|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
419-1477 |
0e+00 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 1538.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 419 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEvglKQADAVYFLPITPQFVTEVIKA 498
Cdd:TIGR01369 3 RTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDP---EMADKVYIEPLTPEAVEKIIEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 499 ERPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESMEDALKAAD 578
Cdd:TIGR01369 80 ERPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 579 TIGYPVMIRSAYALGGLGSGICPNKETLMDLGTKAFAMT--NQILVERSVTGWKEIEYEVVRDADDNCVTVCNMENVDAM 656
Cdd:TIGR01369 160 EIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 657 GVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAF 736
Cdd:TIGR01369 240 GVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 737 IAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMC 816
Cdd:TIGR01369 320 VAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 817 HPSVDGFtpRLPMNKEWPaNLDLRKELSEPSSTRIYAIAKALENNMSLDEIVKLTSIDKWFLYKMRDILNMDKTLKGLNS 896
Cdd:TIGR01369 400 EIGATGF--DLPDREVEP-DEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 897 ESVTEETLRQAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDIKF-DEHG 975
Cdd:TIGR01369 477 TDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 976 IMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACNGCIIS 1055
Cdd:TIGR01369 557 VLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1056 VGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFANSVGYPCLLRPSYVLS 1135
Cdd:TIGR01369 637 FGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLG 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1136 GSAMNVVFSEDEMKRFLEEATRVSQEHPVVLTKFIEGAREVEMDAVGKEGRVISHAISEHVEDAGVHSGDATLMLPTQTI 1215
Cdd:TIGR01369 717 GRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTL 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1216 SQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGESVDEkhLPT 1295
Cdd:TIGR01369 797 SAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEE--LGV 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1296 LEQPiiPSDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQSFRPRF 1374
Cdd:TIGR01369 875 GKEK--EPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGsVLLSVRDKDKEEL 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1375 LGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRR 1454
Cdd:TIGR01369 953 LDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPN-----ILDLIKNGEIELVINTTSKGAGTATDGYKIRR 1027
|
1050 1060
....*....|....*....|...
gi 8393186 1455 TAVDSGIALLTNFQVTKLFAEAV 1477
Cdd:TIGR01369 1028 EALDYGVPLITTLNTAEAFAEAL 1050
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
419-1491 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1434.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 419 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTN-EVglkqADAVYFLPITPQFVTEVIK 497
Cdd:PRK05294 4 RTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDpEM----ADATYIEPITPEFVEKIIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 498 AERPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESMEDALKAA 577
Cdd:PRK05294 80 KERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 578 DTIGYPVMIRSAYALGGLGSGICPNKETLMDLGTKAFAM--TNQILVERSVTGWKEIEYEVVRDADDNCVTVCNMENVDA 655
Cdd:PRK05294 160 EEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 656 MGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIV-GECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPL 734
Cdd:PRK05294 240 MGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 735 AFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALR 814
Cdd:PRK05294 320 AKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 815 MCHPSVDGFTPRL--PMNKEwpanlDLRKELSEPSSTRIYAIAKALENNMSLDEIVKLTSIDKWFLYKMRDILNMDKTLK 892
Cdd:PRK05294 400 SLEIGVTGLDEDLfeEESLE-----ELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 893 GlNSESVTEETLRQAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDIKFD 972
Cdd:PRK05294 475 E-NGLPLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 973 EHGIMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACNGC 1052
Cdd:PRK05294 554 RKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGV 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1053 IISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFANSVGYPCLLRPSY 1132
Cdd:PRK05294 634 IVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSY 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1133 VLSGSAMNVVFSEDEMKRFLEEATRVSQEHPVVLTKFIEGAREVEMDAV--GKEgrVISHAISEHVEDAGVHSGDATLML 1210
Cdd:PRK05294 714 VLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAIcdGED--VLIGGIMEHIEEAGVHSGDSACSL 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1211 PTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGESVDE 1290
Cdd:PRK05294 792 PPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAE 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1291 KHlptLEQPIIPsDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQS 1369
Cdd:PRK05294 872 LG---YTKGLIP-PYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGtVFLSVRDR 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1370 FRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKfVHDN 1449
Cdd:PRK05294 948 DKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPH-----IVDLIKNGEIDLVINTPTGRQA-IRDG 1021
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....
gi 8393186 1450 YVIRRTAVDSGIALLTNFQVTKLFAEAVQKART--VDSKSLFHY 1491
Cdd:PRK05294 1022 FSIRRAALEYKVPYITTLAGARAAVKAIEALKFgeLEVRSLQEY 1065
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
428-980 |
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: 618.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 428 LGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQT-NEVglkqADAVYFLPITPQFVTEVIKAERPDGLIL 506
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTdYDT----ADRLYFEPLTVEDVLDIIEKEKPDGVIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 507 GMGGQTALNCGVELFKRGVLKeyGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESMEDALKAADTIGYPVMI 586
Cdd:COG0458 77 QFGGQTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 587 RSAYALGGLGSGICPNKETLMDLGTKAFA--MTNQILVERSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHTGDSV 664
Cdd:COG0458 155 RPSYVLGGRGMGIVYNEEELEEYLERALKvsPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 665 VVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHptSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALG 744
Cdd:COG0458 235 CVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 745 IPLPEIKNvvsgKTSacFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSVDG-- 822
Cdd:COG0458 313 YTLDELGN----DTG--FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtv 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 823 FTPRLpMNKEWPANLDLRKELSepsstRIYAIAKALENNMSLDEIVKLTSIDKWFLYKMRDILNMDKTLKGlnsESVTEE 902
Cdd:COG0458 387 LLSLV-ADDDKEEALLLARRLA-----RLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEE---IILVIN 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393186 903 TLRQAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDIKFDEHGIMVLG 980
Cdd:COG0458 458 TLLGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIG 535
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
46-400 |
3.36e-172 |
|
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: 519.49 E-value: 3.36e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 46 AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGAPDTTardelglnkyMESDG 125
Cdd:TIGR01368 1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDED----------AESKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 126 IKVAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQSVDF------VDPNKQ- 198
Cdd:TIGR01368 71 IHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEElvekarVSPDITg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 199 -NLIAEVSTKDVKVFGK--GNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTQ---MDYDGLLIAGGPGNPALAQ 272
Cdd:TIGR01368 151 iNLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEikkYNPDGIFLSNGPGDPAAVE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 273 PLIQNVKKILEsdrKEPLFGISTGNIITGLAAGAKSYKMSMANRGQNQPVLNITNRQAFITAQNHGYALDN-TLPAG-WK 350
Cdd:TIGR01368 231 PAIETIRKLLE---KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPdSLPAGdLE 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 8393186 351 PLFVNVNDQTNEGIMHESKPFFAVQFHPEVSPGPTDTEYLFDSFFSLIKK 400
Cdd:TIGR01368 308 VTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
44-398 |
2.45e-143 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 442.98 E-value: 2.45e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 44 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGAPDttaRDelglnkyMES 123
Cdd:PRK12564 3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNR---ED-------FES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 124 DGIKVAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQSVD--------FVDP 195
Cdd:PRK12564 73 DRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEellekaraFPGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 196 NKQNLIAEVSTKDVKVFGKGNPT---KVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTQMDYDGLLIAGGPGNPA 269
Cdd:PRK12564 153 LGLDLVKEVSTKEPYPWPGPGGElkyKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 270 LAQPLIQNVKKILESDRkePLFGISTGNIITGLAAGAKSYKMSMANRGQNQPVLNITNRQAFITAQNHGYALD-NTLPAG 348
Cdd:PRK12564 233 ALDYAIEMIRELLEKKI--PIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDeDSLPAN 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 8393186 349 WKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVSPGPTDTEYLFDSFFSLI 398
Cdd:PRK12564 311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
44-399 |
2.83e-137 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 426.74 E-value: 2.83e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 44 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGAPDttardelglnKYMES 123
Cdd:COG0505 3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVND----------EDFES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 124 DGIKVAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQSVD--------FVDP 195
Cdd:COG0505 73 DRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEellekaraAPGM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 196 NKQNLIAEVSTKDVKVFG--KGNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTQ---MDYDGLLIAGGPGNPAL 270
Cdd:COG0505 153 EGLDLVKEVSTKEPYEWTeaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEilaLNPDGVFLSNGPGDPAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 271 AQPLIQNVKKILESDRkePLFGISTGNIITGLAAGAKSYKMSMANRGQNQPVLNITNRQAFITAQNHGYALD-NTLPA-G 348
Cdd:COG0505 233 LDYAIETIRELLGKGI--PIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDeDSLPAtD 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 8393186 349 WKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVSPGPTDTEYLFDSFFSLIK 399
Cdd:COG0505 311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
546-748 |
1.52e-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: 328.49 E-value: 1.52e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 546 DRQLFSDKLNEINEKIAPSFA--VESMEDALKAADTIGYPVMIRSAYALGGLGSGICPNKETLMDLGTKAFAMT------ 617
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 618 NQILVERSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMgvHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGEC 697
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 8393186 698 NIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLP 748
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
220-395 |
5.63e-96 |
|
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: 305.96 E-value: 5.63e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 220 VVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDF---TQMDYDGLLIAGGPGNPALAQPLIQNVKKILESdrKEPLFGISTG 296
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAeeiLKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGK--KIPIFGICLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 297 NIITGLAAGAKSYKMSMANRGQNQPVLNITNRQAFITAQNHGYALD-NTLPAGWKPLFVNVNDQTNEGIMHESKPFFAVQ 375
Cdd:cd01744 79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDpDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158
|
170 180
....*....|....*....|
gi 8393186 376 FHPEVSPGPTDTEYLFDSFF 395
Cdd:cd01744 159 FHPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
48-183 |
3.08e-64 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.
