|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
7-610 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1075.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 7 KEILLKAKKLGFSDKQIANLLGMDEIEVRDLRKKLNIIPLYKMVDTCAAEFEAKTPYYYSAYEtfvykEQDESNPSDRKK 86
Cdd:PRK05294 482 AELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYE-----EECESNPSDRKK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 87 VIIIGSGPIRIGQGIEFDYSSVHAVLALKEMGIEAIIVNNNPETVSTDYDTSDKLYFEPITFEDVLNIAEREKERGellg 166
Cdd:PRK05294 557 VLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKG---- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 167 VIVQFGGQTAINLAMKLKKAGVNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTKEEALKIAKRIGYPVLVRPS 246
Cdd:PRK05294 633 VIVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPS 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 247 YVLGGRAMQIVYSEEELIEYMEEAVRVSEEHPVLIDKFLEDAIELDVDAVCDGESVLIGAIMEHIEEAGVHSGDSATVIP 326
Cdd:PRK05294 713 YVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACSLP 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 327 PQTLPKEIIDTVIDYTAKLARALNIVGLLNVQYAVKDGVVYVLEANPRASRTVPYVSKSVGIPLAKLATKIMLGKKLEEL 406
Cdd:PRK05294 793 PQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAEL 872
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 407 inDYDVEKVaekvwiakPKYVSIKESVFPFLKLPGVDPVLGPEMKSTGEAIGIDKDFGKAYYKAQLSANMELPIFGNVFI 486
Cdd:PRK05294 873 --GYTKGLI--------PPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFL 942
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 487 SVRDKDKKQIVDVAKKLHELGFTIYATEGTAKVLRENNIPAILVKKISESPnDNVIKLMRDGKIHLIINTSSGKKAKSDG 566
Cdd:PRK05294 943 SVRDRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGR-PHIVDLIKNGEIDLVINTPTGRQAIRDG 1021
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 506213642 567 YYIRRAAVDLGIPYITTIPGAKATVKAIEAVKNGELDVYSLDEL 610
Cdd:PRK05294 1022 FSIRRAALEYKVPYITTLAGARAAVKAIEALKFGELEVRSLQEY 1065
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
1-594 |
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: 858.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 1 MDMEKL----KEILLKAKKLGFSDKQIANLLGMDEIEVRDLRKKLNIIPLYKMVDTCAAEFEAKTPYYYSAYEtfvyKEQ 76
Cdd:TIGR01369 471 LEEVKLtdldPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYE----GER 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 77 DESNPSDRKKVIIIGSGPIRIGQGIEFDYSSVHAVLALKEMGIEAIIVNNNPETVSTDYDTSDKLYFEPITFEDVLNIAE 156
Cdd:TIGR01369 547 DDVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIE 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 157 REKERGellgVIVQFGGQTAINLAMKLKKAGVNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTKEEALKIAKR 236
Cdd:TIGR01369 627 LEKPEG----VIVQFGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASE 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 237 IGYPVLVRPSYVLGGRAMQIVYSEEELIEYMEEAVRVSEEHPVLIDKFLEDAIELDVDAVCDGESVLIGAIMEHIEEAGV 316
Cdd:TIGR01369 703 IGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGV 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 317 HSGDSATVIPPQTLPKEIIDTVIDYTAKLARALNIVGLLNVQYAVKDGVVYVLEANPRASRTVPYVSKSVGIPLAKLATK 396
Cdd:TIGR01369 783 HSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVR 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 397 IMLGKKLEELinDYDVEKvaekvwiaKPKYVSIKESVFPFLKLPGVDPVLGPEMKSTGEAIGIDKDFGKAYYKAQLSANM 476
Cdd:TIGR01369 863 VMLGKKLEEL--GVGKEK--------EPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGN 932
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 477 ELPIFGNVFISVRDKDKKQIVDVAKKLHELGFTIYATEGTAKVLRENNIPAILVKKISESPnDNVIKLMRDGKIHLIINT 556
Cdd:TIGR01369 933 RIPKKGSVLLSVRDKDKEELLDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGR-PNILDLIKNGEIELVINT 1011
|
570 580 590
....*....|....*....|....*....|....*....
