---HNQPCLLVGSGRCFLTSQNHGFAVETDSLPaDWAPLFTNANDGSNEGIVHNSLPFFSVQFHP 337
Cdd:PRK07649 91 GevvRAERLMHGKTSlmhHDGKTIFSDIPNPFTATRYHSLIVKKETLP-DCLEVTSWTEEGEIMAIRHKTLPIEGVQFHP 169
|
170 180
....*....|....*....|....*
gi 18105007 338 EHQAGPSDMELLFDiFLETVKEATA 362
Cdd:PRK07649 170 ESIMTSHGKELLQN-FIRKYSPSVT 193
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
498-712 |
1.49e-08 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 59.83 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 498 GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAAN--SLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREEL 574
Cdd:PRK08463 98 GIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPgTEKLNseSMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 575 SALV------APAFAHTSQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCnmENLDPLGIHTGESIVVAPSQTLNDREYQLL 648
Cdd:PRK08463 178 ENAFesckreALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLC--ERDCSIQRRHQKVIEIAPCPSISDNLRKTM 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18105007 649 RQTAIKVTQHLGIVGECNVQYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALG 712
Cdd:PRK08463 256 GVTAVAAAKAVGYTNAGTIEFLLD-DYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
247-338 |
2.16e-08 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 56.01 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 247 PVFGICLGHQLLALAIGAKTYKMRYGNRG--------HNQPclLVGSGRCFLTSQNHgfAVETDSLPADWAPLFTNANDG 318
Cdd:PRK00758 69 PILGICLGHQLIAKAFGGEVGRGEYGEYAlveveildEDDI--LKGLPPEIRVWASH--ADEVKELPDGFEILARSDICE 144
|
90 100
....*....|....*....|
gi 18105007 319 sNEGIVHNSLPFFSVQFHPE 338
Cdd:PRK00758 145 -VEAMKHKEKPIYGVQFHPE 163
|
|
| 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 18105007 502 LGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREEL----- 574
Cdd:PRK05586 103 IGPDSETIELMGNKSNAREIMIKAGVPVVPgSEGEiENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELikafn 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 575 --SALVAPAFAHTSqVLVDKSLKGWKEIEYEVVRDAYGNCVTV----CNMENldplgiHTGESIVVAPSQTLNDREYQLL 648
Cdd:PRK05586 183 taKSEAKAAFGDDS-MYIEKFIENPKHIEFQILGDNYGNVVHLgerdCSLQR------RNQKVLEEAPSPVMTEELRKKM 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18105007 649 RQTAIKVTQHLGIVGECNVQYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPL 715
Cdd:PRK05586 256 GEIAVKAAKAVNYKNAGTIEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
498-686 |
8.64e-08 |
|
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: 57.78 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 498 GVRVLGTPVETIELTEDRRAfAARMA-EIGEHVAPS--EAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREEL 574
Cdd:COG1038 102 GITFIGPSPEVLEMLGDKVA-ARAAAiEAGVPVIPGteGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEEL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 575 SALVAPAF--AHTS----QVLVDKSLKGWKEIEYEVVRDAYGNCVtvcnmenldplgiHTGE---SI------VV--APS 637
Cdd:COG1038 181 EEAFESARreAKAAfgddEVFLEKYIERPKHIEVQILGDKHGNIV-------------HLFErdcSVqrrhqkVVeiAPA 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18105007 638 QTLNDREYQLLRQTAIKVTQHLGIVGECNVQYaLNPESEQYYIIEVNAR 686
Cdd:COG1038 248 PNLDEELREAICEAAVKLAKAVGYVNAGTVEF-LVDDDGNFYFIEVNPR 295
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
1464-1792 |
9.32e-08 |
|
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: 56.36 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1464 LPGLIDVHVHLR--------EPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDApalalaqkLAEAGARCDFALFL 1535
Cdd:pfam01979 3 LPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEA--------LLEAAEELPLGLRF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1536 GASSENAGTLGTVAGSAA-GLKLYLNETFSELRLDSVVQ-WMEHFETWpshlpivaHAEQQTVAAVLMVAQLTQRSVHIc 1613