Pssm-ID: 460017 [Multi-domain] Cd Length: 126 Bit Score: 213.73 E-value: 3.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 48 IVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGAPDttardelglnKYMESDGIK 127
Cdd:pfam00988 1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNP----------EDFESDKIH 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 8393186 128 VAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI 183
Cdd:pfam00988 71 VAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
44-183 |
8.83e-63 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 209.54 E-value: 8.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 44 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGAPDttardelglnKYMES 123
Cdd:smart01097 1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVND----------EDFES 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 124 DGIKVAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI 183
Cdd:smart01097 71 DKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
839-962 |
4.06e-54 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 184.58 E-value: 4.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 839 LRKELSEPSSTRIYAIAKALENNMSLDEIVKLTSIDKWFLYKMRDILNMDKTLKGLNSESVTEETLRQAKEIGFSDKQIS 918
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 8393186 919 KCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTY 962
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1360-1475 |
1.53e-48 |
|
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: 168.25 E-value: 1.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1360 KGILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSlSSIRKLIRDGSIDLVINLP 1439
Cdd:cd01423 1 KGILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK-PSLRELLAEGKIDLVINLP 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 8393186 1440 NNNTKFVHDN-YVIRRTAVDSGIALLTNFQVTKLFAE 1475
Cdd:cd01423 80 SNRGKRVLDNdYVMRRAADDFAVPLITNPKCAKLFIE 116
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
419-1477 |
0e+00 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 1538.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 419 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEvglKQADAVYFLPITPQFVTEVIKA 498
Cdd:TIGR01369 3 RTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDP---EMADKVYIEPLTPEAVEKIIEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 499 ERPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESMEDALKAAD 578
Cdd:TIGR01369 80 ERPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 579 TIGYPVMIRSAYALGGLGSGICPNKETLMDLGTKAFAMT--NQILVERSVTGWKEIEYEVVRDADDNCVTVCNMENVDAM 656
Cdd:TIGR01369 160 EIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 657 GVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAF 736
Cdd:TIGR01369 240 GVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 737 IAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMC 816
Cdd:TIGR01369 320 VAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 817 HPSVDGFtpRLPMNKEWPaNLDLRKELSEPSSTRIYAIAKALENNMSLDEIVKLTSIDKWFLYKMRDILNMDKTLKGLNS 896
Cdd:TIGR01369 400 EIGATGF--DLPDREVEP-DEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 897 ESVTEETLRQAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDIKF-DEHG 975
Cdd:TIGR01369 477 TDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 976 IMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACNGCIIS 1055
Cdd:TIGR01369 557 VLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1056 VGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFANSVGYPCLLRPSYVLS 1135
Cdd:TIGR01369 637 FGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLG 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1136 GSAMNVVFSEDEMKRFLEEATRVSQEHPVVLTKFIEGAREVEMDAVGKEGRVISHAISEHVEDAGVHSGDATLMLPTQTI 1215
Cdd:TIGR01369 717 GRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTL 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1216 SQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGESVDEkhLPT 1295
Cdd:TIGR01369 797 SAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEE--LGV 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1296 LEQPiiPSDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQSFRPRF 1374
Cdd:TIGR01369 875 GKEK--EPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGsVLLSVRDKDKEEL 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1375 LGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRR 1454
Cdd:TIGR01369 953 LDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPN-----ILDLIKNGEIELVINTTSKGAGTATDGYKIRR 1027
|
1050 1060
....*....|....*....|...
gi 8393186 1455 TAVDSGIALLTNFQVTKLFAEAV 1477
Cdd:TIGR01369 1028 EALDYGVPLITTLNTAEAFAEAL 1050
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
419-1491 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1434.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 419 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTN-EVglkqADAVYFLPITPQFVTEVIK 497
Cdd:PRK05294 4 RTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDpEM----ADATYIEPITPEFVEKIIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 498 AERPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESMEDALKAA 577
Cdd:PRK05294 80 KERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 578 DTIGYPVMIRSAYALGGLGSGICPNKETLMDLGTKAFAM--TNQILVERSVTGWKEIEYEVVRDADDNCVTVCNMENVDA 655
Cdd:PRK05294 160 EEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 656 MGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIV-GECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPL 734
Cdd:PRK05294 240 MGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 735 AFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALR 814
Cdd:PRK05294 320 AKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 815 MCHPSVDGFTPRL--PMNKEwpanlDLRKELSEPSSTRIYAIAKALENNMSLDEIVKLTSIDKWFLYKMRDILNMDKTLK 892
Cdd:PRK05294 400 SLEIGVTGLDEDLfeEESLE-----ELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 893 GlNSESVTEETLRQAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDIKFD 972
Cdd:PRK05294 475 E-NGLPLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 973 EHGIMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACNGC 1052
Cdd:PRK05294 554 RKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGV 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1053 IISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFANSVGYPCLLRPSY 1132
Cdd:PRK05294 634 IVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSY 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1133 VLSGSAMNVVFSEDEMKRFLEEATRVSQEHPVVLTKFIEGAREVEMDAV--GKEgrVISHAISEHVEDAGVHSGDATLML 1210
Cdd:PRK05294 714 VLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAIcdGED--VLIGGIMEHIEEAGVHSGDSACSL 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1211 PTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGESVDE 1290
Cdd:PRK05294 792 PPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAE 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1291 KHlptLEQPIIPsDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQS 1369
Cdd:PRK05294 872 LG---YTKGLIP-PYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGtVFLSVRDR 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1370 FRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKfVHDN 1449
Cdd:PRK05294 948 DKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPH-----IVDLIKNGEIDLVINTPTGRQA-IRDG 1021
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....
gi 8393186 1450 YVIRRTAVDSGIALLTNFQVTKLFAEAVQKART--VDSKSLFHY 1491
Cdd:PRK05294 1022 FSIRRAALEYKVPYITTLAGARAAVKAIEALKFgeLEVRSLQEY 1065
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
419-1493 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1104.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 419 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEvglKQADAVYFLPITPQFVTEVIKA 498
Cdd:PRK12815 4 DTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDP---APADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 499 ERPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESMEDALKAAD 578
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 579 TIGYPVMIRSAYALGGLGSGICPNKETLMDLGTKAFA--MTNQILVERSVTGWKEIEYEVVRDADDNCVTVCNMENVDAM 656
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQasPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 657 GVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAF 736
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 737 IAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRmc 816
Cdd:PRK12815 321 IAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALR-- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 817 hpSVDGFTPRLPM-NKEWPANLD-LRKELSEPSSTRIYAIAKALENNMSLDEIVKLTSIDKWFLYKMRDILNMDKTLKGl 894
Cdd:PRK12815 399 --SLEIKRNGLSLpIELSGKSDEeLLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAE- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 895 NSESVTEETLRQAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQ-EHDIKFDE 973
Cdd:PRK12815 476 DGLDLSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGEsEAEPSSEK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 974 HGIMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACNGCI 1053
Cdd:PRK12815 556 KKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVI 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1054 ISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFANSVGYPCLLRPSYV 1133
Cdd:PRK12815 636 VQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYV 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1134 LSGSAMNVVFSEDEMKRFLEEAtrVSQEHPVVLTKFIEGArEVEMDAVGKEGRVISHAISEHVEDAGVHSGDATLMLPTQ 1213
Cdd:PRK12815 716 IGGQGMAVVYDEPALEAYLAEN--ASQLYPILIDQFIDGK-EYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVLPPQ 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1214 TISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGESVDEKHL 1293
Cdd:PRK12815 793 SLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELGY 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1294 PTLEQPIipSDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQSFRP 1372
Cdd:PRK12815 873 PNGLWPG--SPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGtIFISVRDEDKP 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1373 RFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAwPSQEGQNPSLSsirklIRDGSIDLVINLPNNNTKFVHDNYVI 1452
Cdd:PRK12815 951 EVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVE-KVQEGSPSLLE-----RIKQHRIVLVVNTSLSDSASEDAIKI 1024
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|...