gi 506213642 557 SS-GKKAKSDGYYIRRAAVDLGIPYITTIPGAKATVKAI 594
Cdd:TIGR01369 1012 TSkGAGTATDGYKIRREALDYGVPLITTLNTAEAFAEAL 1050
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
7-609 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 754.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 7 KEILLKAKKLGFSDKQIANLLGMDEIEVRDLRKKLNIIPLYKMVDTCAAEFEAKTPYYYSAYEtfvykEQDESNPS-DRK 85
Cdd:PRK12815 482 ADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYF-----GESEAEPSsEKK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 86 KVIIIGSGPIRIGQGIEFDYSSVHAVLALKEMGIEAIIVNNNPETVSTDYDTSDKLYFEPITFEDVLNIAEREKergeLL 165
Cdd:PRK12815 557 KVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAEN----IK 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 166 GVIVQFGGQTAINLAMKLKKAGVNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTKEEALKIAKRIGYPVLVRP 245
Cdd:PRK12815 633 GVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRP 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 246 SYVLGGRAMQIVYSEEELIEYMEEAVrvSEEHPVLIDKFLeDAIELDVDAVCDGESVLIGAIMEHIEEAGVHSGDSATVI 325
Cdd:PRK12815 713 SYVIGGQGMAVVYDEPALEAYLAENA--SQLYPILIDQFI-DGKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVL 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 326 PPQTLPKEIIDTVIDYTAKLARALNIVGLLNVQYAVKDGVVYVLEANPRASRTVPYVSKSVGIPLAKLATKIMLGKKLEE 405
Cdd:PRK12815 790 PPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAE 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 406 LindydveKVAEKVWIAkPKYVSIKESVFPFLKLPGVDPVLGPEMKSTGEAIGIDKDFGKAYYKAQLSANMELPIFGNVF 485
Cdd:PRK12815 870 L-------GYPNGLWPG-SPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIF 941
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 486 ISVRDKDKKQIVDVAKKLHELGFTIYATEGTAKVLRENNIPAILVKKISESPNdNVIKLMRDGKIHLIINTSSGKKAKSD 565
Cdd:PRK12815 942 ISVRDEDKPEVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGSP-SLLERIKQHRIVLVVNTSLSDSASED 1020
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 506213642 566 GYYIRRAAVDLGIPYITTIPGAKATVKAIEAVKNGELDVYSLDE 609
Cdd:PRK12815 1021 AIKIRDEALSTHIPVFTELETAQAFLQVLESLALTTQPIQELQE 1064
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
90-613 |
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: 742.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 90 IGSGPIRIGQGIEFDYSSVHAVLALKEMGIEAIIVNNNPETVSTDYDTSDKLYFEPITFEDVLNIAEREKERGellgVIV 169
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDG----VIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 170 QFGGQTAINLAMKLKKA----GVNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTKEEALKIAKRIGYPVLVRP 245
Cdd:COG0458 77 QFGGQTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 246 SYVLGGRAMQIVYSEEELIEYMEEAVRVSEEHPVLIDKFLEDAIELDVDAVCDGES-VLIGAIMEHIEEAGVHSGDSATV 324
Cdd:COG0458 157 SYVLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDnVIIVGIMEHIEPAGVHSGDSICV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 325 IPPQTLPKEIIDTVIDYTAKLARALNIVGLLNVQYAVKDGVVYVLEANPRASRTVPYVSKSVGIPLAKLATKIMLGKKLE 404
Cdd:COG0458 237 APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 405 ELINDYDVEKVaekvwiakPKYVSIKESVFPFLKLPGVDPVLGPEMKSTGEAIGIDKDFGKAYYKAQLSANMELPifGNV 484