Cdd:pfam01979 75 LGPGCSLDTDGELEGRKAlREKLKAGAEFIKGMADGVVFvGLAPHGAP--------TFSDDELKAALEEAKKYGLPVAI- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1614 HVAR-KEEILLIKAAKARG---------------LPVTCEVAPHHLFLSHDDLERLGPGKGEVR------PELGSRQDVE 1671
Cdd:pfam01979 146 HALEtKGEVEDAIAAFGGGiehgthlevaesgglLDIIKLILAHGVHLSPTEANLLAEHLKGAGvahcpfSNSKLRSGRI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1672 ALWE--NMAVIDCFASDHAPHTleekcgsRPPPGFPGLETMlpLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTy 1749
Cdd:pfam01979 226 ALRKalEDGVKVGLGTDGAGSG-------NSLNMLEELRLA--LELQFDPEGGLSPLEALRMATINPAKALGLDDKVGS- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 18105007 1750 VEV----DLehewtipshMPFSKAHWTPFEGQKVKGTVRRVVLRGEV 1792
Cdd:pfam01979 296 IEVgkdaDL---------VVVDLDPLAAFFGLKPDGNVKKVIVKGKI 333
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
187-338 |
1.27e-07 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 53.97 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 187 YNQIRCLCQRGAEVTVVPWDH----ALDSQEYEGLFLSNGPGDPASypsvvSTLSR-VLSEPNPR-PVFGICLGHQLLAL 260
Cdd:CHL00101 13 YNLVQSLGELNSDVLVCRNDEidlsKIKNLNIRHIIISPGPGHPRD-----SGISLdVISSYAPYiPILGVCLGHQSIGY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 261 AIGAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVETDSLPadwAPLFTNA--NDGSNEGIVHNSLPF-F 331
Cdd:CHL00101 88 LFGGKIIKAPKPMHGktskiyHNHDDLFQGLPNPFTATRYHSLIIDPLNLP---SPLEITAwtEDGLIMACRHKKYKMlR 164
|
....*..
gi 18105007 332 SVQFHPE 338
Cdd:CHL00101 165 GIQFHPE 171
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
507-687 |
2.04e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 55.96 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 507 ETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREELsalvAPAFAH 584
Cdd:PRK08591 108 ETIRLMGDKVTAKATMKKAGVPVVPgSDGPvDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAEL----EKAFSM 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 585 TSQ----------VLVDKSLKGWKEIEYEVVRDAYGNcvtvcnmenldplGIHTGE---SI------VV--APSQTLNDR 643
Cdd:PRK08591 184 ARAeakaafgnpgVYMEKYLENPRHIEIQVLADGHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEE 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18105007 644 EYQLLRQTAIKVTQHLGIVGECNVQYaLNPESEQYYIIEVNARL 687
Cdd:PRK08591 251 LRRKIGEAAVKAAKAIGYRGAGTIEF-LYEKNGEFYFIEMNTRI 293
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
216-338 |
2.82e-07 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 53.65 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 216 GLFLSNGPGDPASypSVVStLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYG-NRGHNQPC---------LLVGS 285
Cdd:PLN02335 65 GVLISPGPGTPQD--SGIS-LQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVhydekgeegLFSGL 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 18105007 286 GRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFS-VQFHPE 338
Cdd:PLN02335 142 PNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPE 195
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
536-684 |
3.48e-07 |
|
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: 53.09 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 536 NSLEQAQAAAERLGYPVLVRAAfalgGLGSGF----ASNREELSALVAPAFAHTSQVLVDKSLKGwKEIEyevvrdaygn 611
Cdd:pfam07478 23 NPKEWCAQVEEALGYPVFVKPA----RLGSSVgvskVESREELQAAIEEAFQYDEKVLVEEGIEG-REIE---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 612 cVTVCNMENLDPLGIH------------------TGESIVVAPsqtLNDREYQLLRQTAIKVTQHLGIVGECNVQYALnP 673
Cdd:pfam07478 88 -CAVLGNEDPEVSPVGeivpsggfydyeakyiddSAQIVVPAD---LEEEQEEQIQELALKAYKALGCRGLARVDFFL-T 162
|
170
....*....|.