gi 8393186 1453 RRTAVDSGIALLTNFQVTKLFAEAVQKAR--TVDSKSLFHYRQ 1493
Cdd:PRK12815 1025 RDEALSTHIPVFTELETAQAFLQVLESLAltTQPIQELQEKHK 1067
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
404-1482 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 909.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 404 TTITSVLPKPALVASRVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEvglKQADAVY 483
Cdd:PLN02735 5 DTVTRAWSAATKAGKRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDP---ETADRTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 484 FLPITPQFVTEVIKAERPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAP 563
Cdd:PLN02735 82 IAPMTPELVEQVIAKERPDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 564 SFAVESMEDALKAADTIG-YPVMIRSAYALGGLGSGICPNKETLMDLGTKAFA--MTNQILVERSVTGWKEIEYEVVRDA 640
Cdd:PLN02735 162 SGIATTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAasITSQVLVEKSLLGWKEYELEVMRDL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 641 DDNCVTVCNMENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIvgEC---NIQFALHPTSMEYCIIEVNA 717
Cdd:PLN02735 242 ADNVVIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 718 RLSRSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGE 797
Cdd:PLN02735 320 RVSRSSALASKATGFPIAKMAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 798 VMAIGRTFEESFQKALRMCHPSVDGFTPrlPMNKEWPANLD-LRKELSEPSSTRIYAIAKALENNMSLDEIVKLTSIDKW 876
Cdd:PLN02735 400 AMALGRTFQESFQKALRSLETGFSGWGC--AKVKELDWDWEqLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPW 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 877 FLYKMRDILNMDKTLKGLNSESVTEETLRQAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTN 956
Cdd:PLN02735 478 FLTQLKELVDVEQFLKSRSLSELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTP 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 957 YLYVTYNGQEHDIKFDEHGIMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELS 1036
Cdd:PLN02735 558 YMYSSYDGECESAPTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLT 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1037 LERILDIYHQEACNGCIISVGGQIPNNLAVPLYK------------NG-VKIMGTSPLQIDRAEDRSIFSAVLDELKVAQ 1103
Cdd:PLN02735 638 VEDVLNVIDLERPDGIIVQFGGQTPLKLALPIQKyldknpppsasgNGnVKIWGTSPDSIDAAEDRERFNAILNELKIEQ 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1104 APWKAVNTLNEALEFANSVGYPCLLRPSYVLSGSAMNVVFSEDEMKRFLEEATRVSQEHPVVLTKFIEGAREVEMDAVG- 1182
Cdd:PLN02735 718 PKGGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAd 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1183 KEGRVISHAISEHVEDAGVHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLV-KGNDVLVIECNLRAS 1261
Cdd:PLN02735 798 SEGNVVIGGIMEHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRAS 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1262 RSFPFVSKTLGVDFIDVATKVMIGESVDEkhLPTLEQPIIPsdYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEG 1341
Cdd:PLN02735 878 RTVPFVSKAIGHPLAKYASLVMSGKSLKD--LGFTEEVIPA--HVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYE 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1342 IHTAFLKAMLSTGFKIPQKG-ILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAwPSQEGQnpsl 1420
Cdd:PLN02735 954 FSKAFAKAQIAAGQRLPLSGtVFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVL-KLHEGR---- 1028
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8393186 1421 SSIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRRTAVDSGIALLTNFQVTKLFAEAVQKART 1482
Cdd:PLN02735 1029 PHAGDMLANGQIQLMVITSSGDALDQKDGRQLRRMALAYKVPIITTVAGALATAQAVKSLKE 1090
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
428-980 |
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: 618.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 428 LGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQT-NEVglkqADAVYFLPITPQFVTEVIKAERPDGLIL 506
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTdYDT----ADRLYFEPLTVEDVLDIIEKEKPDGVIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 507 GMGGQTALNCGVELFKRGVLKeyGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESMEDALKAADTIGYPVMI 586
Cdd:COG0458 77 QFGGQTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 587 RSAYALGGLGSGICPNKETLMDLGTKAFA--MTNQILVERSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHTGDSV 664
Cdd:COG0458 155 RPSYVLGGRGMGIVYNEEELEEYLERALKvsPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 665 VVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHptSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALG 744
Cdd:COG0458 235 CVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 745 IPLPEIKNvvsgKTSacFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSVDG-- 822
Cdd:COG0458 313 YTLDELGN----DTG--FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtv 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 823 FTPRLpMNKEWPANLDLRKELSepsstRIYAIAKALENNMSLDEIVKLTSIDKWFLYKMRDILNMDKTLKGlnsESVTEE 902
Cdd:COG0458 387 LLSLV-ADDDKEEALLLARRLA-----RLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEE---IILVIN 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393186 903 TLRQAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDIKFDEHGIMVLG 980
Cdd:COG0458 458 TLLGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIG 535
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
979-1494 |
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: 550.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 979 LGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACNGCIISVGG 1058
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1059 QIPNNLAVPLYKN----GVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFANSVGYPCLLRPSYVL 1134
Cdd:COG0458 81 QTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1135 SGSAMNVVFSEDEMKRFLEEATRVSQEHPVVLTKFIEGAREVEMDAVG-KEGRVISHAISEHVEDAGVHSGDATLMLPTQ 1213
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRdGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1214 TISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGESVDEKHL 1293
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1294 PTLEQPIIpsDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPR 1373
Cdd:COG0458 321 DTGFEPTL--DYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLLSLVADDDKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1374 FLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKFVHDNYVIR 1453
Cdd:COG0458 399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPI-----IVDEIELEEIILVINTLLGAKSLGDSDGIIR 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 8393186 1454 RTAVDSGIALLTNF---QVTKLFAEAVQKARTVDSKSLFHYRQY 1494
Cdd:COG0458 474 RALAAKVPYVTTLAaaaAAALAIKAVETEAGEFEEATAYYYSTY 517
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
46-400 |
3.36e-172 |
|
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: 519.49 E-value: 3.36e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 46 AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGAPDTTardelglnkyMESDG 125
Cdd:TIGR01368 1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDED----------AESKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 126 IKVAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQSVDF------VDPNKQ- 198
Cdd:TIGR01368 71 IHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEElvekarVSPDITg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 199 -NLIAEVSTKDVKVFGK--GNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTQ---MDYDGLLIAGGPGNPALAQ 272
Cdd:TIGR01368 151 iNLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEikkYNPDGIFLSNGPGDPAAVE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 273 PLIQNVKKILEsdrKEPLFGISTGNIITGLAAGAKSYKMSMANRGQNQPVLNITNRQAFITAQNHGYALDN-TLPAG-WK 350
Cdd:TIGR01368 231 PAIETIRKLLE---KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPdSLPAGdLE 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 8393186 351 PLFVNVNDQTNEGIMHESKPFFAVQFHPEVSPGPTDTEYLFDSFFSLIKK 400
Cdd:TIGR01368 308 VTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
44-398 |
2.45e-143 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 442.98 E-value: 2.45e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 44 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGAPDttaRDelglnkyMES 123
Cdd:PRK12564 3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNR---ED-------FES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 124 DGIKVAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQSVD--------FVDP 195
Cdd:PRK12564 73 DRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEellekaraFPGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 196 NKQNLIAEVSTKDVKVFGKGNPT---KVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTQMDYDGLLIAGGPGNPA 269
Cdd:PRK12564 153 LGLDLVKEVSTKEPYPWPGPGGElkyKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 270 LAQPLIQNVKKILESDRkePLFGISTGNIITGLAAGAKSYKMSMANRGQNQPVLNITNRQAFITAQNHGYALD-NTLPAG 348
Cdd:PRK12564 233 ALDYAIEMIRELLEKKI--PIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDeDSLPAN 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 8393186 349 WKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVSPGPTDTEYLFDSFFSLI 398
Cdd:PRK12564 311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
44-399 |
2.83e-137 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 426.74 E-value: 2.83e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 44 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGAPDttardelglnKYMES 123
Cdd:COG0505 3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVND----------EDFES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 124 DGIKVAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQSVD--------FVDP 195
Cdd:COG0505 73 DRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEellekaraAPGM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 196 NKQNLIAEVSTKDVKVFG--KGNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTQ---MDYDGLLIAGGPGNPAL 270
Cdd:COG0505 153 EGLDLVKEVSTKEPYEWTeaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEilaLNPDGVFLSNGPGDPAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 271 AQPLIQNVKKILESDRkePLFGISTGNIITGLAAGAKSYKMSMANRGQNQPVLNITNRQAFITAQNHGYALD-NTLPA-G 348
Cdd:COG0505 233 LDYAIETIRELLGKGI--PIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDeDSLPAtD 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 8393186 349 WKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVSPGPTDTEYLFDSFFSLIK 399
Cdd:COG0505 311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
46-402 |
7.98e-107 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 343.80 E-value: 7.98e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 46 AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGAPDttardelglnKYMESDG 125
Cdd:PRK12838 3 AYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINA----------DDYESKQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 126 IKVAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI----EFEGQSVDFVDPNKQNLI 201
Cdd:PRK12838 73 PQVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASItttdDAHAFDQIKALVLPKNVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 202 AEVSTKDVKVFGKGNPTkVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTQMDYDGLLIAGGPGNPALAQPLIQNV 278
Cdd:PRK12838 153 AQVSTKEPYTYGNGGKH-VALIDFGYKKSILRSLSKRGCKVTVLPYDtslEEIKNLNPDGIVLSNGPGDPKELQPYLPEI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 279 KKILESdrkEPLFGISTGNIITGLAAGAKSYKMSMANRGQNQPVLNITNRQAFITAQNHGYAL--DNTLPAGWKPLFVNV 356