Cdd:COG0458 317 ELGNDTGFEPT--------LDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP--GTV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 485 FIS-VRDKDKKQIVDVAKKLHELGFTIYATEGTAKVLRENNIPAILVKKISEsPNDNVIKLMRDGKIHLIINTSSGKKAK 563
Cdd:COG0458 387 LLSlVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSE-GRPIIVDEIELEEIILVINTLLGAKSL 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 506213642 564 SDGYYIRRAAVDLGIPYITTIPGAKATVKAIEAVKNGELDVYSLDELDAS 613
Cdd:COG0458 466 GDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYS 515
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
7-607 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 718.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 7 KEILLKAKKLGFSDKQIANLLGMDEIEVRDLRKKLNIIPLYKMVDTCAAEFEAKTPYYYSAYETfvykeQDESNPSDRKK 86
Cdd:PLN02735 502 KDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDG-----ECESAPTNKKK 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 87 VIIIGSGPIRIGQGIEFDYSSVHAVLALKEMGIEAIIVNNNPETVSTDYDTSDKLYFEPITFEDVLNIAEREKERGellg 166
Cdd:PLN02735 577 VLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDG---- 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 167 VIVQFGGQTAINLAMKLKKA-------------GVNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTKEEALKI 233
Cdd:PLN02735 653 IIVQFGGQTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAI 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 234 AKRIGYPVLVRPSYVLGGRAMQIVYSEEELIEYMEEAVRVSEEHPVLIDKFLEDAIELDVDAVCDGE-SVLIGAIMEHIE 312
Cdd:PLN02735 733 AKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEgNVVIGGIMEHIE 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 313 EAGVHSGDSATVIPPQTLPKEIIDTVIDYTAKLARALNIVGLLNVQYAV-KDGVVYVLEANPRASRTVPYVSKSVGIPLA 391
Cdd:PLN02735 813 QAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRASRTVPFVSKAIGHPLA 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 392 KLATKIMLGKKLEELindydveKVAEKVwiaKPKYVSIKESVFPFLKLPGVDPVLGPEMKSTGEAIGIDKDFGKAYYKAQ 471
Cdd:PLN02735 893 KYASLVMSGKSLKDL-------GFTEEV---IPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQ 962
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 472 LSANMELPIFGNVFISVRDKDKKQIVDVAKKLHELGFTIYATEGTAKVLRENNIPAILVKKISESpNDNVIKLMRDGKIH 551
Cdd:PLN02735 963 IAAGQRLPLSGTVFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEG-RPHAGDMLANGQIQ 1041
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 506213642 552 LIINTSSGKKAKS-DGYYIRRAAVDLGIPYITTIPGAKATVKAIEAVKNGELDVYSL 607
Cdd:PLN02735 1042 LMVITSSGDALDQkDGRQLRRMALAYKVPIITTVAGALATAQAVKSLKECPIEMIAL 1098
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
82-470 |
2.63e-103 |
|
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: 336.59 E-value: 2.63e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 82 SDRKKVIIIGSGPIRIGQGIEFDYSSVHAVLALKEMGIEAIIVNNNPETVSTDYDTSDKLYFEPITFEDVLNIAEREKER 161
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 162 GELLGvivqFGGQTAINLAMKLKKAG------VNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTKEEALKIAK 235
Cdd:TIGR01369 84 AILPT----FGGQTALNLAVELEESGvlekygVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 236 RIGYPVLVRPSYVLGGRAMQIVYSEEELIEYMEEAVRVSEEHPVLIDKFLEDAIELDVDAVCDG-ESVLIGAIMEHIEEA 314
Cdd:TIGR01369 160 EIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSnDNCITVCNMENFDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 315 GVHSGDSATVIPPQTLPKEIIDTVIDYTAKLARALNIVGLLNVQYAV--KDGVVYVLEANPRASRTVPYVSKSVGIPLAK 392
