|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
430-1488 |
0e+00 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 1531.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 430 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEvglKQADTVYFLPITPQFVTEVIKA 509
Cdd:TIGR01369 3 RTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDP---EMADKVYIEPLTPEAVEKIIEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 510 EQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAAD 589
Cdd:TIGR01369 80 ERPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 590 TIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAMT--NQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAM 667
Cdd:TIGR01369 160 EIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 668 GVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAF 747
Cdd:TIGR01369 240 GVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 748 IAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMC 827
Cdd:TIGR01369 320 VAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 828 HPSIEGFtpRLPMNKEWPsNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNS 907
Cdd:TIGR01369 400 EIGATGF--DLPDREVEP-DEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 908 ESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDVNF-DDHG 986
Cdd:TIGR01369 477 TDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 987 MMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGCIIS 1066
Cdd:TIGR01369 557 VLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1067 VGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLS 1146
Cdd:TIGR01369 637 FGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLG 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1147 GSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAGVHSGDATLMLPTQTI 1226
Cdd:TIGR01369 717 GRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTL 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1227 SQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDEkhLPT 1306
Cdd:TIGR01369 797 SAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEE--LGV 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1307 LDHPiiPADYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQSFRPRF 1385
Cdd:TIGR01369 875 GKEK--EPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGsVLLSVRDKDKEEL 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1386 LGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRR 1465
Cdd:TIGR01369 953 LDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPN-----ILDLIKNGEIELVINTTSKGAGTATDGYKIRR 1027
|
1050 1060
....*....|....*....|...
gi 1603768567 1466 TAVDSGIPLLTNFQVTKLFAEAV 1488
Cdd:TIGR01369 1028 EALDYGVPLITTLNTAEAFAEAL 1050
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
430-1502 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1418.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 430 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTN-EVglkqADTVYFLPITPQFVTEVIK 508
Cdd:PRK05294 4 RTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDpEM----ADATYIEPITPEFVEKIIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 509 AEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAA 588
Cdd:PRK05294 80 KERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 589 DTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAM--TNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDA 666
Cdd:PRK05294 160 EEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 667 MGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIV-GECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPL 745
Cdd:PRK05294 240 MGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 746 AFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALR 825
Cdd:PRK05294 320 AKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 826 MCHPSIEGFTPRL--PMNKEwpsnlDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLK 903
Cdd:PRK05294 400 SLEIGVTGLDEDLfeEESLE-----ELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 904 GlNSESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDVNFD 983
Cdd:PRK05294 475 E-NGLPLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 984 DHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGC 1063
Cdd:PRK05294 554 RKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGV 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1064 IISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSY 1143
Cdd:PRK05294 634 IVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSY 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1144 VLSGSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAV--GKDgrVISHAISEHVEDAGVHSGDATLML 1221
Cdd:PRK05294 714 VLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAIcdGED--VLIGGIMEHIEEAGVHSGDSACSL 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1222 PTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDE 1301
Cdd:PRK05294 792 PPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAE 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1302 KHLPTldhPIIPaDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQS 1380
Cdd:PRK05294 872 LGYTK---GLIP-PYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGtVFLSVRDR 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1381 FRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKfVHDN 1460
Cdd:PRK05294 948 DKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPH-----IVDLIKNGEIDLVINTPTGRQA-IRDG 1021
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....
gi 1603768567 1461 YVIRRTAVDSGIPLLTNFQVTKLFAEAVQ--KSRKVDSKSLFHY 1502
Cdd:PRK05294 1022 FSIRRAALEYKVPYITTLAGARAAVKAIEalKFGELEVRSLQEY 1065
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
439-973 |
0e+00 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 616.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 439 LGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQT-NEVglkqADTVYFLPITPQFVTEVIKAEQPDGLIL 517
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTdYDT----ADRLYFEPLTVEDVLDIIEKEKPDGVIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 518 GMGGQTALNCGVELFKRGVLKeyGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMI 597
Cdd:COG0458 77 QFGGQTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 598 RSAYALGGLGSGICPNRETLMDLSTKAFA--MTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHTGDSV 675
Cdd:COG0458 155 RPSYVLGGRGMGIVYNEEELEEYLERALKvsPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 676 VVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHptSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALG 755
Cdd:COG0458 235 CVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 756 IPLPEIKNVVSgktsacFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIegft 835
Cdd:COG0458 313 YTLDELGNDTG------FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGL---- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 836 PRLPMNKEWPSNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGlnsESMTEETL 915
Cdd:COG0458 383 PGTVLLSLVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEE---IILVINTL 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1603768567 916 KRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTY 973
Cdd:COG0458 460 LGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTY 517
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
57-411 |
4.14e-176 |
|
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 529.89 E-value: 4.14e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 57 AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTAldelglskylESNG 136
Cdd:TIGR01368 1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDA----------ESKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 137 IKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVDF------VDPNKQ- 209
Cdd:TIGR01368 71 IHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEElvekarVSPDITg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 210 -NLIAEVSTKDVKVYGK--GNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFT---KMEYDGILIAGGPGNPALAE 283
Cdd:TIGR01368 151 iNLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEeikKYNPDGIFLSNGPGDPAAVE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 284 PLIQNVRKILEsdrKEPLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDN-TLPAG-WK 361
Cdd:TIGR01368 231 PAIETIRKLLE---KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPdSLPAGdLE 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1603768567 362 PLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKK 411
Cdd:TIGR01368 308 VTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
55-409 |
2.34e-143 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 443.36 E-value: 2.34e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 55 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTtalDElglskylES 134
Cdd:PRK12564 3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---DF-------ES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 135 NGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI--------EFEGQPVDFVDP 206
Cdd:PRK12564 73 DRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIatedfdaeELLEKARAFPGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 207 NKQNLIAEVSTKDVKVYGKGNPT---KVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTKMEYDGILIAGGPGNPA 280
Cdd:PRK12564 153 LGLDLVKEVSTKEPYPWPGPGGElkyKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 281 LAEPLIQNVRKILESDRkePLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPAG 359
Cdd:PRK12564 233 ALDYAIEMIRELLEKKI--PIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDeDSLPAN 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1603768567 360 WKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLI 409
Cdd:PRK12564 311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
55-410 |
2.39e-137 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 427.13 E-value: 2.39e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 55 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTtalDElglskylES 134
Cdd:COG0505 3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDE---DF-------ES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 135 NGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVD--------FVDP 206
Cdd:COG0505 73 DRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEellekaraAPGM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 207 NKQNLIAEVSTKDVKVYG--KGNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTKMEYDGILIAGGPGNPAL 281
Cdd:COG0505 153 EGLDLVKEVSTKEPYEWTeaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATtsaEEILALNPDGVFLSNGPGDPAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 282 AEPLIQNVRKILESDRkePLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPA-G 359
Cdd:COG0505 233 LDYAIETIRELLGKGI--PIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDeDSLPAtD 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1603768567 360 WKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIK 410
Cdd:COG0505 311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
557-759 |
5.91e-104 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 329.65 E-value: 5.91e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 557 DRQLFSDKLNEINEKIAPSFA--VESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAMT------ 628
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 629 NQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMgvHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGEC 708
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1603768567 709 NIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLP 759
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
231-406 |
9.10e-97 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 308.27 E-value: 9.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 231 VVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDF---TKMEYDGILIAGGPGNPALAEPLIQNVRKILESdrKEPLFGISTG 307
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAeeiLKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGK--KIPIFGICLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 308 NLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPAGWKPLFVNVNDQTNEGIMHESKPFFAVQ 386
Cdd:cd01744 79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDpDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158
|
170 180
....*....|....*....|
gi 1603768567 387 FHPEVTPGPIDTEYLFDSFF 406
Cdd:cd01744 159 FHPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
59-194 |
3.70e-64 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.