Cdd:PRK12838 232 KKLISS---YPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVdeDSLDGTPLSVRFFNV 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 8393186 357 NDQTNEGIMHESKPFFAVQFHPEVSPGPTDTEYLFDSFFSLIKKGK 402
Cdd:PRK12838 309 NDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKAR 354
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
546-748 |
1.52e-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: 328.49 E-value: 1.52e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 546 DRQLFSDKLNEINEKIAPSFA--VESMEDALKAADTIGYPVMIRSAYALGGLGSGICPNKETLMDLGTKAFAMT------ 617
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 618 NQILVERSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMgvHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGEC 697
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 8393186 698 NIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLP 748
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
220-395 |
5.63e-96 |
|
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: 305.96 E-value: 5.63e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 220 VVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDF---TQMDYDGLLIAGGPGNPALAQPLIQNVKKILESdrKEPLFGISTG 296
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAeeiLKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGK--KIPIFGICLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 297 NIITGLAAGAKSYKMSMANRGQNQPVLNITNRQAFITAQNHGYALD-NTLPAGWKPLFVNVNDQTNEGIMHESKPFFAVQ 375
Cdd:cd01744 79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDpDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158
|
170 180
....*....|....*....|
gi 8393186 376 FHPEVSPGPTDTEYLFDSFF 395
Cdd:cd01744 159 FHPEASPGPHDTEYLFDEFL 178
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
46-402 |
2.51e-82 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 275.91 E-value: 2.51e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 46 AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGapdTTARDelglnkyMESDG 125
Cdd:CHL00197 7 AILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTG---INLED-------IESVK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 126 IKVAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQSVDFVDPNKQ------- 198
Cdd:CHL00197 77 IQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSYLRAKIKesphmps 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 199 -NLIAEVSTKDVKVFGK----------------GNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTQ-MDY--DG 258
Cdd:CHL00197 157 sDLIPRVTTSSYYEWDEkshpsfyladnkrphsSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDiLSYqpDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 259 LLIAGGPGNPALAQPLIQNVKKILesDRKEPLFGISTGNIITGLAAGAKSYKMSMANRGQNQPVLniTNRQAFITAQNHG 338
Cdd:CHL00197 237 ILLSNGPGDPSAIHYGIKTVKKLL--KYNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSG--LNQQVEITSQNHG 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393186 339 YALDntLPAGWKPLF----VNVNDQTNEGIMHESKPFFAVQFHPEVSPGPTDTEYLFDSFFSLIKKGK 402
Cdd:CHL00197 313 FAVN--LESLAKNKFyithFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSK 378
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
17-391 |
6.22e-69 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 238.73 E-value: 6.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 17 GFGLANVTSKRQWDFSRPGIRLLSVKAQT-------------------AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGL 77
Cdd:PLN02771 9 GFVLPTSLSSQPSFDRRGGVRVSVIRCSSspltsdgagvverpwktsdARLVLEDGSVWKAKSFGARGTQVGEVVFNTSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 78 GGYSEALTDPAYKGQILTMANPIIGNGGA-PDttarDElglnkymESDGIKVAGLLVLNYSHDYNHWLATKSLGQWLQEE 156
Cdd:PLN02771 89 TGYQEILTDPSYAGQFVLMTNPHIGNTGVnFD----DE-------ESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 157 KVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQSVD--------FVDPNKQNLIAEVSTK-------------DVKVFGK- 214
Cdd:PLN02771 158 NIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDeellkmsrSWDIVGIDLISGVSCKspyewvdktnpewDFNTNSRd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 215 GNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTQMDYDGLLIAGGPGNPALAQPLIQNVKKILEsdrKEPLF 291
Cdd:PLN02771 238 GESYHVIAYDFGIKHNILRRLASYGCKITVVPSTwpaSEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLG---KVPVF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 292 GISTGNIITGLAAGAKSYKMSMANRGQNQPVLNITNRQAFITAQNHGYALD-NTLPAGWKPLFVNVNDQTNEGIMHESKP 370
Cdd:PLN02771 315 GICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDpASLPEGVEVTHVNLNDGSCAGLAFPALN 394
|
410 420
....*....|....*....|.
gi 8393186 371 FFAVQFHPEVSPGPTDTEYLF 391
Cdd:PLN02771 395 VMSLQYHPEASPGPHDSDNAF 415
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
48-183 |
3.08e-64 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.
Pssm-ID: 460017 [Multi-domain] Cd Length: 126 Bit Score: 213.73 E-value: 3.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 48 IVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGAPDttardelglnKYMESDGIK 127
Cdd:pfam00988 1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNP----------EDFESDKIH 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 8393186 128 VAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI 183
Cdd:pfam00988 71 VAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
44-183 |
8.83e-63 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 209.54 E-value: 8.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 44 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGAPDttardelglnKYMES 123
Cdd:smart01097 1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVND----------EDFES 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 124 DGIKVAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI 183
Cdd:smart01097 71 DKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
839-962 |
4.06e-54 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 184.58 E-value: 4.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 839 LRKELSEPSSTRIYAIAKALENNMSLDEIVKLTSIDKWFLYKMRDILNMDKTLKGLNSESVTEETLRQAKEIGFSDKQIS 918
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 8393186 919 KCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTY 962
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
221-395 |
4.73e-52 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 181.28 E-value: 4.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 221 VAVDCG--IKNNVIRLLVKRGAEVHLVPWNHDFT---QMDYDGLLIAGGPGNPALAQPLIQNVKKILEsdRKEPLFGIST 295
Cdd:pfam00117 1 LLIDNGdsFTYNLARALRELGVEVTVVPNDTPAEeilEENPDGIILSGGPGSPGAAGGAIEAIREARE--LKIPILGICL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 296 GNIITGLAAGAKSYKMSM-ANRGQNQPVLNITNR------QAFITAQNHGYALDN-TLPAGWKPLFVNVNDQTNEGIMHE 367
Cdd:pfam00117 79 GHQLLALAFGGKVVKAKKfGHHGKNSPVGDDGCGlfyglpNVFIVRRYHSYAVDPdTLPDGLEVTATSENDGTIMGIRHK 158
|
170 180
....*....|....*....|....*...
gi 8393186 368 SKPFFAVQFHPEVSPGPTDTEYLFDSFF 395
Cdd:pfam00117 159 KLPIFGVQFHPESILTPHGPEILFNFFI 186
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1360-1475 |
1.53e-48 |
|
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: 168.25 E-value: 1.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1360 KGILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSlSSIRKLIRDGSIDLVINLP 1439
Cdd:cd01423 1 KGILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK-PSLRELLAEGKIDLVINLP 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 8393186 1440 NNNTKFVHDN-YVIRRTAVDSGIALLTNFQVTKLFAE 1475
Cdd:cd01423 80 SNRGKRVLDNdYVMRRAADDFAVPLITNPKCAKLFIE 116
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
841-919 |
1.87e-29 |
|
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: 112.47 E-value: 1.87e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8393186 841 KELSEPSSTRIYAIAKALENNMSLDEIVKLTSIDKWFLYKMRDILNMDKTLKGlNSESVTEETLRQAKEIGFSDKQISK 919
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKE-AGLDLDAELLREAKRLGFSDRQIAK 78
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
1088-1289 |
1.22e-28 |
|
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: 115.09 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1088 DRSIFSAVLDELKVAQAPWKA--VNTLNEALEFANSVGYPCLLRPSYVLSGSAMNVVFSEDEM----KRFLEEATRVSQE 1161
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELaelfALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1162 HPVVLTKFIEGAREVEMDAVG-KEGRVIsHAISEHVEDAgVHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPF 1240
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRdAHGNCI-TVCNRECSDQ-RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 8393186 1241 NVQFLV--KGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGESVD 1289
Cdd:pfam02786 159 TVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1373-1465 |
1.29e-23 |
|
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: 96.40 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1373 RFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPNNNTKFVHDNYVI 1452
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEGRPGGRVQIGDLIKNGEIDLVINTLYPFKATVHDGYAI 80
|
90
....*....|...
gi 8393186 1453 RRTAVDSGIALLT 1465
Cdd:pfam02142 81 RRAAENIDIPGPT 93
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
1077-1288 |
2.91e-23 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 101.10 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1077 GTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFANSVGYPCLLRPSYvLSGSA-MNVVFSEDEMKRFLE-- 1153
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPAD-GAGSRgVRVVRDEEELEAALAea 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1154 --EATRVSQEHPVVLTKFIEGaREVEMDAVGKEGRVISHAISEHVEDA--GVHSGDatlMLPTQtISQGAIEKVKDATRK 1229
Cdd:COG0439 122 raEAKAGSPNGEVLVEEFLEG-REYSVEGLVRDGEVVVCSITRKHQKPpyFVELGH---EAPSP-LPEELRAEIGELVAR 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8393186 1230 IAKAFAIS-GPFNVQFLVKGNDVLV-IECNLRAS--RSFPFVSKTLGVDFIDVATKVMIGESV 1288
Cdd:COG0439 197 ALRALGYRrGAFHTEFLLTPDGEPYlIEINARLGgeHIPPLTELATGVDLVREQIRLALGEPR 259
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
535-746 |
5.97e-16 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 79.53 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 535 GTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESMEDALKAADTIGYPVMIRSAYALGGLGSGICPNKETLmdlgTKAF 614
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEL----EAAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 615 AMTNQ----------ILVERSVTGwKEIEYEVVrdADDNCVTVCNM---ENVDAMGVHTGDsvvVAPAQtLSNAEFQMLR 681
Cdd:COG0439 119 AEARAeakagspngeVLVEEFLEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIG 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393186 682 RTSINVVRHLGIV-GECNIQFALHPtSMEYCIIEVNARLS--RSSALASKATGYPLAFIAAKIALGIP 746
Cdd:COG0439 192 ELVARALRALGYRrGAFHTEFLLTP-DGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
1371-1466 |
8.82e-15 |
|
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: 71.74 E-value: 8.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1371 RPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNtKFVHDNY 1450
Cdd:cd01424 12 KPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPN-----IVDLIKNGEIQLVINTPSGK-RAIRDGF 85
|
90
....*....|....*.