gi 18105007 674 ESEQYYIIEVN 684
Cdd:pfam07478 163 EDGEIVLNEVN 173
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
190-263 |
4.22e-07 |
|
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: 50.67 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 190 IRCLCQRGAEVTVVPWDH-----ALDSQEYEGLFLSNGPGDP---ASYPSVVSTLSRVLSepNPRPVFGICLGHQLLALA 261
Cdd:cd01653 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPddlARDEALLALLREAAA--AGKPILGICLGAQLLVLG 95
|
..
gi 18105007 262 IG 263
Cdd:cd01653 96 VQ 97
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
247-353 |
7.83e-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: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 247 PVFGICLGHQLLALAIGAKTYkmrygnrghnqPCLLVGSgrcfltsqNHGFAVetDSLPADWAPLFTnANDGSNEGIVHN 326
Cdd:cd01745 102 PILGICRGMQLLNVALGGTLY-----------QDIRVNS--------LHHQAI--KRLADGLRVEAR-APDGVIEAIESP 159
|
90 100
....*....|....*....|....*....
gi 18105007 327 SLPF-FSVQFHPE-HQAGPSDMELLFDIF 353
Cdd:cd01745 160 DRPFvLGVQWHPEwLADTDPDSLKLFEAF 188
|
|
| PRK06849 |
PRK06849 |
hypothetical protein; Provisional |
1032-1219 |
2.62e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235876 [Multi-domain] Cd Length: 389 Bit Score: 51.97 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1032 CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQF-CQTVGYPCVVRPSYVLSGAAMNVAYTdgdlERF 1110
Cdd:PRK06849 101 CEVLHFDFELLLLLHNKWEFAEQARSLGLSVPKTYLITDPEAIRNFmFKTPHTPYVLKPIYSRFVRRVDLLPK----EAA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1111 LSSaAAVSKEHPVVISKFIQeAKEIDVDAVASDGVVAAIA--ISEHVENAGVHSGDATLVTPpqditaktleRIKAIVHA 1188
Cdd:PRK06849 177 LKE-LPISKDNPWVMQEFIQ-GKEYCSYSIVRSGELRAHScyKPEYCAGSGAQIAFQPINHP----------RIEEFVTH 244
|
170 180 190
....*....|....*....|....*....|..
gi 18105007 1189 VGQELQVTGPFNLQLI-AKDDQLKVIECNVRV 1219
Cdd:PRK06849 245 FVKELNYTGQISFDFIeTENGDAYPIECNPRT 276
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
190-258 |
3.29e-06 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 47.20 E-value: 3.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18105007 190 IRCLCQRGAEVTVVPWDH-----ALDSQEYEGLFLSNGPGDP---ASYPSVVSTLSRVLSepNPRPVFGICLGHQLL 258
Cdd:cd03128 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPddlAWDEALLALLREAAA--AGKPVLGICLGAQLL 92
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
395-718 |
3.67e-06 |
|
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: 51.26 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 395 KVLILgSGGLSigqaGEFD---YSGSQAIKALKEENIQtllinpniatvqtsqgladkVYFLPITPHYVTQVIRNERPDG 471
Cdd:COG1181 2 RVAVL-FGGRS----AEREvslKSGRAVAAALDKAGYD--------------------VVPIGIDVEDLPAALKELKPDV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 472 VLLtfggqtALNC--GVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANS--LEQAQAAAER 547
Cdd:COG1181 57 VFP------ALHGrgGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRgeLADLEAIEEE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 548 LGYPVLVRAAFAlgglGSGF----ASNREELSALVAPAFAHTSQVLVDKSLKGwKEIEyevvrdaygncVTVCNMENLDP 623
Cdd:COG1181 131 LGLPLFVKPARE----GSSVgvskVKNAEELAAALEEAFKYDDKVLVEEFIDG-REVT-----------VGVLGNGGPRA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 624 LGI----------------HTGESIVVAPSQtLNDREYQLLRQTAIKVTQHLGIVGecnvqYA-----LNPEsEQYYIIE 682
Cdd:COG1181 195 LPPieivpengfydyeakyTDGGTEYICPAR-LPEELEERIQELALKAFRALGCRG-----YArvdfrLDED-GEPYLLE 267
|
330 340 350
....*....|....*....|....*....|....*...