Cdd:TIGR01369 240 GVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALnpDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506213642 393 LATKIMLGKKLEELINdyDVEKVAEKVWIAKPKYVSIKESVFPFLKLPGVDPVLGPEMKSTGEAIGIDKDFGKAYYKA 470
Cdd:TIGR01369 320 VAAKLAVGYTLDELKN--PVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKA 395
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
83-497 |
1.59e-97 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 321.28 E-value: 1.59e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 83 DRKKVIIIGSGPIRIGQGIEFDYSSVHAVLALKEMGIEAIIVNNNPETVSTDYDTSDKLYFEPITFEDVLNIAEREKERG 162
Cdd:PRK05294 6 DIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 163 ELLGvivqFGGQTAINLAMKLKKAG------VNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTKEEALKIAKR 236
Cdd:PRK05294 86 ILPT----MGGQTALNLAVELAESGvlekygVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 237 IGYPVLVRPSYVLGGRAMQIVYSEEELIEYMEEAVRVSEEHPVLIDKFL----EdaIELDV--DA------VCDgesvli 304
Cdd:PRK05294 162 IGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLlgwkE--YEYEVmrDKndnciiVCS------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 305 gaiMEHIEEAGVHSGDSATVIPPQTLPKEIIDTVIDYTAKLARALNIV-GLLNVQYAV--KDGVVYVLEANPRASRTVPY 381
Cdd:PRK05294 234 ---IENIDPMGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALnpKDGRYIVIEMNPRVSRSSAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 382 VSKSVGIPLAKLATKIMLGKKLEELIN--------------DYDVEKVaekvwiakPKyvsikesvFPFLKLPGVDPVLG 447
Cdd:PRK05294 311 ASKATGYPIAKVAAKLAVGYTLDEIKNditgktpasfepslDYVVTKI--------PR--------FAFEKFPGADRRLG 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 506213642 448 PEMKSTGEAIGIDKDFGKAYYKAQLSanMELPIFGNVFISVRDKDKKQIV 497
Cdd:PRK05294 375 TQMKSVGEVMAIGRTFEESLQKALRS--LEIGVTGLDEDLFEEESLEELR 422
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
82-508 |
2.10e-94 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 312.67 E-value: 2.10e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 82 SDRKKVIIIGSGPIRIGQGIEFDYSSVHAVLALKEMGIEAIIVNNNPETVSTDYDTSDKLYFEPITFEDVLNIAEREKER 161
Cdd:PRK12815 5 TDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 162 gellGVIVQFGGQTAINLAMKLKKAG------VNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTKEEALKIAK 235
Cdd:PRK12815 85 ----ALLATLGGQTALNLAVKLHEDGileqygVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 236 RIGYPVLVRPSYVLGGRAMQIVYSEEELIEYMEEAVRVSEEHPVLIDK----FLEdaIELDVDAVCDGESVLIGAiMEHI 311
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEEsiagWKE--IEYEVMRDRNGNCITVCN-MENI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 312 EEAGVHSGDSATVIPPQTLPKEIIDTVIDYTAKLARALNIVGLLNVQYAVK--DGVVYVLEANPRASRTVPYVSKSVGIP 389
Cdd:PRK12815 238 DPVGIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDpkSKQYYLIEVNPRVSRSSALASKATGYP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 390 LAKLATKIMLGKKLEELINDYDVEKVA--EKVWiakpKYVSIKESVFPFLKLPGVDPVLGPEMKSTGEAIGIDKDFGKAY 467
Cdd:PRK12815 318 IAKIAAKLAVGYTLNELKNPVTGLTYAsfEPAL----DYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAF 393
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 506213642 468 YKAQLSanMELPIFG-NVFISVRDKDKKQIVDVAKKLHELGF 508