gi 8393186 1451 VIRRTAVDSGIALLTN 1466
Cdd:cd01424 86 SIRRAALEYKVPYFTT 101
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1373-1465 |
1.32e-14 |
|
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: 70.58 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1373 RFLGVAEQLHNEGFKLFATEATSDWLNANNVP--ATPVAWPSqEGQNpslsSIRKLIRDGSIDLVINLPNNNTK-FVHDN 1449
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPvvKTLHPKVH-GGIP----QILDLIKNGEIDLVINTLYPFEAqAHEDG 75
|
90
....*....|....*.
gi 8393186 1450 YVIRRTAVDSGIALLT 1465
Cdd:smart00851 76 YSIRRAAENIDIPGPT 91
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
1097-1255 |
8.27e-13 |
|
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: 68.05 E-value: 8.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1097 DELKVAQAPWKAVNTLNEALEFANSVGYPCLL---RPSYvlSGSAMNVVFSEDEMKRFLEEATRVsqehPVVLTKFIEGA 1173
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEELGDG----PVIVEEFVPFD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1174 REV-EMDAVGKEGRVISHAISEHVEdagvHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQ-FLVKGNDV 1251
Cdd:pfam02222 75 RELsVLVVRSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVElFVTEDGDL 150
|
....
gi 8393186 1252 LVIE 1255
Cdd:pfam02222 151 LINE 154
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
424-750 |
2.70e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 69.91 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 424 KVLILGSGGlsigqagefdysGSQAVKAMKEE----NVKTVLMNPNIAsvqtnevGLKQADAVYFLP-ITP----QFVTE 494
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSllkgRVIGADISELAP-------ALYFADKFYVVPkVTDpnyiDRLLD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 495 VIKAERPDGLILGMGgqtalncgVELFK----RGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESM 570
Cdd:PRK12767 64 ICKKEKIDLLIPLID--------PELPLlaqnRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 571 EDALKA--ADTIGYPVMIRSAYALGGLGSGICPNKETLMDLgtkaFAMTNQILVERSVTGwKEIEYEVVRDADDNCVTVC 648
Cdd:PRK12767 136 EDFKAAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELEFL----LEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 649 NMENVDAMGVHTGDSVVVapaqtlsnaEFQMLRRTSINVVRHLGIVGECNIQFALhpTSMEYCIIEVNARLSRSSALASK 728
Cdd:PRK12767 211 PRKRIEVRAGETSKGVTV---------KDPELFKLAERLAEALGARGPLNIQCFV--TDGEPYLFEINPRFGGGYPLSYM 279
|
330 340
....*....|....*....|...
gi 8393186 729 ATG-YPlAFIAAKIALGIPLPEI 750
Cdd:PRK12767 280 AGAnEP-DWIIRNLLGGENEPII 301
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
563-832 |
1.15e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 65.82 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 563 PSFAVESMEDALKAADTIGYPVMIRSAYALGGLGSGICPNKETLmdlgTKAFAMTNQ----------ILVERSVTGWKEI 632
Cdd:PRK06111 134 ITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQEL----TKAFESNKKraanffgngeMYIEKYIEDPRHI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 633 EYEVVRDADDNCvtvcnmenvdamgVHTGD---SV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQF 701
Cdd:PRK06111 210 EIQLLADTHGNT-------------VYLWErecSVqrrhqkVIeeAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEF 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 702 ALHPTSMEYcIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLP----EIKnvVSGKTSAC---------FEPSldy 768
Cdd:PRK06111 277 LVDEQKNFY-FLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSftqdDIK--RSGHAIEVriyaedpktFFPS--- 350
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393186 769 mVTKIPRWDLDRfhGTSSRIGSSMKS-----------VGEVMAIGRTFEESFQK---ALRMCHpsVDGFTPRLPMNKE 832
Cdd:PRK06111 351 -PGKITDLTLPG--GEGVRHDHAVENgvtvtpfydpmIAKLIAHGETREEAISRlhdALEELK--VEGIKTNIPLLLQ 423
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
230-379 |
5.24e-10 |
|
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.
Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 60.57 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 230 NVIRLLVKRGAEVHlVPWNHDFTQMDYDGLL-----IAGGPGNPALAQpliQNVKKILESDRKEPLFGISTGNIITGLAA 304
Cdd:TIGR00566 14 NLVQYFCELGAEVV-VKRNDSLTLQEIEALLpllivISPGPCTPNEAG---ISLEAIRHFAGKLPILGVCLGHQAMGQAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 305 GAKsykMSMANRGQNQPVLNITNRQAFITAqnhgyALDNTLPAG-WKPLFVN---------VNDQTNE-----GIMHESK 369
Cdd:TIGR00566 90 GGD---VVRANTVMHGKTSEIEHNGAGIFR-----GLFNPLTATrYHSLVVEpetlptcfpVTAWEEEnieimAIRHRDL 161
|
170
....*....|
gi 8393186 370 PFFAVQFHPE 379
Cdd:TIGR00566 162 PLEGVQFHPE 171
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
528-748 |
2.11e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 61.66 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 528 EYGVKVLGTSVESImatedRQLfSDKLNEINEKIAPSFAV--------ESMEDALKAADTIGYPVMIRSAYALGGLGSGI 599
Cdd:PRK07178 96 ERGIKFIGPSAEVI-----RRM-GDKTEARRAMIKAGVPVtpgsegnlADLDEALAEAERIGYPVMLKATSGGGGRGIRR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 600 CPNKETL-------MDLGTKAFAMTnQILVERSVTGWKEIEYEVVRDADDNCVTV----CNMENVDAMGVHtgdsvvVAP 668
Cdd:PRK07178 170 CNSREELeqnfprvISEATKAFGSA-EVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQRRNQKLIE------IAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 669 AQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYcIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLP 748
Cdd:PRK07178 243 SPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVY-FMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLS 321
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
424-748 |
5.07e-09 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 59.94 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 424 KVLILGS--GGLSIgqagefdysgsqaVKAMKEENVKTVLmnpniASVQTNEVGL--KQADAVYFLP----ITPQFV--- 492
Cdd:COG3919 7 RVVVLGGdiNALAV-------------ARSLGEAGVRVIV-----VDRDPLGPAArsRYVDEVVVVPdpgdDPEAFVdal 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 493 TEVIKAERPDgLILGMGgqtalNCGVELF--KRGVLKEYgVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESM 570
Cdd:COG3919 69 LELAERHGPD-VLIPTG-----DEYVELLsrHRDELEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 571 EDALKAADTIGYPVMIRSAY--------ALGGLGSGICPNKETLMDLGTKAFAMTNQILVERSVTGWKEIEY--EVVRDA 640
Cdd:COG3919 142 DDLDALAEDLGFPVVVKPADsvgydelsFPGKKKVFYVDDREELLALLRRIAAAGYELIVQEYIPGDDGEMRglTAYVDR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 641 DDNCVTVC----NMENVDAMGVHTGdsvvvapAQTLSNAEfqmLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVN 716
Cdd:COG3919 222 DGEVVATFtgrkLRHYPPAGGNSAA-------RESVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEIN 291
|
330 340 350
....*....|....*....|....*....|..
gi 8393186 717 ARLSRSSALASKAtGYPLAFIAAKIALGIPLP 748
Cdd:COG3919 292 PRFWRSLYLATAA-GVNFPYLLYDDAVGRPLE 322
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1070-1290 |
5.14e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 59.51 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1070 KNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALE--FANSVGYPCLLRPsYVLSGSA-MNVVFSED 1146
Cdd:PRK12767 93 EIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAalAKGELQFPLFVKP-RDGSASIgVFKVNDKE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1147 EMKRFLEEATrvsqehPVVLTKFIEGaREVEMDA-VGKEGRVISHAISEHVEdagVHSGDATlmlptQTISqGAIEKVKD 1225
Cdd:PRK12767 172 ELEFLLEYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGETS-----KGVT-VKDPELFK 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8393186 1226 ATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFvSKTLGVDFIDVATKVMIGESVDE 1290
Cdd:PRK12767 236 LAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL-SYMAGANEPDWIIRNLLGGENEP 299
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
229-379 |
5.86e-09 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 57.16 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 229 NNVIRLLVKRGAEVHLVPwNHDFT-----QMDYDGLLIAGGPGNPALAQPLIQNVKKILesdRKEPLFGISTGNIITGLA 303
Cdd:cd01743 12 YNLVQYLRELGAEVVVVR-NDEITleeleLLNPDAIVISPGPGHPEDAGISLEIIRALA---GKVPILGVCLGHQAIAEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 304 AGAKSYKMSMANRGQnQPVLNITNR-------QAFITAQNHGYALD-NTLPAGWKplfvnVNDQTNEG-IM---HESKPF 371
Cdd:cd01743 88 FGGKVVRAPEPMHGK-TSEIHHDGSglfkglpQPFTVGRYHSLVVDpDPLPDLLE-----VTASTEDGvIMalrHRDLPI 161
|
....*...