gi 18105007 683 VNAR--LSRSSalaskatGYPLAYVAAklalGIPLPEL 718
Cdd:COG1181 268 VNTLpgMTPTS-------LLPKAAAAA----GISYEEL 294
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
247-338 |
1.39e-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: 48.41 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 247 PVFGICLGHQLLALAIGAKTY---KMRYGNRGHNQPC----------LLVGSGRCF--LTSQN-------HGFAVetDSL 304
Cdd:pfam07722 107 PILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapshaVNVEPGSLLasLLGSEefrvnslHHQAI--DRL 184
|
90 100 110
....*....|....*....|....*....|....*.
gi 18105007 305 PADWAPLFTnANDGSNEGIVHNSLPFF--SVQFHPE 338
Cdd:pfam07722 185 APGLRVEAV-APDGTIEAIESPNAKGFalGVQWHPE 219
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
187-338 |
1.41e-05 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 47.99 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 187 YNQIRCLCQRGAEVTVVPWDH----ALDSQEYEGLFLSNGPGDPASypSVVStLSRVLSEPNPRPVFGICLGHQLLALAI 262
Cdd:PRK08007 13 WNLYQYFCELGADVLVKRNDAltlaDIDALKPQKIVISPGPCTPDE--AGIS-LDVIRHYAGRLPILGVCLGHQAMAQAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 263 GA---KTYKMRYGNRG---HNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAplfTNANDGSNE--GIVHNSLPFFSVQ 334
Cdd:PRK08007 90 GGkvvRAAKVMHGKTSpitHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLEGVQ 166
|
....
gi 18105007 335 FHPE 338
Cdd:PRK08007 167 FHPE 170
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
177-338 |
3.00e-05 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 48.89 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 177 RILALDCGLKYNQ-----IRCL---CQrgaevtVVPWDHALDS-QEYE--GLFLSNGPgdpASypsvvstlsrVLSEPNP 245
Cdd:PRK00074 5 KILILDFGSQYTQliarrVRELgvySE------IVPYDISAEEiRAFNpkGIILSGGP---AS----------VYEEGAP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 246 R----------PVFGICLGHQLLALAIGAK---TYKMRYGN---RGHNQPCLLVGSGRCFLTSQNHGFAVETdsLPADWA 309
Cdd:PRK00074 66 RadpeifelgvPVLGICYGMQLMAHQLGGKverAGKREYGRaelEVDNDSPLFKGLPEEQDVWMSHGDKVTE--LPEGFK 143
|
170 180
....*....|....*....|....*....
gi 18105007 310 PLFTNANdGSNEGIVHNSLPFFSVQFHPE 338
Cdd:PRK00074 144 VIASTEN-CPIAAIANEERKFYGVQFHPE 171
|
|
| GATase1_Glutamyl_Hydrolase |
cd01747 |
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ... |
247-341 |
3.52e-05 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153218 [Multi-domain] Cd Length: 273 Bit Score: 47.70 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 247 PVFGICLGHQLLAL----------AIGAKTYKMRYGNRGHNQPCLLVGS----------GRCFlTSQNHGFAVETDSLP- 305
Cdd:cd01747 94 PVWGTCLGFELLTYltsgetllleATEATNSALPLNFTEDALQSRLFKRfppdllkslaTEPL-TMNNHRYGISPENFTe 172
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 18105007 306 ----ADWAP-LFTNANDGSNEGIV---HNSLPFFSVQFHPEHQA 341
Cdd:cd01747 173 ngllSDFFNvLTTNDDWNGVEFIStveAYKYPIYGVQWHPEKNA 216
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
1053-1185 |
4.27e-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: 47.79 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1053 RLLDTIGISQPQWRELS--DLESARQFCQTVGYPCVVRPsyVLSGAA--MNVAYTDGDLERFLSSAAAVSkeHPVVISKF 1128
Cdd:COG1181 101 RVLAAAGLPTPPYVVLRrgELADLEAIEEELGLPLFVKP--AREGSSvgVSKVKNAEELAAALEEAFKYD--DKVLVEEF 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18105007 1129 IqEAKEIDVdAVASDGVVAAIAISEHVENAGV-------HSGDATLVTPPqDITAKTLERIKAI 1185
Cdd:COG1181 177 I-DGREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPA-RLPEELEERIQEL 237
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
1054-1242 |
8.02e-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: 45.77 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1054 LLDTIGISQPQW-------RELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLssAAAVSKEHPVVIS 1126
Cdd:pfam07478 1 LLKAAGLPVVPFvtftradWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAI--EEAFQYDEKVLVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1127 KFIqEAKEIDVdAVASDGVVAAIAISEHVENAGV------HSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTG--- 1197
Cdd:pfam07478 79 EGI-EGREIEC-AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGlar 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18105007 1198 -PFNLQliaKDDQLKVIECN-----VRVSRsFPFVSKTLGVDLVALATRVI 1242
Cdd:pfam07478 157 vDFFLT---EDGEIVLNEVNtipgfTSISM-FPKLAAAAGVSFPDLVDQLI 203
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
522-601 |
1.24e-04 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 46.65 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 522 MAEIGEHVAPSEAANSLEQA----QAAAERLGYPVLVRAAfalgGLGSGF----ASNREELSALVAPAFAHTSQVLVDKS 593
Cdd:PRK01966 131 LAAAGIPVAPYVVLTRGDWEeaslAEIEAKLGLPVFVKPA----NLGSSVgiskVKNEEELAAALDLAFEYDRKVLVEQG 206
|
....*...