Pssm-ID: 460017 [Multi-domain] Cd Length: 126 Bit Score: 213.34 E-value: 3.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 59 IVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDttaldelglsKYLESNGIK 138
Cdd:pfam00988 1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNP----------EDFESDKIH 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1603768567 139 VSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI 194
Cdd:pfam00988 71 VAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
55-194 |
3.28e-63 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 211.08 E-value: 3.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 55 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDttaldelglsKYLES 134
Cdd:smart01097 1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVND----------EDFES 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 135 NGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI 194
Cdd:smart01097 71 DKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
850-973 |
5.83e-55 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 186.89 E-value: 5.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 850 LRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNSESMTEETLKRAKEIGFSDKQIS 929
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1603768567 930 KCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTY 973
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1371-1486 |
1.76e-49 |
|
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.
Pssm-ID: 238711 [Multi-domain] Cd Length: 116 Bit Score: 170.94 E-value: 1.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1371 KGILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSlSSIRKLIRDGSIDLVINLP 1450
Cdd:cd01423 1 KGILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK-PSLRELLAEGKIDLVINLP 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 1603768567 1451 NNNTKFVHDN-YVIRRTAVDSGIPLLTNFQVTKLFAE 1486
Cdd:cd01423 80 SNRGKRVLDNdYVMRRAADDFAVPLITNPKCAKLFIE 116
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
430-1488 |
0e+00 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 1531.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 430 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEvglKQADTVYFLPITPQFVTEVIKA 509
Cdd:TIGR01369 3 RTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDP---EMADKVYIEPLTPEAVEKIIEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 510 EQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAAD 589
Cdd:TIGR01369 80 ERPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 590 TIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAMT--NQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAM 667
Cdd:TIGR01369 160 EIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 668 GVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAF 747
Cdd:TIGR01369 240 GVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 748 IAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMC 827
Cdd:TIGR01369 320 VAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 828 HPSIEGFtpRLPMNKEWPsNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNS 907
Cdd:TIGR01369 400 EIGATGF--DLPDREVEP-DEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 908 ESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDVNF-DDHG 986
Cdd:TIGR01369 477 TDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 987 MMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGCIIS 1066
Cdd:TIGR01369 557 VLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1067 VGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLS 1146
Cdd:TIGR01369 637 FGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLG 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1147 GSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAGVHSGDATLMLPTQTI 1226
Cdd:TIGR01369 717 GRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTL 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1227 SQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDEkhLPT 1306
Cdd:TIGR01369 797 SAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEE--LGV 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1307 LDHPiiPADYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQSFRPRF 1385
Cdd:TIGR01369 875 GKEK--EPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGsVLLSVRDKDKEEL 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1386 LGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRR 1465
Cdd:TIGR01369 953 LDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPN-----ILDLIKNGEIELVINTTSKGAGTATDGYKIRR 1027
|
1050 1060
....*....|....*....|...
gi 1603768567 1466 TAVDSGIPLLTNFQVTKLFAEAV 1488
Cdd:TIGR01369 1028 EALDYGVPLITTLNTAEAFAEAL 1050
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
430-1502 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1418.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 430 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTN-EVglkqADTVYFLPITPQFVTEVIK 508
Cdd:PRK05294 4 RTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDpEM----ADATYIEPITPEFVEKIIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 509 AEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAA 588
Cdd:PRK05294 80 KERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 589 DTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAM--TNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDA 666
Cdd:PRK05294 160 EEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 667 MGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIV-GECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPL 745
Cdd:PRK05294 240 MGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 746 AFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALR 825
Cdd:PRK05294 320 AKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 826 MCHPSIEGFTPRL--PMNKEwpsnlDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLK 903
Cdd:PRK05294 400 SLEIGVTGLDEDLfeEESLE-----ELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 904 GlNSESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDVNFD 983
Cdd:PRK05294 475 E-NGLPLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 984 DHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGC 1063
Cdd:PRK05294 554 RKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGV 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1064 IISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSY 1143
Cdd:PRK05294 634 IVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSY 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1144 VLSGSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAV--GKDgrVISHAISEHVEDAGVHSGDATLML 1221
Cdd:PRK05294 714 VLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAIcdGED--VLIGGIMEHIEEAGVHSGDSACSL 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1222 PTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDE 1301
Cdd:PRK05294 792 PPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAE 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1302 KHLPTldhPIIPaDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQS 1380
Cdd:PRK05294 872 LGYTK---GLIP-PYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGtVFLSVRDR 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1381 FRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKfVHDN 1460
Cdd:PRK05294 948 DKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPH-----IVDLIKNGEIDLVINTPTGRQA-IRDG 1021
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....
gi 1603768567 1461 YVIRRTAVDSGIPLLTNFQVTKLFAEAVQ--KSRKVDSKSLFHY 1502
Cdd:PRK05294 1022 FSIRRAALEYKVPYITTLAGARAAVKAIEalKFGELEVRSLQEY 1065
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
430-1489 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1105.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 430 RVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEvglKQADTVYFLPITPQFVTEVIKA 509
Cdd:PRK12815 4 DTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDP---APADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 510 EQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAAD 589
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 590 TIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFA--MTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAM 667
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQasPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 668 GVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAF 747
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 748 IAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRmc 827
Cdd:PRK12815 321 IAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALR-- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 828 hpSIEGFTP--RLPMNKEWPSNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGl 905
Cdd:PRK12815 399 --SLEIKRNglSLPIELSGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAE- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 906 NSESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQ-EHDVNFDD 984
Cdd:PRK12815 476 DGLDLSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGEsEAEPSSEK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 985 HGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGCI 1064
Cdd:PRK12815 556 KKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVI 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1065 ISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYV 1144
Cdd:PRK12815 636 VQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYV 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1145 LSGSAMNVVFSEDEMKKFLEEAtrVSQEHPVVLTKFVEGArEVEMDAVgKDGRVISHA-ISEHVEDAGVHSGDATLMLPT 1223
Cdd:PRK12815 716 IGGQGMAVVYDEPALEAYLAEN--ASQLYPILIDQFIDGK-EYEVDAI-SDGEDVTIPgIIEHIEQAGVHSGDSIAVLPP 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1224 QTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDEKH 1303
Cdd:PRK12815 792 QSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELG 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1304 LPTLDHPIipADYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQSFR 1382
Cdd:PRK12815 872 YPNGLWPG--SPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGtIFISVRDEDK 949
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1383 PRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAwPSQEGQNPSLSsirklIRDGSIDLVINLPNNNTKFVHDNYV 1462
Cdd:PRK12815 950 PEVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVE-KVQEGSPSLLE-----RIKQHRIVLVVNTSLSDSASEDAIK 1023
|
1050 1060
....*....|....*....|....*..