gi 8393186 372 FAVQFHPE 379
Cdd:cd01743 162 YGVQFHPE 169
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
525-749 |
1.79e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 58.60 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 525 VLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSF--AVESMEDALKAADTIGYPVMIRSAYALGGLGSGICPN 602
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 603 KETLMDLGTKAF--AMT----NQILVERSVTGWKEIEYEVVRDADDNCVTV----CNMENvdamgvHTGDSVVVAPAQTL 672
Cdd:PRK08462 176 ESDLENLYLAAEseALSafgdGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVL 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8393186 673 SNAEFQMLRRTSINVVRHLGIVGECNIQFaLHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLPE 749
Cdd:PRK08462 250 DEKTRERLHETAIKAAKAIGYEGAGTFEF-LLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPS 325
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
233-382 |
2.33e-08 |
|
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: 56.49 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 233 RLLVKRGAEVH--------LVPWNHDFTqmDYDGLLIAGGPGNP----ALAQPLIQNVKKILESDRkePLFGISTGNIIT 300
Cdd:COG0518 20 RRLREAGIELDvlrvyageILPYDPDLE--DPDGLILSGGPMSVydedPWLEDEPALIREAFELGK--PVLGICYGAQLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 301 GLAAGAKSYKMSMANRGQnQPVlNITNRQA--------FITAQNHGYALDnTLPAGWKPLFVNVNDQtNEGIMHEsKPFF 372
Cdd:COG0518 96 AHALGGKVEPGPGREIGW-APV-ELTEADPlfaglpdeFTVWMSHGDTVT-ELPEGAEVLASSDNCP-NQAFRYG-RRVY 170
|
170
....*....|
gi 8393186 373 AVQFHPEVSP 382
Cdd:COG0518 171 GVQFHPEVTH 180
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
996-1188 |
4.19e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 57.69 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 996 AVSSIRTLRQLGKKTVVVncnpetvstdFDECDK-----LYFEE-------------LSLERILDIYHQEACNGciISVG 1057
Cdd:PRK08654 14 AIRVMRACRELGIKTVAV----------YSEADKnalfvKYADEaypigpappsksyLNIERIIDVAKKAGADA--IHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1058 -GQIPNN--LAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPW--KAVNTLNEALEFANSVGYPCLLRPSY 1132
Cdd:PRK08654 82 yGFLAENpeFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGteEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8393186 1133 VLSGSAMNVVFSEDEMKRFLEEATRVSQ----EHPVVLTKFIEGAREVEMDAVG-KEGRVI 1188
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQsafgDSTVFIEKYLEKPRHIEIQILAdKHGNVI 222
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
996-1358 |
8.01e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 56.57 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 996 AVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYF--------EELSLERILDIyhQEACNGCIISVG-GQIPNN--L 1064
Cdd:PRK06111 14 AVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLiggprvqeSYLNLEKIIEI--AKKTGAEAIHPGyGLLSENasF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1065 AVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPW--KAVNTLNEALEFANSVGYPCLLRPSYVLSGSAMNVV 1142
Cdd:PRK06111 92 AERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGitTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1143 FSEDEMKRFLE----EATRVSQEHPVVLTKFIEGAREVEM----DAVGkegrvisHAI----------SEH---VEDAgv 1201
Cdd:PRK06111 172 ETEQELTKAFEsnkkRAANFFGNGEMYIEKYIEDPRHIEIqllaDTHG-------NTVylwerecsvqRRHqkvIEEA-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1202 hsgdatlmlPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLV-KGNDVLVIECNLRASRSFPFVSKTLGVDFIDVAT 1280
Cdd:PRK06111 243 ---------PSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVdEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1281 KVMIGESVdekhlpTLEQPIIPSDYVAIKApmfswpRLRDADPILRceMASTGEVACF----GEGI-HTAFLKAmlstGF 1355
Cdd:PRK06111 314 RIAAGEKL------SFTQDDIKRSGHAIEV------RIYAEDPKTF--FPSPGKITDLtlpgGEGVrHDHAVEN----GV 375
|
...
gi 8393186 1356 KIP 1358
Cdd:PRK06111 376 TVT 378
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1070-1288 |
1.03e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 53.21 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1070 KNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWK--AVNTLNEALEFANSVGYPCLLRPSYVLSGSAMNVVFSEDE 1147
Cdd:PRK08462 99 HHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1148 MKR-FL---EEATRVSQEHPVVLTKFIEGAREVEMDAVG-KEGRVIshaisehvedagvHSGDATLMLptQTISQGAIEK 1222
Cdd:PRK08462 179 LENlYLaaeSEALSAFGDGTMYMEKFINNPRHIEVQILGdKHGNVI-------------HVGERDCSL--QRRHQKLIEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1223 -----VKDATR--------KIAKAFAISGPFNVQFLVKGN-DVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGESV 1288
Cdd:PRK08462 244 spavvLDEKTRerlhetaiKAAKAIGYEGAGTFEFLLDSNlDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1107-1289 |
1.43e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 52.41 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1107 KAVNTLNEALEFANSVGYPCLLRPSYVLSGSAMNVVFSEDEMKRFLEEATRVSQ----EHPVVLTKFIEGAREVEMDAVG 1182
Cdd:PRK05586 136 GEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKaafgDDSMYIEKFIENPKHIEFQILG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1183 KE-GRVIshaiseHV--EDAGVHSGDATLM--LPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLV-KGNDVLVIEC 1256
Cdd:PRK05586 216 DNyGNVV------HLgeRDCSLQRRNQKVLeeAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEM 289
|
170 180 190
....*....|....*....|....*....|...
gi 8393186 1257 NLRASRSFPFVSKTLGVDFIDVATKVMIGESVD 1289
Cdd:PRK05586 290 NTRIQVEHPITEMITGVDLVKEQIKIAYGEKLS 322
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
220-296 |
2.99e-06 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 47.59 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 220 VVAVDCGIKN-----NVIRLLVKRGAEVHLVPWNHDFTQM-----DYDGLLIAGGPGNP---ALAQPLIQNVKKILESDR 286
Cdd:cd01653 1 VAVLLFPGFEelelaSPLDALREAGAEVDVVSPDGGPVESdvdldDYDGLILPGGPGTPddlARDEALLALLREAAAAGK 80
|
90
....*....|
gi 8393186 287 kePLFGISTG 296
Cdd:cd01653 81 --PILGICLG 88
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
220-296 |
3.25e-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: 46.81 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 220 VVAVDCGIKN-----NVIRLLVKRGAEVHLVPWNHDFTQM-----DYDGLLIAGGPGNP---ALAQPLIQNVKKILESDR 286
Cdd:cd03128 1 VAVLLFGGSEelelaSPLDALREAGAEVDVVSPDGGPVESdvdldDYDGLILPGGPGTPddlAWDEALLALLREAAAAGK 80
|
90
....*....|
gi 8393186 287 kePLFGISTG 296
Cdd:cd03128 81 --PVLGICLG 88
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
566-719 |
3.75e-06 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 51.17 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 566 AVESMEDALKAADTIGYPVMIRSAYALGGLGSGICPNKETLmdlgTKAFAMTNQ----------ILVERSVTGWKEIEYE 635
Cdd:COG4770 137 PVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEEL----EEAFESARReakaafgddrVYLEKYIERPRHIEVQ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 636 VVRDADDNCvtvcnmenvdamgVHTGD---SV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALH 704
Cdd:COG4770 213 VLADKHGNV-------------VHLGErdcSIqrrhqkVIeeAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVD 279
|
170
....*....|....*
gi 8393186 705 PtSMEYCIIEVNARL 719
Cdd:COG4770 280 A-DGNFYFLEMNTRL 293
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
566-651 |
1.03e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 49.98 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 566 AVESMEDALKAADTIGYPVMIRSAYALGGLGSGICPNKETL-------MDLGTKAFAmTNQILVERSVTGWKEIEYEVVR 638
Cdd:PRK08654 137 GIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELedaiestQSIAQSAFG-DSTVFIEKYLEKPRHIEIQILA 215
|
90
....*....|...