gi 18105007 594 LKGwKEIE 601
Cdd:PRK01966 207 IKG-REIE 213
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
529-684 |
1.39e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 46.26 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 529 VAPSEAANSLEQAQAAAERLGYPVLVRAafALGG--LGSGFASNREELSALVAPAFAHTSQVLVDKSLKGwkeIEYevvr 606
Cdd:PRK01372 113 TPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGssVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKG---REL---- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 607 daygncvTVCNMEN--LDPLGI-------------HTGESIVVAPSQtLNDREYQLLRQTAIKVTQHLGIVGECNVQYAL 671
Cdd:PRK01372 184 -------TVAVLGGkaLPVIEIvpagefydyeakyLAGGTQYICPAG-LPAEIEAELQELALKAYRALGCRGWGRVDFML 255
|
170
....*....|...
gi 18105007 672 NpESEQYYIIEVN 684
Cdd:PRK01372 256 D-EDGKPYLLEVN 267
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
1079-1143 |
4.88e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 44.82 E-value: 4.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18105007 1079 QTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVskEHPVVISKFIqEAKEIDVDAVASD 1143
Cdd:PRK14570 168 EVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKY--DLTVVIEKFI-EAREIECSVIGNE 229
|
|
| 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 18105007 1035 LGTSPEAIDSAENRFKFSRLLDTIGISQPQWRE--LSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLS 1112
Cdd:PRK08654 103 IGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEegIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIE 182
|
90 100 110
....*....|....*....|....*....|...
gi 18105007 1113 S----AAAVSKEHPVVISKFIQEAKEIDVDAVA 1141
Cdd:PRK08654 183 StqsiAQSAFGDSTVFIEKYLEKPRHIEIQILA 215
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
507-663 |
9.93e-04 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 43.91 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 507 ETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFalGGL-GSG--FASNREELSALVApAFA 583
Cdd:COG0026 82 EALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRR--GGYdGKGqvVIKSAADLEAAWA-ALG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 584 HTSQVL---VDkslkgwkeIEYE----VVRDAYGNCVT--VCnmENldplgIHTG----ESIVVAP-SQTLNDReyqlLR 649
Cdd:COG0026 159 GGPCILeefVP--------FERElsviVARSPDGEVATypVV--EN-----VHRNgildESIAPARiSEALAAE----AE 219
|
170
....*....|....
gi 18105007 650 QTAIKVTQHLGIVG 663
Cdd:COG0026 220 EIAKRIAEALDYVG 233
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
1036-1275 |
1.16e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 44.07 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1036 GTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPsyVLSGAAMNVAYTDGDLERFLSSAA 1115
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKP--RMGSGSVGVRLCASVAEAAAHCAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1116 AVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISE-------HVENAGvHSGDATLVTPPQDITAKTLERikaIVHA 1188
Cdd:PRK02186 174 LRRAGTRAALVQAYVEGDEYSVETLTVARGHQVLGITRkhlgpppHFVEIG-HDFPAPLSAPQRERIVRTVLR---ALDA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1189 VGQELqvtGPFNLQLIAKDDQLKVIECNVRVSRSF-P-FVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVGVKVPQF 1266
Cdd:PRK02186 250 VGYAF---GPAHTELRVRGDTVVIIEINPRLAGGMiPvLLEEAFGVDLLDHVIDLHLGVAAFADPTAKRYGAIRFVLPAR 326
|
....*....