gi 1603768567 1463 IRRTAVDSGIPLLTNFQVTKLFAEAVQ 1489
Cdd:PRK12815 1024 IRDEALSTHIPVFTELETAQAFLQVLE 1050
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
414-1492 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 902.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 414 ATTITSVLPKPALVASRVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEvglKQADTV 493
Cdd:PLN02735 4 ADTVTRAWSAATKAGKRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDP---ETADRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 494 YFLPITPQFVTEVIKAEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIA 573
Cdd:PLN02735 81 YIAPMTPELVEQVIAKERPDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 574 PSFAVESIEDALKAADTIG-YPVMIRSAYALGGLGSGICPNRETLMDLSTKAFA--MTNQILVEKSVTGWKEIEYEVVRD 650
Cdd:PLN02735 161 PSGIATTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAasITSQVLVEKSLLGWKEYELEVMRD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 651 ADDNCVTVCNMENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIvgEC---NIQFALHPTSMEYCIIEVN 727
Cdd:PLN02735 241 LADNVVIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 728 ARLSRSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVG 807
Cdd:PLN02735 319 PRVSRSSALASKATGFPIAKMAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 808 EVMAIGRTFEESFQKALRMCHPSIEGFTPrlPMNKEWPSNLD-LRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDK 886
Cdd:PLN02735 399 EAMALGRTFQESFQKALRSLETGFSGWGC--AKVKELDWDWEqLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 887 WFLYKMRDILNMEKTLKGLNSESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVT 966
Cdd:PLN02735 477 WFLTQLKELVDVEQFLKSRSLSELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 967 NYLYVTYNGQEHDVNFDDHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEEL 1046
Cdd:PLN02735 557 PYMYSSYDGECESAPTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPL 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1047 SLERILDIYHQEACGGCIISVGGQIPNNLAVPLYK------------NG-VKIMGTSPLQIDRAEDRSIFSAVLDELKVA 1113
Cdd:PLN02735 637 TVEDVLNVIDLERPDGIIVQFGGQTPLKLALPIQKyldknpppsasgNGnVKIWGTSPDSIDAAEDRERFNAILNELKIE 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1114 QAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVG 1193
Cdd:PLN02735 717 QPKGGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALA 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1194 -KDGRVISHAISEHVEDAGVHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLV-KGNDVLVIECNLRA 1271
Cdd:PLN02735 797 dSEGNVVIGGIMEHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRA 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1272 SRSFPFVSKTLGVDFIDVATKVMIGenvdeKHLPTLD--HPIIPAdYVAIKAPMFSWPRLRDADPILRCEMASTGEVACF 1349
Cdd:PLN02735 877 SRTVPFVSKAIGHPLAKYASLVMSG-----KSLKDLGftEEVIPA-HVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGI 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1350 GEGIHTAFLKAMLSTGFKIPQKG-ILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAwPSQEGQn 1428
Cdd:PLN02735 951 DYEFSKAFAKAQIAAGQRLPLSGtVFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVL-KLHEGR- 1028
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1603768567 1429 pslSSIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRRTAVDSGIPLLTNFQVTKLFAEAVQKSR 1492
Cdd:PLN02735 1029 ---PHAGDMLANGQIQLMVITSSGDALDQKDGRQLRRMALAYKVPIITTVAGALATAQAVKSLK 1089
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
439-973 |
0e+00 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 616.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 439 LGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQT-NEVglkqADTVYFLPITPQFVTEVIKAEQPDGLIL 517
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTdYDT----ADRLYFEPLTVEDVLDIIEKEKPDGVIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 518 GMGGQTALNCGVELFKRGVLKeyGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMI 597
Cdd:COG0458 77 QFGGQTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 598 RSAYALGGLGSGICPNRETLMDLSTKAFA--MTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHTGDSV 675
Cdd:COG0458 155 RPSYVLGGRGMGIVYNEEELEEYLERALKvsPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 676 VVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHptSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALG 755
Cdd:COG0458 235 CVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 756 IPLPEIKNVVSgktsacFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIegft 835
Cdd:COG0458 313 YTLDELGNDTG------FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGL---- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 836 PRLPMNKEWPSNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGlnsESMTEETL 915
Cdd:COG0458 383 PGTVLLSLVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEE---IILVINTL 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1603768567 916 KRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTY 973
Cdd:COG0458 460 LGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTY 517
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
990-1506 |
1.93e-177 |
|
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: 540.62 E-value: 1.93e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 990 LGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGCIISVGG 1069
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1070 QIPNNLAVPLYKN----GVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVL 1145
Cdd:COG0458 81 QTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1146 SGSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVG-KDGRVISHAISEHVEDAGVHSGDATLMLPTQ 1224
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRdGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1225 TISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDEKHL 1304
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1305 PTLDHPIIpaDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPR 1384
Cdd:COG0458 321 DTGFEPTL--DYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLLSLVADDDKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1385 FLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNTKFVHDNYVIR 1464
Cdd:COG0458 399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPI-----IVDEIELEEIILVINTLLGAKSLGDSDGIIR 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1603768567 1465 RTAVDSGIPLLTNFQVTK-LFAEAVQKSRKVDSKSLFHYRQYS 1506
Cdd:COG0458 474 RALAAKVPYVTTLAAAAAaALAIKAVETEAGEFEEATAYYYST 516
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
57-411 |
4.14e-176 |
|
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 529.89 E-value: 4.14e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 57 AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTAldelglskylESNG 136
Cdd:TIGR01368 1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDA----------ESKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 137 IKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVDF------VDPNKQ- 209
Cdd:TIGR01368 71 IHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEElvekarVSPDITg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 210 -NLIAEVSTKDVKVYGK--GNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFT---KMEYDGILIAGGPGNPALAE 283
Cdd:TIGR01368 151 iNLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEeikKYNPDGIFLSNGPGDPAAVE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 284 PLIQNVRKILEsdrKEPLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDN-TLPAG-WK 361
Cdd:TIGR01368 231 PAIETIRKLLE---KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPdSLPAGdLE 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1603768567 362 PLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKK 411
Cdd:TIGR01368 308 VTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
55-409 |
2.34e-143 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 443.36 E-value: 2.34e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 55 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTtalDElglskylES 134
Cdd:PRK12564 3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---DF-------ES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 135 NGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI--------EFEGQPVDFVDP 206
Cdd:PRK12564 73 DRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIatedfdaeELLEKARAFPGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 207 NKQNLIAEVSTKDVKVYGKGNPT---KVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTKMEYDGILIAGGPGNPA 280
Cdd:PRK12564 153 LGLDLVKEVSTKEPYPWPGPGGElkyKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 281 LAEPLIQNVRKILESDRkePLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPAG 359
Cdd:PRK12564 233 ALDYAIEMIRELLEKKI--PIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDeDSLPAN 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1603768567 360 WKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLI 409
Cdd:PRK12564 311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
55-410 |
2.39e-137 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 427.13 E-value: 2.39e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 55 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTtalDElglskylES 134
Cdd:COG0505 3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDE---DF-------ES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 135 NGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVD--------FVDP 206
Cdd:COG0505 73 DRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEellekaraAPGM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 207 NKQNLIAEVSTKDVKVYG--KGNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTKMEYDGILIAGGPGNPAL 281
Cdd:COG0505 153 EGLDLVKEVSTKEPYEWTeaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATtsaEEILALNPDGVFLSNGPGDPAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 282 AEPLIQNVRKILESDRkePLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPA-G 359
Cdd:COG0505 233 LDYAIETIRELLGKGI--PIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDeDSLPAtD 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1603768567 360 WKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIK 410
Cdd:COG0505 311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
57-413 |
2.42e-107 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 345.34 E-value: 2.42e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 57 AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDttaldelglsKYLESNG 136
Cdd:PRK12838 3 AYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINA----------DDYESKQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 137 IKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI------EFEGQPVDFVDPnkQN 210
Cdd:PRK12838 73 PQVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASItttddaHAFDQIKALVLP--KN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 211 LIAEVSTKDVKVYGKGNPTkVVAVDCGIKNNVIRLLVKRGAEVHLVPWNhdfTKMEY------DGILIAGGPGNPALAEP 284
Cdd:PRK12838 151 VVAQVSTKEPYTYGNGGKH-VALIDFGYKKSILRSLSKRGCKVTVLPYD---TSLEEiknlnpDGIVLSNGPGDPKELQP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 285 LIQNVRKILESdrkEPLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYAL--DNTLPAGWKP 362
Cdd:PRK12838 227 YLPEIKKLISS---YPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVdeDSLDGTPLSV 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1603768567 363 LFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKKGK 413
Cdd:PRK12838 304 RFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKAR 354
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
557-759 |
5.91e-104 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 329.65 E-value: 5.91e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 557 DRQLFSDKLNEINEKIAPSFA--VESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAMT------ 628
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 629 NQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMgvHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGEC 708
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1603768567 709 NIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLP 759
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
231-406 |
9.10e-97 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 308.27 E-value: 9.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 231 VVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDF---TKMEYDGILIAGGPGNPALAEPLIQNVRKILESdrKEPLFGISTG 307
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAeeiLKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGK--KIPIFGICLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 308 NLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPAGWKPLFVNVNDQTNEGIMHESKPFFAVQ 386
Cdd:cd01744 79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDpDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158
|
170 180
....*....|....*....|
gi 1603768567 387 FHPEVTPGPIDTEYLFDSFF 406
Cdd:cd01744 159 FHPEASPGPHDTEYLFDEFL 178
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
57-413 |
2.12e-81 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 273.21 E-value: 2.12e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 57 AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGapdtTALDElglskyLESNG 136
Cdd:CHL00197 7 AILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTG----INLED------IESVK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 137 IKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVDFVDPNKQ------- 209
Cdd:CHL00197 77 IQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSYLRAKIKesphmps 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 210 -NLIAEVSTKDVKVYGK----------------GNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTKMEY---DG 269
Cdd:CHL00197 157 sDLIPRVTTSSYYEWDEkshpsfyladnkrphsSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSyqpDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 270 ILIAGGPGNPALAEPLIQNVRKILesDRKEPLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLniTNKQAFITAQNHG 349
Cdd:CHL00197 237 ILLSNGPGDPSAIHYGIKTVKKLL--KYNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSG--LNQQVEITSQNHG 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1603768567 350 YALDntLPAGWKPLF----VNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKKGK 413
Cdd:CHL00197 313 FAVN--LESLAKNKFyithFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSK 378
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
27-402 |
7.05e-69 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 238.34 E-value: 7.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 27 TGFGFTNVTAHQKWKFSRPGIRLLSVKAQT-------------------AHIVLEDGTKMKGYSFGHPSSVAGEVVFNTG 87
Cdd:PLN02771 8 LGFVLPTSLSSQPSFDRRGGVRVSVIRCSSspltsdgagvverpwktsdARLVLEDGSVWKAKSFGARGTQVGEVVFNTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 88 LGGYPEAITDPAYKGQILTMANPIIGNGGA-PDttalDElglskylESNGIKVSGLLVLDYSKDYNHWLATKSLGQWLQE 166
Cdd:PLN02771 88 LTGYQEILTDPSYAGQFVLMTNPHIGNTGVnFD----DE-------ESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 167 EKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVD--------FVDPNKQNLIAEVSTK-------------DVKVYGK 225
Cdd:PLN02771 157 RNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDeellkmsrSWDIVGIDLISGVSCKspyewvdktnpewDFNTNSR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 226 -GNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWN---HDFTKMEYDGILIAGGPGNPALAEPLIQNVRKILEsdrKEPL 301
Cdd:PLN02771 237 dGESYHVIAYDFGIKHNILRRLASYGCKITVVPSTwpaSEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLG---KVPV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 302 FGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALD-NTLPAGWKPLFVNVNDQTNEGIMHESK 380
Cdd:PLN02771 314 FGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDpASLPEGVEVTHVNLNDGSCAGLAFPAL 393
|
410 420
....*....|....*....|..