gi 8393186 639 DADDNCVTVCNME 651
Cdd:PRK08654 216 DKHGNVIHLGDRE 228
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
566-748 |
1.62e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 49.37 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 566 AVESMEDALKAADTIGYPVMIRSAYALGGLGSGICPNKETL---MDLGTK----AFAmTNQILVERSVTGWKEIEYEVVR 638
Cdd:PRK12833 140 VVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLaaeLPLAQReaqaAFG-DGGVYLERFIARARHIEVQILG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 639 DADDncvTVCNMENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNAR 718
Cdd:PRK12833 219 DGER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTR 295
|
170 180 190
....*....|....*....|....*....|
gi 8393186 719 LSRSSALASKATGYPLAFIAAKIALGIPLP 748
Cdd:PRK12833 296 IQVEHPVTEAITGIDLVQEMLRIADGEPLR 325
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
566-719 |
2.91e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 48.98 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 566 AVESMEDALKAADTIGYPVMIRSayALGGLGSG--ICPNKETLMDLGTKAFAMTNQ------ILVERSVTGWKEIEYEVV 637
Cdd:PRK12999 141 PIDDIEEALEFAEEIGYPIMLKA--SAGGGGRGmrIVRSEEELEEAFERAKREAKAafgndeVYLEKYVENPRHIEVQIL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 638 RDADDNCVTV----CnmenvdamgvhtgdSV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFaLHP 705
Cdd:PRK12999 219 GDKHGNVVHLyerdC--------------SVqrrhqkVVeiAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEF-LVD 283
|
170
....*....|....
gi 8393186 706 TSMEYCIIEVNARL 719
Cdd:PRK12999 284 ADGNFYFIEVNPRI 297
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
230-395 |
4.70e-05 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 46.03 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 230 NVIRLLVKRGAEVHLVPWNHDFTQMDY-----DGLLIAGGPGN--PALAQPLIQN---------------VKKILEsdRK 287
Cdd:cd01745 23 YYVDAVRKAGGLPVLLPPVDDEEDLEQylellDGLLLTGGGDVdpPLYGEEPHPElgpidperdafelalLRAALE--RG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 288 EPLFGISTGNIITGLAAGAKSYKMSMANRgqnqpvlnitnrqafitaqNHGYALDnTLPAGWKPLFVnVNDQTNEGIMHE 367
Cdd:cd01745 101 KPILGICRGMQLLNVALGGTLYQDIRVNS-------------------LHHQAIK-RLADGLRVEAR-APDGVIEAIESP 159
|
170 180 190
....*....|....*....|....*....|
gi 8393186 368 SKPF-FAVQFHPEV-SPGPTDTEYLFDSFF 395
Cdd:cd01745 160 DRPFvLGVQWHPEWlADTDPDSLKLFEAFV 189
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1107-1259 |
7.57e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 47.44 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1107 KAVNTLNEALEFANSVGYPCLLRPSYVLSGSAMNVVFSEDEMKRFLEEATRVSQ------EhpVVLTKFIEGAREVEMDA 1180
Cdd:PRK12999 140 GPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafgndE--VYLEKYVENPRHIEVQI 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1181 VG-KEGRVIshaiseH---------------VEDAgvhsgdatlmlPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQF 1244
Cdd:PRK12999 218 LGdKHGNVV------HlyerdcsvqrrhqkvVEIA-----------PAPGLSEELRERICEAAVKLARAVGYVNAGTVEF 280
|
170
....*....|....*..
gi 8393186 1245 LV--KGNDVLvIECNLR 1259
Cdd:PRK12999 281 LVdaDGNFYF-IEVNPR 296
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
1120-1184 |
8.90e-05 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 46.75 E-value: 8.90e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8393186 1120 NSVGYPCLLRPSYVLSGSAMNVVFSEDEMKRFLEEAtrVSQEHPVVLTKFIEgAREVEMDAVGKE 1184
Cdd:PRK14570 168 EVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEA--FKYDLTVVIEKFIE-AREIECSVIGNE 229
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1108-1190 |
1.00e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 46.67 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1108 AVNTLNEALEFANSVGYPCLLRPSYVLSGSAMNVVFSEDEMKRFLEEATRVSQ----EHPVVLTKFIEGAREVEMDAVGk 1183
Cdd:PRK12833 140 VVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQaafgDGGVYLERFIARARHIEVQILG- 218
|
....*..
gi 8393186 1184 EGRVISH 1190
Cdd:PRK12833 219 DGERVVH 225
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
336-395 |
1.04e-04 |
|
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: 44.83 E-value: 1.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8393186 336 NHGYALDnTLPAGWKPLFVNVNDQtNEGIMHESKPFFAVQFHPEVspgpTDTEY---LFDSFF 395
Cdd:cd01742 125 SHGDEVV-KLPEGFKVIASSDNCP-VAAIANEEKKIYGVQFHPEV----THTEKgkeILKNFL 181
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
566-619 |
1.46e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 45.95 E-value: 1.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 8393186 566 AVESMEDALKAADTIGYPVMIRSAYALGGLGSGICPNKETLMdlgtKAFAMTNQ 619
Cdd:PRK08591 137 PVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELE----KAFSMARA 186
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
1094-1253 |
1.81e-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: 45.45 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1094 AVLDELKVAQAPWKAVNTLNEALEFANSVGYPCLLRPS---Y----VLsgsamnVVFSEDEmkrfLEEATRVSQEHPVVL 1166
Cdd:COG0026 95 AFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrggYdgkgQV------VIKSAAD----LEAAWAALGGGPCIL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1167 TKFIEGAREVemdAV----GKEGRVISHAISEHVEDAGV-HsgdaTLMLPTQtISQGAIEKVKDATRKIAKAFAISGPFN 1241
Cdd:COG0026 165 EEFVPFEREL---SVivarSPDGEVATYPVVENVHRNGIlD----ESIAPAR-ISEALAAEAEEIAKRIAEALDYVGVLA 236
|
170
....*....|...
gi 8393186 1242 VQ-FLVKGNDVLV 1253
Cdd:COG0026 237 VEfFVTKDGELLV 249
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
527-648 |
1.90e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 45.86 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 527 KEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSF--AVESMEDALKAADTIGYPVMIRSAYALGGLGSGICPNKE 604
Cdd:PRK05586 96 KECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSegEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 8393186 605 TL-MDLGT-----KAFAMTNQILVERSVTGWKEIEYEVVRDADDNCVTVC 648
Cdd:PRK05586 176 ELiKAFNTakseaKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLG 225
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1107-1259 |
3.02e-04 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 45.46 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1107 KAVNTLNEALEFANSVGYPCLLRPSYVLSGSAMNVVFSEDEMKRFLEEATRVSQ------EhpVVLTKFIEGAREVEMDA 1180
Cdd:COG1038 139 GPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafgddE--VFLEKYIERPKHIEVQI 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1181 VG-KEGRVIshaiseH---------------VEDAgvhsgdatlmlPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQF 1244
Cdd:COG1038 217 LGdKHGNIV------HlferdcsvqrrhqkvVEIA-----------PAPNLDEELREAICEAAVKLAKAVGYVNAGTVEF 279
|
170
....*....|....*.
gi 8393186 1245 LV-KGNDVLVIECNLR 1259
Cdd:COG1038 280 LVdDDGNFYFIEVNPR 295
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
535-815 |
3.44e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 45.22 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 535 GTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESMEDALKAADTIGYPVMIRSAYALGGLGSGICPNKETLMDLGTKAF 614
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 615 -AMTNQILVERSVTGwKEIEYEVVRDADDNCVtvcnmenVDAMGVHTGDS---VVVA---PAQtLSNAEFQMLRRTSINV 687
Cdd:PRK02186 176 rAGTRAALVQAYVEG-DEYSVETLTVARGHQV-------LGITRKHLGPPphfVEIGhdfPAP-LSAPQRERIVRTVLRA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 688 VRHLGI-VGECNIQFALHPTSMeyCIIEVNARLSRS--SALASKATGYPLAFIAAKIALGIP----------------LP 748
Cdd:PRK02186 247 LDAVGYaFGPAHTELRVRGDTV--VIIEINPRLAGGmiPVLLEEAFGVDLLDHVIDLHLGVAafadptakrygairfvLP 324
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8393186 749 EiknvVSGK-TSACFEPSLDYMVTKIprwdldRFH-----GTSSRI-GSSMKSVGEVMAIGRTFEESFQKALRM 815
Cdd:PRK02186 325 A----RSGVlRGLLFLPDDIAARPEL------RFHplkqpGDALRLeGDFRDRIAAVVCAGDHRDSVAAAAERA 388
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
1101-1277 |
4.41e-04 |
|
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: 43.07 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1101 VAQAPWKAVN----TLNEALEFAN---SVGYPCLLRPSYVLSGSAMNVVFSEDEMKRFLEEATRvsQEHPVVLTKFIEGa 1173
Cdd:pfam07478 7 LPVVPFVTFTradwKLNPKEWCAQveeALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQ--YDEKVLVEEGIEG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1174 REVEMDAVGKEGRVISHAIsEHVEDAGVH-------SGDATLMLPTQtISQGAIEKVKDATRKIAKAFAISGPFNVQFLV 1246
Cdd:pfam07478 84 REIECAVLGNEDPEVSPVG-EIVPSGGFYdyeakyiDDSAQIVVPAD-LEEEQEEQIQELALKAYKALGCRGLARVDFFL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 8393186 1247 -KGNDVLVIECN----LRASRSFPFVSKTLGVDFID 1277
Cdd:pfam07478 162 tEDGEIVLNEVNtipgFTSISMFPKLAAAAGVSFPD 197
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
1163-1290 |
4.86e-04 |
|
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.