Cdd:PRK12815 394 QKALRS--LEIKRNGlSLPIELSGKSDEELLQDLRHPDDRRL 433
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
82-470 |
3.09e-73 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 254.70 E-value: 3.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 82 SDRKKVIIIGSGPIRIGQGIEFDYSSVHAVLALKEMGIEAIIVNNNPETVSTDYDTSDKLYFEPITFEDVLNIAEREKER 161
Cdd:PLN02735 21 TDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 162 gellGVIVQFGGQTAINLAMK------LKKAGVNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTKEEALKIAK 235
Cdd:PLN02735 101 ----ALLPTMGGQTALNLAVAlaesgiLEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 236 RIG-YPVLVRPSYVLGGRAMQIVYSEEELIEYMEEAVRVSEEHPVLIDKFLEDAIELDVDAVCD-GESVLIGAIMEHIEE 313
Cdd:PLN02735 177 DIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDlADNVVIICSIENIDP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 314 AGVHSGDSATVIPPQTLPKEIIDTVIDYTAKLARALNI-VGLLNVQYAV--KDGVVYVLEANPRASRTVPYVSKSVGIPL 390
Cdd:PLN02735 257 MGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVeCGGSNVQFAVnpVDGEVMIIEMNPRVSRSSALASKATGFPI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 391 AKLATKIMLGKKLEELINDYDVEKVAEkvwiAKPK--YVSIKESVFPFLKLPGVDPVLGPEMKSTGEAIGIDKDFGKAYY 468
Cdd:PLN02735 337 AKMAAKLSVGYTLDQIPNDITLKTPAS----FEPSidYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQ 412
|
..
gi 506213642 469 KA 470
Cdd:PLN02735 413 KA 414
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
482-592 |
6.70e-50 |
|
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: 168.43 E-value: 6.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 482 GNVFISVRDKDKKQIVDVAKKLHELGFTIYATEGTAKVLRENNIPAILVKKISE-SPndNVIKLMRDGKIHLIINTSSGK 560
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEgRP--NIVDLIKNGEIQLVINTPSGK 78
|
90 100 110
....*....|....*....|....*....|..
gi 506213642 561 KAKSDGYYIRRAAVDLGIPYITTIPGAKATVK 592
Cdd:cd01424 79 RAIRDGFSIRRAALEYKVPYFTTLDTARAAVE 110
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
203-404 |
1.32e-36 |
|
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: 135.90 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 203 DREEFSKLLKKLNIPQAEGGTAF--TKEEALKIAKRIGYPVLVRPSYVLGGRAMQIVYSEEELIEYMEEAVRVS----EE 276
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 277 HPVLIDKFLEDAIELDVDAVCDGE-SVLIGAIMEHIEEagVHSGDSATVIPPQTLPKEIIDTVIDYTAKLARALNIVGLL 355
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHgNCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506213642 356 NVQYAV--KDGVVYVLEANPRASRTVPYVSKSVGIPLAKLATKIMLGKKLE 404
Cdd:pfam02786 159 TVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
7-68 |
9.37e-34 |
|
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: 124.87 E-value: 9.37e-34
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506213642 7 KEILLKAKKLGFSDKQIANLLGMDEIEVRDLRKKLNIIPLYKMVDTCAAEFEAKTPYYYSAY 68
Cdd:smart01096 63 ADLLRKAKRLGFSDRQIAKLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
496-582 |
2.74e-27 |
|
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: 105.65 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 496 IVDVAKKLHELGFTIYATEGTAKVLRENNIPAI-LVKKISESPND---NVIKLMRDGKIHLIINTSSGKKAK-SDGYYIR 570
Cdd:pfam02142 2 LVELAKALVELGFELLATGGTAKFLREAGIPVTeVVEKTGEGRPGgrvQIGDLIKNGEIDLVINTLYPFKATvHDGYAIR 81
|
90
....*....|..