gi 1603768567 381 PFFAVQFHPEVTPGPIDTEYLF 402
Cdd:PLN02771 394 NVMSLQYHPEASPGPHDSDNAF 415
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
59-194 |
3.70e-64 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.
Pssm-ID: 460017 [Multi-domain] Cd Length: 126 Bit Score: 213.34 E-value: 3.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 59 IVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDttaldelglsKYLESNGIK 138
Cdd:pfam00988 1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNP----------EDFESDKIH 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1603768567 139 VSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI 194
Cdd:pfam00988 71 VAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
55-194 |
3.28e-63 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 211.08 E-value: 3.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 55 QTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDttaldelglsKYLES 134
Cdd:smart01097 1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVND----------EDFES 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 135 NGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKI 194
Cdd:smart01097 71 DKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
850-973 |
5.83e-55 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 186.89 E-value: 5.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 850 LRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNSESMTEETLKRAKEIGFSDKQIS 929
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1603768567 930 KCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTY 973
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
232-406 |
6.50e-55 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 189.37 E-value: 6.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 232 VAVDCG--IKNNVIRLLVKRGAEVHLVPWNHDFT---KMEYDGILIAGGPGNPALAEPLIQNVRKILEsdRKEPLFGIST 306
Cdd:pfam00117 1 LLIDNGdsFTYNLARALRELGVEVTVVPNDTPAEeilEENPDGIILSGGPGSPGAAGGAIEAIREARE--LKIPILGICL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 307 GNLITGLAAGAKTYKMSM-ANRGQNQPVLNITN------KQAFITAQNHGYALDN-TLPAGWKPLFVNVNDQTNEGIMHE 378
Cdd:pfam00117 79 GHQLLALAFGGKVVKAKKfGHHGKNSPVGDDGCglfyglPNVFIVRRYHSYAVDPdTLPDGLEVTATSENDGTIMGIRHK 158
|
170 180
....*....|....*....|....*...
gi 1603768567 379 SKPFFAVQFHPEVTPGPIDTEYLFDSFF 406
Cdd:pfam00117 159 KLPIFGVQFHPESILTPHGPEILFNFFI 186
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1371-1486 |
1.76e-49 |
|
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.
Pssm-ID: 238711 [Multi-domain] Cd Length: 116 Bit Score: 170.94 E-value: 1.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1371 KGILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSlSSIRKLIRDGSIDLVINLP 1450
Cdd:cd01423 1 KGILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK-PSLRELLAEGKIDLVINLP 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 1603768567 1451 NNNTKFVHDN-YVIRRTAVDSGIPLLTNFQVTKLFAE 1486
Cdd:cd01423 80 SNRGKRVLDNdYVMRRAADDFAVPLITNPKCAKLFIE 116
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
852-930 |
6.00e-30 |
|
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 460695 Cd Length: 79 Bit Score: 114.01 E-value: 6.00e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1603768567 852 KELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGlNSESMTEETLKRAKEIGFSDKQISK 930
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKE-AGLDLDAELLREAKRLGFSDRQIAK 78
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
1099-1300 |
1.30e-27 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 112.01 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1099 DRSIFSAVLDELKVAQAPWKA--VNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVS----QE 1172
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1173 HPVVLTKFVEGAREVEMDAVG-KDGRVIsHAISEHVEDAgVHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPF 1251
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRdAHGNCI-TVCNRECSDQ-RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1603768567 1252 NVQFLV--KGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVD 1300
Cdd:pfam02786 159 TVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1384-1476 |
7.38e-25 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 99.87 E-value: 7.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1384 RFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPNNNTKFVHDNYVI 1463
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEGRPGGRVQIGDLIKNGEIDLVINTLYPFKATVHDGYAI 80
|
90
....*....|...
gi 1603768567 1464 RRTAVDSGIPLLT 1476
Cdd:pfam02142 81 RRAAENIDIPGPT 93
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
1088-1297 |
1.05e-22 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 99.56 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1088 GTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYvLSGSA-MNVVFSEDEMKKFLE-- 1164
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPAD-GAGSRgVRVVRDEEELEAALAea 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1165 --EATRVSQEHPVVLTKFVEGaREVEMDAVGKDGRVISHAISEHVEDA--GVHSGDatlMLPTQtISQGAIEKVKDATRK 1240
Cdd:COG0439 122 raEAKAGSPNGEVLVEEFLEG-REYSVEGLVRDGEVVVCSITRKHQKPpyFVELGH---EAPSP-LPEELRAEIGELVAR 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1603768567 1241 IAKAFAIS-GPFNVQFLVKGNDVLV-IECNLRAS--RSFPFVSKTLGVDFIDVATKVMIGE 1297
Cdd:COG0439 197 ALRALGYRrGAFHTEFLLTPDGEPYlIEINARLGgeHIPPLTELATGVDLVREQIRLALGE 257
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
546-757 |
1.28e-16 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 81.46 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 546 GTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLmdlsTKAF 625
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEL----EAAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 626 AMTNQ----------ILVEKSVTGwKEIEYEVVrdADDNCVTVCNM---ENVDAMGVHTGDsvvVAPAQtLSNAEFQMLR 692
Cdd:COG0439 119 AEARAeakagspngeVLVEEFLEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIG 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1603768567 693 RTSINVVRHLGIV-GECNIQFALHPtSMEYCIIEVNARLS--RSSALASKATGYPLAFIAAKIALGIP 757
Cdd:COG0439 192 ELVARALRALGYRrGAFHTEFLLTP-DGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
1382-1477 |
5.57e-16 |
|
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.