Pssm-ID: 434824 [Multi-domain] Cd Length: 131 Bit Score: 41.83 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1163 PVVLTKFIEGArEVEMDAVGKEGRVIShAISEHVEDAGVhsgdatlmlptQTISQ--GAIEkvkdATRKIAKAFAISGPF 1240
Cdd:pfam15632 4 PLLVMEYLPGP-EYSVDCLAGHGELIA-AVPRRKGDGGI-----------QTLEDdpELIE----AARRLAEAFGLDGLF 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 8393186 1241 NVQFLVKGNDVLVIECNLRASRSFPfVSKTLGVDFIDVATKVMIGESVDE 1290
Cdd:pfam15632 67 NVQFRYDGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLALKLLLGLETPD 115
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
233-398 |
6.36e-04 |
|
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: 42.30 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 233 RLLVKRGAEVHLVPWNHDFTQ---MDYDGLLIAGGPgNPALAQPLIQNVKKILESDRkePLFGISTGNIITGLAAGAKSY 309
Cdd:TIGR00888 16 RRLRELGVYSELVPNTTPLEEireKNPKGIILSGGP-SSVYAENAPRADEKIFELGV--PVLGICYGMQLMAKQLGGEVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 310 KMSMANRGQNQpvLNITNRQAFITAQN--------HGYALdNTLPAGWKPLFVNVNDQtNEGIMHESKPFFAVQFHPEVs 381
Cdd:TIGR00888 93 RAEKREYGKAE--LEILDEDDLFRGLPdestvwmsHGDKV-KELPEGFKVLATSDNCP-VAAMAHEEKPIYGVQFHPEV- 167
|
170 180
....*....|....*....|
gi 8393186 382 pgpTDTEY---LFDSFFSLI 398
Cdd:TIGR00888 168 ---THTEYgneLLENFVYDV 184
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
568-744 |
1.20e-03 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 43.26 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 568 ESMEDALKAADTIGYPVMIRSAYALGGLGSGICPNKETLMDL------GTKAFAMTNQILVERSVTGWKEIEYEVVRDAD 641
Cdd:PRK08463 139 ESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAfesckrEALAYFNNDEVFMEKYVVNPRHIEFQILGDNY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 642 DNCVTVCnmENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYcIIEVNARLSR 721
Cdd:PRK08463 219 GNIIHLC--ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFY-FMEMNTRIQV 295
|
170 180
....*....|....*....|...
gi 8393186 722 SSALASKATGYPLAFIAAKIALG 744
Cdd:PRK08463 296 EHGVTEEITGIDLIVRQIRIAAG 318
|
|
| PRK13526 |
PRK13526 |
glutamine amidotransferase subunit PdxT; Provisional |
220-391 |
1.29e-03 |
|
glutamine amidotransferase subunit PdxT; Provisional
Pssm-ID: 184113 [Multi-domain] Cd Length: 179 Bit Score: 41.48 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 220 VVAVDCGIKNNViRLLVKRGAEVHLVPWNHDFTQMDYdgLLIAGGPGNpALAQPLI--QNVKKILESDRKEPLFGISTGN 297
Cdd:PRK13526 7 VLAIQGGYQKHA-DMFKSLGVEVKLVKFNNDFDSIDR--LVIPGGEST-TLLNLLNkhQIFDKLYNFCSSKPVFGTCAGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 298 IITGLAAGAKSYKMSMANRgqnqpvlNITNRQAFITAQNHGYaLDNTLPAGW--KPLFVNVNDQTNEGIMHESKPFFAVQ 375
Cdd:PRK13526 83 IILSKGEGYLNLLDLEVQR-------NAYGRQVDSFVADISF-NDKNITGVFirAPKFIVVGNQVDILSKYQNSPVLLRQ 154
|
170 180
....*....|....*....|...
gi 8393186 376 -------FHPEVSPGPTDTEYLF 391
Cdd:PRK13526 155 anilvssFHPELTQDPTVHEYFL 177
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
500-717 |
1.61e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 42.35 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 500 RPDGLILGMGGQTALNCGVElfkrGVLKEYGVKVLGTSVESIMATEDRQLFSDKLneINEKIaPSFAVESMEDALKAADT 579
Cdd:PRK14569 56 KPDKCFVALHGEDGENGRVS----ALLEMLEIKHTSSSMKSSVITMDKMISKEIL--MHHRM-PTPMAKFLTDKLVAEDE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 580 IGYPVMIRSAYAlgglGSGICPNKETLMDLGTKAFAMTN---QILVERSVTGwKEIEYEVVRDADDNCVTVCNM-ENVDA 655
Cdd:PRK14569 129 ISFPVAVKPSSG----GSSIATFKVKSIQELKHAYEEASkygEVMIEQWVTG-KEITVAIVNDEVYSSVWIEPQnEFYDY 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8393186 656 MGVHTGDSVVVAPAQTLSNAEFQmLRRTSINVVRHLGIVGECNIQFaLHPTSMEYCIIEVNA 717
Cdd:PRK14569 204 ESKYSGKSIYHSPSGLCEQKELE-VRQLAKKAYDLLGCSGHARVDF-IYDDRGNFYIMEINS 263
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
362-401 |
1.65e-03 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 40.99 E-value: 1.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 8393186 362 EGIMHESKPFFAVQFHPEVSpgptDTEY---LFDSFFSLIKKG 401
Cdd:PRK00758 146 EAMKHKEKPIYGVQFHPEVA----HTEYgeeIFKNFLEICGKY 184
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
234-379 |
1.70e-03 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 41.39 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 234 LLVKRGAEVHLvpwnHDFTQMDYDGLLIAGGPGNPALAQPLIQNVKKILEsdrKEPLFGISTGNIITGLAAGAKSYKMSM 313
Cdd:PRK06774 26 VMVKRNDELQL----TDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFAD---KLPILGVCLGHQALGQAFGARVVRARQ 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8393186 314 ANRGQN-------QPVLNITNRQAFITaQNHGYALD-NTLPA-----GWKPLFVNVNDQTneGIMHESKPFFAVQFHPE 379
Cdd:PRK06774 99 VMHGKTsaichsgQGVFRGLNQPLTVT-RYHSLVIAaDSLPGcfeltAWSERGGEMDEIM--GIRHRTLPLEGVQFHPE 174
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1108-1188 |
2.21e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 42.48 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1108 AVNTLNEALEFANSVGYPCLLRPSYVLSGSAMNVVFSEDEmkrfLEEATRVSQEHP--------VVLTKFIEGAREVEMD 1179
Cdd:PRK08591 137 PVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAE----LEKAFSMARAEAkaafgnpgVYMEKYLENPRHIEIQ 212
|
90
....*....|
gi 8393186 1180 AVG-KEGRVI 1188
Cdd:PRK08591 213 VLAdGHGNAI 222
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
996-1286 |
2.73e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 42.01 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 996 AVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYF-------EELSLERILDIYHQEACNGciISVG-GQIPNN--LA 1065
Cdd:PRK07178 14 AVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSigadplaGYLNPRRLVNLAVETGCDA--LHPGyGFLSENaeLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1066 VPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVN--TLNEALEFANSVGYPCLLRPSYVLSGSAMNVVF 1143
Cdd:PRK07178 92 EICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNlaDLDEALAEAERIGYPVMLKATSGGGGRGIRRCN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 1144 SEDEMK----RFLEEATRVSQEHPVVLTKFIEGAREVEM----DAVGkegrvisHAISEHVEDAGVHSGDATL--MLPTQ 1213
Cdd:PRK07178 172 SREELEqnfpRVISEATKAFGSAEVFLEKCIVNPKHIEVqilaDSHG-------NVVHLFERDCSIQRRNQKLieIAPSP 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8393186 1214 TISQGAIEKVKDATRKIAKAFAISGPFNVQFLV-KGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGE 1286
Cdd:PRK07178 245 QLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
255-379 |
3.32e-03 |
|
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: 40.31 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 255 DYDGLLIAGGPGNPALAQ-----PLIQNVKKILESDRkePLFGISTGNIITGLAAGAK-----------SYKMSMANRGQ 318
Cdd:cd01741 46 DYDGLVILGGPMSVDEDDypwlkKLKELIRQALAAGK--PVLGICLGHQLLARALGGKvgrnpkgweigWFPVTLTEAGK 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8393186 319 NQPvLNITNRQAFITAQNHGYALDnTLPAGWKPLFVNVNDQtNEGIMHESKpFFAVQFHPE 379
Cdd:cd01741 124 ADP-LFAGLPDEFPVFHWHGDTVV-ELPPGAVLLASSEACP-NQAFRYGDR-ALGLQFHPE 180
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
566-718 |
5.57e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 41.60 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 566 AVESMEDALKAADTIGYPVMIRSayALGGLGSG--ICPNKETLMDL-------GTKAFAmTNQILVERSVTGWKEIEYEV 636
Cdd:COG1038 140 PVDDLEEALAFAEEIGYPVMLKA--AAGGGGRGmrVVRSEEELEEAfesarreAKAAFG-DDEVFLEKYIERPKHIEVQI 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393186 637 VRDADDNCVTV----CnmenvdamgvhtgdSV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALH 704
Cdd:COG1038 217 LGDKHGNIVHLferdC--------------SVqrrhqkVVeiAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVD 282
|
170
....*....|....
gi 8393186 705 PTsMEYCIIEVNAR 718
Cdd:COG1038 283 DD-GNFYFIEVNPR 295
|
|
| |