gi 506213642 571 RAAVDLGIPYIT 582
Cdd:pfam02142 82 RAAENIDIPGPT 93
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
496-582 |
8.86e-26 |
|
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: 101.40 E-value: 8.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 496 IVDVAKKLHELGFTIYATEGTAKVLRENNIPAI--LVKKISESPnDNVIKLMRDGKIHLIINTSSG--KKAKSDGYYIRR 571
Cdd:smart00851 2 LVEFAKRLAELGFELLATGGTAKFLREAGLPVVktLHPKVHGGI-PQILDLIKNGEIDLVINTLYPfeAQAHEDGYSIRR 80
|
90
....*....|.
gi 506213642 572 AAVDLGIPYIT 582
Cdd:smart00851 81 AAENIDIPGPT 91
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
483-589 |
7.49e-21 |
|
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: 88.13 E-value: 7.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 483 NVFISVRDKDKKQIVDVAKKLHELGFTIYATEGTAKVLRENNIPAILVKKISESPNDNVIKL---MRDGKIHLIIN-TSS 558
Cdd:cd01423 2 GILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDKPSLrelLAEGKIDLVINlPSN 81
|
90 100 110
....*....|....*....|....*....|..
gi 506213642 559 GKKAKSDGYYI-RRAAVDLGIPYITTIPGAKA 589
Cdd:cd01423 82 RGKRVLDNDYVmRRAADDFAVPLITNPKCAKL 113
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
192-402 |
1.37e-18 |
|
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: 86.08 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 192 GTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTKEEALKIAKRIGYPVLVRPSYVLGGRAMQIVYS----EEELIEYM 267
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDeeelEAALAEAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 268 EEAVRVSEEHPVLIDKFLE-DAIELDVdAVCDGESVLIGAIMEHIEEA-GVHSGDSAtvipPQTLPKEIIDTVIDYTAKL 345
Cdd:COG0439 123 AEAKAGSPNGEVLVEEFLEgREYSVEG-LVRDGEVVVCSITRKHQKPPyFVELGHEA----PSPLPEELRAEIGELVARA 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506213642 346 ARALNIV-GLLNVQYAV-KDGVVYVLEANPRAS--RTVPYVSKSVGIPLAKLATKIMLGKK 402
Cdd:COG0439 198 LRALGYRrGAFHTEFLLtPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
484-590 |
3.14e-14 |
|
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: 69.08 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 484 VFISVRDKDKKQIVDVAKKLHELGFTIYATEGTAKVLRENNIPAILVKKISESPNDNVIKLMRD-GKIHLIINTSSG--- 559
Cdd:cd00532 2 VFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEDGEPTVDAAIAEkGKFDVVINLRDPrrd 81
|
90 100 110
....*....|....*....|....*....|.
gi 506213642 560 KKAKSDGYYIRRAAVDLGIPYITTIPGAKAT 590
Cdd:cd00532 82 RCTDEDGTALLRLARLYKIPVTTPNATAMFV 112
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
182-411 |
1.50e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 69.14 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 182 KLKKAGVNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTKEEALKI--AKRIGYPVLVRPsyvLGGRAMQIVYS 259
Cdd:PRK12767 90 RFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAAlaKGELQFPLFVKP---RDGSASIGVFK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 260 EEELIEYMEEAVRVSEehpVLIDKFLEDaIELDVDAVCDGESVLIGAI-MEHIEeagVHSGDSATVIppqTLPKEIIdtv 338
Cdd:PRK12767 167 VNDKEELEFLLEYVPN---LIIQEFIEG-QEYTVDVLCDLNGEVISIVpRKRIE---VRAGETSKGV---TVKDPEL--- 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506213642 339 IDYTAKLARALNIVGLLNVQYAVKDGVVYVLEANPRASRTVPyVSKSVGIPLAKLATKIMLGKKLEELINDYD 411
Cdd:PRK12767 234 FKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYP-LSYMAGANEPDWIIRNLLGGENEPIIGEYK 305