Pssm-ID: 238712 [Multi-domain] Cd Length: 110 Bit Score: 75.21 E-value: 5.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1382 RPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNpslssIRKLIRDGSIDLVINLPNNNtKFVHDNY 1461
Cdd:cd01424 12 KPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPN-----IVDLIKNGEIQLVINTPSGK-RAIRDGF 85
|
90
....*....|....*.
gi 1603768567 1462 VIRRTAVDSGIPLLTN 1477
Cdd:cd01424 86 SIRRAALEYKVPYFTT 101
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1384-1476 |
1.13e-15 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 73.66 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1384 RFLGVAEQLHNEGFKLFATEATSDWLNANNVP--ATPVAWPSqEGQNpslsSIRKLIRDGSIDLVINLPNNNTK-FVHDN 1460
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPvvKTLHPKVH-GGIP----QILDLIKNGEIDLVINTLYPFEAqAHEDG 75
|
90
....*....|....*.
gi 1603768567 1461 YVIRRTAVDSGIPLLT 1476
Cdd:smart00851 76 YSIRRAAENIDIPGPT 91
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
435-761 |
1.40e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 70.68 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 435 KVLILGSGGlsigqagefdysGSQAVKAMKEE----NVKTVLMNPNIAsvqtnevGLKQADTVYFLP-ITP----QFVTE 505
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSllkgRVIGADISELAP-------ALYFADKFYVVPkVTDpnyiDRLLD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 506 VIKAEQPDGLILGMGgqtalncgVELFK----RGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESI 581
Cdd:PRK12767 64 ICKKEKIDLLIPLID--------PELPLlaqnRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 582 EDALKA--ADTIGYPVMIRSAYALGGLGSGICPNRETLMDLstkaFAMTNQILVEKSVTGwKEIEYEVVRDADDNCVTVC 659
Cdd:PRK12767 136 EDFKAAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELEFL----LEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 660 NMENVDAMGVHTGDSVVVapaqtlsnaEFQMLRRTSINVVRHLGIVGECNIQFALhpTSMEYCIIEVNARLSRSSALASK 739
Cdd:PRK12767 211 PRKRIEVRAGETSKGVTV---------KDPELFKLAERLAEALGARGPLNIQCFV--TDGEPYLFEINPRFGGGYPLSYM 279
|
330 340
....*....|....*....|...
gi 1603768567 740 ATG-YPlAFIAAKIALGIPLPEI 761
Cdd:PRK12767 280 AGAnEP-DWIIRNLLGGENEPII 301
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
574-843 |
1.16e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 68.90 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 574 PSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLmdlsTKAFAMTNQ----------ILVEKSVTGWKEI 643
Cdd:PRK06111 134 ITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQEL----TKAFESNKKraanffgngeMYIEKYIEDPRHI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 644 EYEVVRDADDNCvtvcnmenvdamgVHTGD---SV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQF 712
Cdd:PRK06111 210 EIQLLADTHGNT-------------VYLWErecSVqrrhqkVIeeAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEF 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 713 ALHPTSMEYcIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLP----EIKnvVSGKTSAC---------FEPSldy 779
Cdd:PRK06111 277 LVDEQKNFY-FLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSftqdDIK--RSGHAIEVriyaedpktFFPS--- 350
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1603768567 780 mVTKIPRWDLDRfhGTSSRIGSSMKS-----------VGEVMAIGRTFEESFQK---ALRMCHpsIEGFTPRLPMNKE 843
Cdd:PRK06111 351 -PGKITDLTLPG--GEGVRHDHAVENgvtvtpfydpmIAKLIAHGETREEAISRlhdALEELK--VEGIKTNIPLLLQ 423
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
244-393 |
7.26e-11 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 63.81 E-value: 7.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 244 RLLVKRGAEVH--------LVPWNHDFTkmEYDGILIAGGPGNP----ALAEPLIQNVRKILESDRkePLFGISTGNLIT 311
Cdd:COG0518 20 RRLREAGIELDvlrvyageILPYDPDLE--DPDGLILSGGPMSVydedPWLEDEPALIREAFELGK--PVLGICYGAQLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 312 GLAAGAKTYKMSMANRGQnQPVlNITNKQA--------FITAQNHGYALDnTLPAGWKPLFVNVNDQtNEGIMHEsKPFF 383
Cdd:COG0518 96 AHALGGKVEPGPGREIGW-APV-ELTEADPlfaglpdeFTVWMSHGDTVT-ELPEGAEVLASSDNCP-NQAFRYG-RRVY 170
|
170
....*....|
gi 1603768567 384 AVQFHPEVTP 393
Cdd:COG0518 171 GVQFHPEVTH 180
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
539-759 |
1.19e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 65.89 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 539 EYGVKVLGTSVESImatedRQLfSDKLNEINEKIAPSFAV--------ESIEDALKAADTIGYPVMIRSAYALGGLGSGI 610
Cdd:PRK07178 96 ERGIKFIGPSAEVI-----RRM-GDKTEARRAMIKAGVPVtpgsegnlADLDEALAEAERIGYPVMLKATSGGGGRGIRR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 611 CPNRETL-------MDLSTKAFAMTnQILVEKSVTGWKEIEYEVVRDADDNCVTV----CNMENVDAMGVHtgdsvvVAP 679
Cdd:PRK07178 170 CNSREELeqnfprvISEATKAFGSA-EVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQRRNQKLIE------IAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 680 AQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYcIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLP 759
Cdd:PRK07178 243 SPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVY-FMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLS 321
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
241-390 |
1.01e-09 |
|
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.
Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 59.42 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 241 NVIRLLVKRGAEVHlVPWNHDFTKMEYDG-----ILIAGGPGNPALAEpliQNVRKILESDRKEPLFGISTGNLITGLAA 315
Cdd:TIGR00566 14 NLVQYFCELGAEVV-VKRNDSLTLQEIEAllpllIVISPGPCTPNEAG---ISLEAIRHFAGKLPILGVCLGHQAMGQAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 316 GAKtykMSMANRGQNQPVLNITNKQAFITAqnhgyALDNTLPAG-WKPLFVN---------VNDQTNE-----GIMHESK 380
Cdd:TIGR00566 90 GGD---VVRANTVMHGKTSEIEHNGAGIFR-----GLFNPLTATrYHSLVVEpetlptcfpVTAWEEEnieimAIRHRDL 161
|
170
....*....|
gi 1603768567 381 PFFAVQFHPE 390
Cdd:TIGR00566 162 PLEGVQFHPE 171
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
240-390 |
1.28e-09 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 59.09 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 240 NNVIRLLVKRGAEVHLVPwNHDFT-----KMEYDGILIAGGPGNPALAEPLIQnVRKILESDRkePLFGISTGNLITGLA 314
Cdd:cd01743 12 YNLVQYLRELGAEVVVVR-NDEITleeleLLNPDAIVISPGPGHPEDAGISLE-IIRALAGKV--PILGVCLGHQAIAEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 315 AGAKTYKMSMANRGQ------NQPVLNITNKQAFITAQNHGYALD-NTLPAGWKplfvnVNDQTNEG-IM---HESKPFF 383
Cdd:cd01743 88 FGGKVVRAPEPMHGKtseihhDGSGLFKGLPQPFTVGRYHSLVVDpDPLPDLLE-----VTASTEDGvIMalrHRDLPIY 162
|
....*..