gi 18105007 1267 SfSRLAGAD 1275
Cdd:PRK02186 327 S-GVLRGLL 334
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
1038-1212 |
1.43e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 43.22 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1038 SPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVV---RPSY------VLSGAAmnvaytdgDLE 1108
Cdd:PRK06019 91 GPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLktrRGGYdgkgqwVIRSAE--------DLE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1109 RFLSSAAAVskehPVVISKFIQEAKEIDVDAVAS-DGVVAAIAIsehVENagVHSG---DATLVtpPQDITAKTLERIKA 1184
Cdd:PRK06019 163 AAWALLGSV----PCILEEFVPFEREVSVIVARGrDGEVVFYPL---VEN--VHRNgilRTSIA--PARISAELQAQAEE 231
|
170 180
....*....|....*....|....*....
gi 18105007 1185 IVHAVGQELQVTGPFNLQL-IAKDDQLKV 1212
Cdd:PRK06019 232 IASRIAEELDYVGVLAVEFfVTGDGELLV 260
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
507-663 |
2.34e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 42.83 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 507 ETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFaLG--GLGSGFASNREELSALVApAFAH 584
Cdd:PRK06019 93 DALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTRR-GGydGKGQWVIRSAEDLEAAWA-LLGS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 585 TSQVlvdksLKGWKEIEYE----VVRDAYGNCVT---VcnmENLDPLGI-HTgesiVVAPSQtLNDREYQLLRQTAIKVT 656
Cdd:PRK06019 171 VPCI-----LEEFVPFEREvsviVARGRDGEVVFyplV---ENVHRNGIlRT----SIAPAR-ISAELQAQAEEIASRIA 237
|
....*..
gi 18105007 657 QHLGIVG 663
Cdd:PRK06019 238 EELDYVG 244
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1068-1249 |
5.20e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 41.65 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1068 LSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLER-FL---SSAAAVSKEHPVVISKFIQEAKEIDVDAVAsD 1143
Cdd:PRK08462 140 LKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENlYLaaeSEALSAFGDGTMYMEKFINNPRHIEVQILG-D 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1144 GVVAAIAISEhvENAGVHSGDATLV--TPPQDITAKTLER-----IKAiVHAVGQELQVTGPFnlqLIAKDDQLKVIECN 1216
Cdd:PRK08462 219 KHGNVIHVGE--RDCSLQRRHQKLIeeSPAVVLDEKTRERlhetaIKA-AKAIGYEGAGTFEF---LLDSNLDFYFMEMN 292
|
170 180 190
....*....|....*....|....*....|...
gi 18105007 1217 VRVSRSFPFVSKTLGVDLVALATRVIMGEEVEP 1249
Cdd:PRK08462 293 TRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPS 325
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1443-1631 |
7.12e-03 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 41.10 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1443 IGPAPPLKV-----HVDCmtSQKLVrLPGLIDVHVHLREPGGTHKEDFASGT---------------AAALAGGITMVCA 1502
Cdd:COG1228 41 VGPAADLAVpagaeVIDA--TGKTV-LPGLIDAHTHLGLGGGRAVEFEAGGGitptvdlvnpadkrlRRALAAGVTTVRD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105007 1503 MPNTRPPIIDAPA------LALAQKLAEAGArcdFALFLGASSENAGTLG-----TVAGSAAGLKLYLNETFSELRLDSV 1571
Cdd:COG1228 118 LPGGPLGLRDAIIagesklLPGPRVLAAGPA---LSLTGGAHARGPEEARaalreLLAEGADYIKVFAEGGAPDFSLEEL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18105007 1572 VQWMEhfETWPSHLPIVAHAEQQtvAAVLMVAQLTQRSV-HICHVArkEEIllIKAAKARG 1631
Cdd:COG1228 195 RAILE--AAHALGLPVAAHAHQA--DDIRLAVEAGVDSIeHGTYLD--DEV--ADLLAEAG 247
|
|
| |