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
184-404 |
1.39e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 63.58 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 184 KKAGVNILGTTPENINAAEDREEFSKLLKKLNIPQAEG--GTAFTKEEALKIAKRIGYPVLVRPSYVLGGRAMQIVYSEE 261
Cdd:PRK05586 96 KECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGseGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 262 ELIEYMEEAVRVSE----EHPVLIDKFLEDAIELDVDAVCD--GESVLIG----AIMEH----IEEAgvhsgdsatviPP 327
Cdd:PRK05586 176 ELIKAFNTAKSEAKaafgDDSMYIEKFIENPKHIEFQILGDnyGNVVHLGerdcSLQRRnqkvLEEA-----------PS 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506213642 328 QTLPKEIIDTVIDYTAKLARALNIVGLLNVQYAV-KDGVVYVLEANPRASRTVPYVSKSVGIPLAKLATKIMLGKKLE 404
Cdd:PRK05586 245 PVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLS 322
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
486-535 |
3.09e-10 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 62.80 E-value: 3.09e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 506213642 486 ISVRDKDkkQIVDVAKKLHELGFTIYATEGTAKVLRENNIPailVKKISE 535
Cdd:PRK00881 9 ISVSDKT--GIVEFAKALVELGVEILSTGGTAKLLAEAGIP---VTEVSD 53
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
486-535 |
1.12e-09 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 61.19 E-value: 1.12e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 506213642 486 ISVRDKDKkqIVDVAKKLHELGFTIYATEGTAKVLRENNIPailVKKISE 535
Cdd:COG0138 8 ISVSDKTG--LVEFARALVELGVEIISTGGTAKALREAGIP---VTEVSE 52
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
179-404 |
3.42e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 59.61 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 179 LAMKLKKAGVNILGTTPENINAAEDREEFSKLLKKLNIPQAEG--GTAFTKEEALKIAKRIGYPVLVRPSYVLGGRAMQI 256
Cdd:PRK08654 91 FAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGteEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 257 VYSEEELIEYMEEAVRVSE----EHPVLIDKFLEDA--IELDVDAVCDGESVLIG----AIM-EH---IEEAgvhsgdSA 322
Cdd:PRK08654 171 VYSEEELEDAIESTQSIAQsafgDSTVFIEKYLEKPrhIEIQILADKHGNVIHLGdrecSIQrRHqklIEEA------PS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 323 TVIPPQtLPKEIIDTVIdytaKLARALNIVGLLNVQYAVKDGVVYVLEANPRASRTVPYVSKSVGIPLAKLATKIMLGKK 402
Cdd:PRK08654 245 PIMTPE-LRERMGEAAV----KAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319
|
..
gi 506213642 403 LE 404
Cdd:PRK08654 320 LS 321
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
179-403 |
5.34e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 58.89 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 179 LAMKLKKAGVNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAF--TKEEALKIAKRIGYPVLVRPSYVLGGRAMQI 256
Cdd:PRK06111 91 FAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNleDAEEAIAIARQIGYPVMLKASAGGGGIGMQL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 257 VYSEEELIEY----MEEAVRVSEEHPVLIDKFLEDA--IELDVDAVCDGESVLIG----AIMEH----IEEAgvhsgdsa 322
Cdd:PRK06111 171 VETEQELTKAfesnKKRAANFFGNGEMYIEKYIEDPrhIEIQLLADTHGNTVYLWerecSVQRRhqkvIEEA-------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 323 tviPPQTLPKEIIDTVIDYTAKLARALNIVGLLNVQYAV-KDGVVYVLEANPRASRTVPYVSKSVGIPLAKLATKIMLGK 401
Cdd:PRK06111 243 ---PSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVdEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGE 319
|
..