gi 1603768567 384 AVQFHPE 390
Cdd:cd01743 163 GVQFHPE 169
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
501-759 |
4.36e-09 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 60.33 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 501 QFVTEVIKAEQPDgLILGMGgqtalNCGVELF--KRGVLKEYgVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAV 578
Cdd:COG3919 66 DALLELAERHGPD-VLIPTG-----DEYVELLsrHRDELEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 579 ESIEDALKAADTIGYPVMIRSAY--------ALGGLGSGICPNRETLMDLSTKAFAMTNQILVEKSVTGWKEIEY--EVV 648
Cdd:COG3919 139 DSADDLDALAEDLGFPVVVKPADsvgydelsFPGKKKVFYVDDREELLALLRRIAAAGYELIVQEYIPGDDGEMRglTAY 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 649 RDADDNCVTVC----NMENVDAMGVHTGdsvvvapAQTLSNAEfqmLRRTSINVVRHLGIVGECNIQFALHPTSMEYCII 724
Cdd:COG3919 219 VDRDGEVVATFtgrkLRHYPPAGGNSAA-------RESVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYKLI 288
|
250 260 270
....*....|....*....|....*....|....*
gi 1603768567 725 EVNARLSRSSALASKAtGYPLAFIAAKIALGIPLP 759
Cdd:COG3919 289 EINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLE 322
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
536-760 |
4.88e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 60.53 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 536 VLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSF--AVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPN 613
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 614 RETLMD--LSTKAFAMT----NQILVEKSVTGWKEIEYEVVRDADDNCVTV----CNMENvdamgvHTGDSVVVAPAQTL 683
Cdd:PRK08462 176 ESDLENlyLAAESEALSafgdGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVL 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1603768567 684 SNAEFQMLRRTSINVVRHLGIVGECNIQFaLHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLPE 760
Cdd:PRK08462 250 DEKTRERLHETAIKAAKAIGYEGAGTFEF-LLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPS 325
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1081-1301 |
7.62e-08 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 56.05 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1081 KNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALE--FAKSVDYPCLLRPsYVLSGSA-MNVVFSED 1157
Cdd:PRK12767 93 EIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAalAKGELQFPLFVKP-RDGSASIgVFKVNDKE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1158 EMKKFLEEATrvsqehPVVLTKFVEGaREVEMDA-VGKDGRVISHAISEHVEdagVHSGDATlmlptQTISqGAIEKVKD 1236
Cdd:PRK12767 172 ELEFLLEYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGETS-----KGVT-VKDPELFK 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1603768567 1237 ATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFvSKTLGVDFIDVATKVMIGENVDE 1301
Cdd:PRK12767 236 LAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL-SYMAGANEPDWIIRNLLGGENEP 299
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
577-730 |
3.66e-07 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 54.64 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 577 AVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDL--STKAFAMTN----QILVEKSVTGWKEIEYEVVRD 650
Cdd:COG4770 137 PVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAfeSARREAKAAfgddRVYLEKYIERPRHIEVQVLAD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 651 ADDNCvtvcnmenvdamgVHTGD---SV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPtSM 719
Cdd:COG4770 217 KHGNV-------------VHLGErdcSIqrrhqkVIeeAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDA-DG 282
|
170
....*....|.
gi 1603768567 720 EYCIIEVNARL 730
Cdd:COG4770 283 NFYFLEMNTRL 293
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1007-1199 |
5.08e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 54.22 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1007 AVSSIRTLRQLGKKTVVVncnpetvstdFDECDK-----LYFEE-------------LSLERILDIyhQEACGGCIISVG 1068
Cdd:PRK08654 14 AIRVMRACRELGIKTVAV----------YSEADKnalfvKYADEaypigpappsksyLNIERIIDV--AKKAGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1069 -GQIPNN--LAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPW--KAVNTLNEALEFAKSVDYPCLLRPSY 1143
Cdd:PRK08654 82 yGFLAENpeFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGteEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1603768567 1144 VLSGSAMNVVFSEDEMKKFLEEATRVSQ----EHPVVLTKFVEGAREVEMDAVG-KDGRVI 1199
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQsafgDSTVFIEKYLEKPRHIEIQILAdKHGNVI 222
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
577-662 |
8.66e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 53.45 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 577 AVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDL--STKAFAMTN----QILVEKSVTGWKEIEYEVVRD 650
Cdd:PRK08654 137 GIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAieSTQSIAQSAfgdsTVFIEKYLEKPRHIEIQILAD 216
|
90
....*....|..
gi 1603768567 651 ADDNCVTVCNME 662
Cdd:PRK08654 217 KHGNVIHLGDRE 228
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
231-307 |
1.48e-06 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 47.97 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 231 VVAVDCGIKN-----NVIRLLVKRGAEVHLVPWNHDFTKME-----YDGILIAGGPGNP---ALAEPLIQNVRKILESDR 297
Cdd:cd03128 1 VAVLLFGGSEelelaSPLDALREAGAEVDVVSPDGGPVESDvdlddYDGLILPGGPGTPddlAWDEALLALLREAAAAGK 80
|
90
....*....|
gi 1603768567 298 kePLFGISTG 307
Cdd:cd03128 81 --PVLGICLG 88
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
231-307 |
1.56e-06 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 48.36 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 231 VVAVDCGIKN-----NVIRLLVKRGAEVHLVPWNHDFTKME-----YDGILIAGGPGNP---ALAEPLIQNVRKILESDR 297
Cdd:cd01653 1 VAVLLFPGFEelelaSPLDALREAGAEVDVVSPDGGPVESDvdlddYDGLILPGGPGTPddlARDEALLALLREAAAAGK 80
|
90
....*....|
gi 1603768567 298 kePLFGISTG 307
Cdd:cd01653 81 --PILGICLG 88
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1118-1300 |
6.83e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 50.48 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1118 KAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVSQ----EHPVVLTKFVEGAREVEMDAVG 1193
Cdd:PRK05586 136 GEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKaafgDDSMYIEKFIENPKHIEFQILG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1194 KD-GRVIshaiseHV--EDAGVHSGDATLM--LPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLV-KGNDVLVIEC 1267
Cdd:PRK05586 216 DNyGNVV------HLgeRDCSLQRRNQKVLeeAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEM 289
|
170 180 190
....*....|....*....|....*....|...
gi 1603768567 1268 NLRASRSFPFVSKTLGVDFIDVATKVMIGENVD 1300
Cdd:PRK05586 290 NTRIQVEHPITEMITGVDLVKEQIKIAYGEKLS 322
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1081-1299 |
7.25e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 50.51 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1081 KNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWK--AVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDE 1158
Cdd:PRK08462 99 HHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1159 MKK-FL---EEATRVSQEHPVVLTKFVEGAREVEMDAVG-KDGRVIshaisehvedagvHSGDATLMLptQTISQGAIEK 1233
Cdd:PRK08462 179 LENlYLaaeSEALSAFGDGTMYMEKFINNPRHIEVQILGdKHGNVI-------------HVGERDCSL--QRRHQKLIEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1234 -----VKDATR--------KIAKAFAISGPFNVQFLVKGN-DVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENV 1299
Cdd:PRK08462 244 spavvLDEKTRerlhetaiKAAKAIGYEGAGTFEFLLDSNlDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
577-730 |
8.06e-06 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 50.91 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 577 AVESIEDALKAADTIGYPVMIRSayALGGLGSG--ICPNRETLMDLSTKAFAMTNQ------ILVEKSVTGWKEIEYEVV 648
Cdd:PRK12999 141 PIDDIEEALEFAEEIGYPIMLKA--SAGGGGRGmrIVRSEEELEEAFERAKREAKAafgndeVYLEKYVENPRHIEVQIL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 649 RDADDNCVTV----CnmenvdamgvhtgdSV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFaLHP 716
Cdd:PRK12999 219 GDKHGNVVHLyerdC--------------SVqrrhqkVVeiAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEF-LVD 283
|
170
....*....|....
gi 1603768567 717 TSMEYCIIEVNARL 730
Cdd:PRK12999 284 ADGNFYFIEVNPRI 297
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
244-406 |
1.07e-05 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 47.53 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 244 RLLVKR----GAEVHLVPWN---HDFTKMEYDGILIAGGPgNPALAEPLIQNVRKILESdrKEPLFGISTGN-LITgLAA 315
Cdd:cd01742 12 HLIARRvrelGVYSEILPNTtplEEIKLKNPKGIILSGGP-SSVYEEDAPRVDPEIFEL--GVPVLGICYGMqLIA-KAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 316 GAKTYKMSmaNRGQNQPVLNITNKQAFITAQ--------NHGYALDnTLPAGWKPLFVNVNDQtNEGIMHESKPFFAVQF 387
Cdd:cd01742 88 GGKVERGD--KREYGKAEIEIDDSSPLFEGLpdeqtvwmSHGDEVV-KLPEGFKVIASSDNCP-VAAIANEEKKIYGVQF 163
|
170 180
....*....|....*....|..
gi 1603768567 388 HPEVTpgpiDTEY---LFDSFF 406
Cdd:cd01742 164 HPEVT----HTEKgkeILKNFL 181
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
247-390 |
1.46e-05 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 47.74 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 247 VKRGAEVHLVpwNHDFTKMEYDGILIAGGPGNPALAEPLIQNVRKIleSDRKEPLFGISTGNLITGLAAGA--------- 317
Cdd:PRK07765 29 VWRNDDPRLA--DEAAVAAQFDGVLLSPGPGTPERAGASIDMVRAC--AAAGTPLLGVCLGHQAIGVAFGAtvdrapell 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 318 --KTYKMSMANRG--QNQPvlnitnkQAFITAQNHGYA-LDNTLPAGwkplfVNVNDQTNEGI----MHESKPFFAVQFH 388
Cdd:PRK07765 105 hgKTSSVHHTGVGvlAGLP-------DPFTATRYHSLTiLPETLPAE-----LEVTARTDSGVimavRHRELPIHGVQFH 172
|
..
gi 1603768567 389 PE 390
Cdd:PRK07765 173 PE 174
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
241-406 |
2.63e-05 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 46.41 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 241 NVIRLLVKRGAEVHLVPWNHDFTKMEY-----DGILIAGGPGN--PALAEPLIQN---------------VRKILEsdRK 298
Cdd:cd01745 23 YYVDAVRKAGGLPVLLPPVDDEEDLEQylellDGLLLTGGGDVdpPLYGEEPHPElgpidperdafelalLRAALE--RG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 299 EPLFGISTGNLITGLAAGAKTYKMSMANRgqnqpvlnitnkqafitaqNHGYALDnTLPAGWKPLFVnVNDQTNEGIMHE 378
Cdd:cd01745 101 KPILGICRGMQLLNVALGGTLYQDIRVNS-------------------LHHQAIK-RLADGLRVEAR-APDGVIEAIESP 159
|
170 180 190
....*....|....*....|....*....|
gi 1603768567 379 SKPF-FAVQFHPEVTP-GPIDTEYLFDSFF 406
Cdd:cd01745 160 DRPFvLGVQWHPEWLAdTDPDSLKLFEAFV 189
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
577-759 |
3.93e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 47.83 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 577 AVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETL---MDLSTK----AFAmTNQILVEKSVTGWKEIEYEVVR 649
Cdd:PRK12833 140 VVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLaaeLPLAQReaqaAFG-DGGVYLERFIARARHIEVQILG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 650 DADDncvTVCNMENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNAR 729
Cdd:PRK12833 219 DGER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTR 295
|
170 180 190
....*....|....*....|....*....|
gi 1603768567 730 LSRSSALASKATGYPLAFIAAKIALGIPLP 759
Cdd:PRK12833 296 IQVEHPVTEAITGIDLVQEMLRIADGEPLR 325
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
1105-1264 |
9.00e-05 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 46.61 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1105 AVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPS---Y----VLsgsamnVVFSEDEMKKFLEEATRVsqehPVVL 1177
Cdd:COG0026 95 AFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrggYdgkgQV------VIKSAADLEAAWAALGGG----PCIL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1178 TKFVEGAREVemdAV----GKDGRVISHAISEHVEDAGV-HsgdaTLMLPTQtISQGAIEKVKDATRKIAKAFAISGPFN 1252
Cdd:COG0026 165 EEFVPFEREL---SVivarSPDGEVATYPVVENVHRNGIlD----ESIAPAR-ISEALAAEAEEIAKRIAEALDYVGVLA 236
|
170
....*....|...
gi 1603768567 1253 VQ-FLVKGNDVLV 1264
Cdd:COG0026 237 VEfFVTKDGELLV 249
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
577-730 |
9.50e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 46.72 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 577 AVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMdlstKAFAMTNQ----------ILVEKSVTGWKEIEYE 646
Cdd:PRK08591 137 PVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELE----KAFSMARAeakaafgnpgVYMEKYLENPRHIEIQ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 647 VVRDADDNcvtvcnmenvdamGVHTGD---SV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFaLH 715
Cdd:PRK08591 213 VLADGHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEF-LY 278
|
170
....*....|....*
gi 1603768567 716 PTSMEYCIIEVNARL 730
Cdd:PRK08591 279 EKNGEFYFIEMNTRI 293
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
244-392 |
9.85e-05 |
|
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 45.00 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 244 RLLVKRGAEVHLVPWN---HDFTKMEYDGILIAGGPgNPALAEPLIQNVRKILESDRkePLFGISTGNLITGLAAGAKTY 320
Cdd:TIGR00888 16 RRLRELGVYSELVPNTtplEEIREKNPKGIILSGGP-SSVYAENAPRADEKIFELGV--PVLGICYGMQLMAKQLGGEVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 321 KMSMANRGQNQpvLNITNKQAFITAQN--------HGYALdNTLPAGWKPLFVNVNDQtNEGIMHESKPFFAVQFHPEVT 392
Cdd:TIGR00888 93 RAEKREYGKAE--LEILDEDDLFRGLPdestvwmsHGDKV-KELPEGFKVLATSDNCP-VAAMAHEEKPIYGVQFHPEVT 168
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
538-659 |
2.57e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 45.47 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 538 KEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSF--AVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRE 615
Cdd:PRK05586 96 KECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSegEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1603768567 616 TLMDL--STKAFAMTN----QILVEKSVTGWKEIEYEVVRDADDNCVTVC 659
Cdd:PRK05586 176 ELIKAfnTAKSEAKAAfgddSMYIEKFIENPKHIEFQILGDNYGNVVHLG 225
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
1131-1195 |
3.34e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 44.82 E-value: 3.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1603768567 1131 KSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEAtrVSQEHPVVLTKFVEgAREVEMDAVGKD 1195
Cdd:PRK14570 168 EVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEA--FKYDLTVVIEKFIE-AREIECSVIGNE 229
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
577-729 |
3.64e-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: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 577 AVESIEDALKAADTIGYPVMIRSayALGGLGSG--ICPNRETLMDL-------STKAFAmTNQILVEKSVTGWKEIEYEV 647
Cdd:COG1038 140 PVDDLEEALAFAEEIGYPVMLKA--AAGGGGRGmrVVRSEEELEEAfesarreAKAAFG-DDEVFLEKYIERPKHIEVQI 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 648 VRDADDNCVTV----CnmenvdamgvhtgdSV------VV--APAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALH 715
Cdd:COG1038 217 LGDKHGNIVHLferdC--------------SVqrrhqkVVeiAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVD 282
|
170
....*....|....
gi 1603768567 716 PTsMEYCIIEVNAR 729
Cdd:COG1038 283 DD-GNFYFIEVNPR 295
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
1174-1322 |
4.16e-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: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1174 PVVLTKFVEGArEVEMDAVGKDGRVIShAISEHVEDAGVhsgdatlmlptQTISQ--GAIEkvkdATRKIAKAFAISGPF 1251
Cdd:pfam15632 4 PLLVMEYLPGP-EYSVDCLAGHGELIA-AVPRRKGDGGI-----------QTLEDdpELIE----AARRLAEAFGLDGLF 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1603768567 1252 NVQFLVKGNDVLVIECNLRASRSFPfVSKTLGVDFIDVATKVMIGENVDEkhlptLDHPIIPADYVAIKAP 1322
Cdd:pfam15632 67 NVQFRYDGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLALKLLLGLETPD-----PVEPRLGLRVREIEKV 131
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
546-826 |
4.59e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 44.84 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 546 GTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAF 625
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 626 -AMTNQILVEKSVTGwKEIEYEVVRDADDNCVtvcnmenVDAMGVHTGDS---VVVA---PAQtLSNAEFQMLRRTSINV 698
Cdd:PRK02186 176 rAGTRAALVQAYVEG-DEYSVETLTVARGHQV-------LGITRKHLGPPphfVEIGhdfPAP-LSAPQRERIVRTVLRA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 699 VRHLGI-VGECNIQFALHPTSMeyCIIEVNARLSRS--SALASKATGYPLAFIAAKIALGIP----------------LP 759
Cdd:PRK02186 247 LDAVGYaFGPAHTELRVRGDTV--VIIEINPRLAGGmiPVLLEEAFGVDLLDHVIDLHLGVAafadptakrygairfvLP 324
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1603768567 760 EiknvVSGK-TSACFEPSLDYMVTKIprwdldRFH-----GTSSRI-GSSMKSVGEVMAIGRTFEESFQKALRM 826
Cdd:PRK02186 325 A----RSGVlRGLLFLPDDIAARPEL------RFHplkqpGDALRLeGDFRDRIAAVVCAGDHRDSVAAAAERA 388
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
579-755 |
8.43e-04 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 43.65 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 579 ESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDL------STKAFAMTNQILVEKSVTGWKEIEYEVVRDAD 652
Cdd:PRK08463 139 ESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAfesckrEALAYFNNDEVFMEKYVVNPRHIEFQILGDNY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 653 DNCVTVCnmENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYcIIEVNARLSR 732
Cdd:PRK08463 219 GNIIHLC--ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFY-FMEMNTRIQV 295
|
170 180
....*....|....*....|...
gi 1603768567 733 SSALASKATGYPLAFIAAKIALG 755
Cdd:PRK08463 296 EHGVTEEITGIDLIVRQIRIAAG 318
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
266-390 |
8.57e-04 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 42.23 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 266 EYDGILIAGGPGNPALAE-----PLIQNVRKILESDRkePLFGISTGNLITGLAAGAK-----------TYKMSMANRGQ 329
Cdd:cd01741 46 DYDGLVILGGPMSVDEDDypwlkKLKELIRQALAAGK--PVLGICLGHQLLARALGGKvgrnpkgweigWFPVTLTEAGK 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1603768567 330 NQPvLNITNKQAFITAQNHGYALDnTLPAGWKPLFVNVNDQtNEGIMHESKpFFAVQFHPE 390
Cdd:cd01741 124 ADP-LFAGLPDEFPVFHWHGDTVV-ELPPGAVLLASSEACP-NQAFRYGDR-ALGLQFHPE 180
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
245-390 |
1.41e-03 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 41.39 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 245 LLVKRGAEVHLvpwnHDFTKMEYDGILIAGGPGNPALAEPLIQNVRKILEsdrKEPLFGISTGNLITGLAAGAKTYKMSM 324
Cdd:PRK06774 26 VMVKRNDELQL----TDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFAD---KLPILGVCLGHQALGQAFGARVVRARQ 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1603768567 325 ANRGQN-------QPVLNITNKQAFITaQNHGYALD-NTLPA-----GWKPLFVNVNDQTneGIMHESKPFFAVQFHPE 390
Cdd:PRK06774 99 VMHGKTsaichsgQGVFRGLNQPLTVT-RYHSLVIAaDSLPGcfeltAWSERGGEMDEIM--GIRHRTLPLEGVQFHPE 174
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
511-728 |
2.04e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 41.97 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 511 QPDGLILGMGGQTALNCGVElfkrGVLKEYGVKVLGTSVESIMATEDRQLFSDKLneINEKIaPSFAVESIEDALKAADT 590
Cdd:PRK14569 56 KPDKCFVALHGEDGENGRVS----ALLEMLEIKHTSSSMKSSVITMDKMISKEIL--MHHRM-PTPMAKFLTDKLVAEDE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 591 IGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAfAMTNQILVEKSVTGwKEIEYEVVRDADDNCVTVCNM-ENVDAMGV 669
Cdd:PRK14569 129 ISFPVAVKPSSGGSSIATFKVKSIQELKHAYEEA-SKYGEVMIEQWVTG-KEITVAIVNDEVYSSVWIEPQnEFYDYESK 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1603768567 670 HTGDSVVVAPAQTLSNAEFQmLRRTSINVVRHLGIVGECNIQFaLHPTSMEYCIIEVNA 728
Cdd:PRK14569 207 YSGKSIYHSPSGLCEQKELE-VRQLAKKAYDLLGCSGHARVDF-IYDDRGNFYIMEINS 263
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
1112-1288 |
2.19e-03 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1112 VAQAPWKAVN----TLNEALEFAKSVD---YPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRvsQEHPVVLTKFVEGa 1184
Cdd:pfam07478 7 LPVVPFVTFTradwKLNPKEWCAQVEEalgYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQ--YDEKVLVEEGIEG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1185 REVEMdAVGKDGRVISHAISEHVEDAGVH-------SGDATLMLPTQtISQGAIEKVKDATRKIAKAFAISGPFNVQFLV 1257
Cdd:pfam07478 84 REIEC-AVLGNEDPEVSPVGEIVPSGGFYdyeakyiDDSAQIVVPAD-LEEEQEEQIQELALKAYKALGCRGLARVDFFL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1603768567 1258 -KGNDVLVIECN----LRASRSFPFVSKTLGVDFID 1288
Cdd:pfam07478 162 tEDGEIVLNEVNtipgFTSISMFPKLAAAAGVSFPD 197
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1118-1270 |
3.08e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 42.37 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1118 KAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVSQ------EhpVVLTKFVEGAREVEMDA 1191
Cdd:COG1038 139 GPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafgddE--VFLEKYIERPKHIEVQI 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1192 VG-KDGRVIshaiseH---------------VEDAgvhsgdatlmlPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQF 1255
Cdd:COG1038 217 LGdKHGNIV------HlferdcsvqrrhqkvVEIA-----------PAPNLDEELREAICEAAVKLAKAVGYVNAGTVEF 279
|
170
....*....|....*.
gi 1603768567 1256 LV-KGNDVLVIECNLR 1270
Cdd:COG1038 280 LVdDDGNFYFIEVNPR 295
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
241-390 |
4.99e-03 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 41.24 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 241 NVIRLLVKRGAEVHLVPWNHDFT-----KMEYDGILIAGGPGNPALAEPLIQNVRKIlesDRKEPLFGISTGNLITGLAA 315
Cdd:PRK14607 14 NIYQYIGELGPEEIEVVRNDEITieeieALNPSHIVISPGPGRPEEAGISVEVIRHF---SGKVPILGVCLGHQAIGYAF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 316 GAKTYKMSMANRGQNQPV------LNITNKQAFITAQNHGYALD-NTLPAGWKPLfVNVNDQTNEGIMHESKPFFAVQFH 388
Cdd:PRK14607 91 GGKIVHAKRILHGKTSPIdhngkgLFRGIPNPTVATRYHSLVVEeASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFH 169
|
..
gi 1603768567 389 PE 390
Cdd:PRK14607 170 PE 171
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
1372-1480 |
5.53e-03 |
|
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 238297 [Multi-domain] Cd Length: 112 Bit Score: 38.26 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1372 GILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAwpsqEGQNPSLSSIRKLIRD-GSIDLVINLP 1450
Cdd:cd00532 1 GVFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVS----KRHEDGEPTVDAAIAEkGKFDVVINLR 76
|
90 100 110
....*....|....*....|....*....|..
gi 1603768567 1451 N--NNTKFVHDNYVIRRTAVDSGIPLLTNFQV 1480
Cdd:cd00532 77 DprRDRCTDEDGTALLRLARLYKIPVTTPNAT 108
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1119-1201 |
5.62e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 40.89 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768567 1119 AVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVSQ----EHPVVLTKFVEGAREVEMDAVGk 1194
Cdd:PRK12833 140 VVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQaafgDGGVYLERFIARARHIEVQILG- 218
|
....*..
gi 1603768567 1195 DGRVISH 1201
Cdd:PRK12833 219 DGERVVH 225
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
373-412 |
8.59e-03 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 39.06 E-value: 8.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1603768567 373 EGIMHESKPFFAVQFHPEVTpgpiDTEY---LFDSFFSLIKKG 412
Cdd:PRK00758 146 EAMKHKEKPIYGVQFHPEVA----HTEYgeeIFKNFLEICGKY 184
|
|
|