gi 506213642 402 KL 403
Cdd:PRK06111 320 KL 321
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
212-374 |
2.49e-08 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 53.80 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 212 KKLNIPQAEGGTAFTKEEALKIAKRIGYPVLVRpSYVLG--GRAMQIVYSeeelIEYMEEAVRVSEEHPVLIDKFLEDAI 289
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVK-ARRGGydGKGQYVVRS----EADLPQAWEELGDGPVIVEEFVPFDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 290 ELDVDAVCDGE-SVLIGAIMEHIEEagvhSGDSATVIPPQTLPKEIIDTVIDYTAKLARALNIVGLLNVQ-YAVKDGVVY 367
Cdd:pfam02222 76 ELSVLVVRSVDgETAFYPVVETIQE----DGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVElFVTEDGDLL 151
|
....*..
gi 506213642 368 VLEANPR 374
Cdd:pfam02222 152 INELAPR 158
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
190-393 |
3.46e-08 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 55.70 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 190 ILGTTPENINAAEDREEFSKLLKKLNIPQAEggTAFTKEEAlkiakriGYPVLVRPSYVLGGRAMQIVYSeeelieymee 269
Cdd:COG2232 99 LLGNPPEVVRRVKDPLRFFALLDELGIPHPE--TRFEPPPD-------PGPWLVKPIGGAGGWHIRPADS---------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 270 AVRVSEEHpvlidkFLEDAIE---LDVDAVCDG-ESVLIGAIMEHIEEAGVH----SGdsatVIPPQTLPKEIIDTVIDY 341
Cdd:COG2232 160 EAPPAPGR------YFQRYVEgtpASVLFLADGsDARVLGFNRQLIGPAGERpfryGG----NIGPLALPPALAEEMRAI 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506213642 342 TAKLARALNIVGLLNVQYAVKDGVVYVLEANPRASRTVPYVSKSVGIPLAKL 393
Cdd:COG2232 230 AEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFDA 281
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
180-403 |
2.85e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 53.22 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 180 AMKLKKAGVNILGTTPENINAAEDREEFSKLLKKLNIPQAEG--GTAFTKEEALKIAKRIGYPVLVRPSYVLGGRAMQIV 257
Cdd:PRK12833 95 AEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGsdGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 258 YSEEELIEYMEEAVRVSE----EHPVLIDKFLEDAIELDVDAVCDGESVLigaimeHI---------------EEAgvhs 318
Cdd:PRK12833 175 HDAAQLAAELPLAQREAQaafgDGGVYLERFIARARHIEVQILGDGERVV------HLferecslqrrrqkilEEA---- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 319 gdsatviPPQTLPKEIIDTVIDYTAKLARALNIVGLLNVQYAVKD--GVVYVLEANPRASRTVPYVSKSVGIPLAKLATK 396
Cdd:PRK12833 245 -------PSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDarGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLR 317
|
....*..
gi 506213642 397 IMLGKKL 403
Cdd:PRK12833 318 IADGEPL 324
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
339-424 |
4.32e-07 |
|
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: 49.15 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 339 IDYTAKLARALNIVGLLNVQYAVKDGVVYVLEANPRASRTVPYvSKSVGIPLAKLATKIMLGKKLEELIndyDVEKVAEK 418
Cdd:pfam15632 50 IEAARRLAEAFGLDGLFNVQFRYDGDGPKLLEINPRMSGGIGY-SCLAGVNLPYLALKLLLGLETPDPV---EPRLGLRV 125
|
....*.
gi 506213642 419 VWIAKP 424
Cdd:pfam15632 126 REIEKV 131
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
209-397 |
1.07e-06 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 50.88 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 209 KLLKKLNIPQAEGgTAFTKEEAL---KIAKRIGYPVLVRPsyVLGG--RAMQIVYSEEELIEYMEEAVRvsEEHPVLIDK 283
Cdd:COG1181 101 RVLAAAGLPTPPY-VVLRRGELAdleAIEEELGLPLFVKP--AREGssVGVSKVKNAEELAAALEEAFK--YDDKVLVEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 284 FLeDAIELDVdAVCDGESVLIGAIMEHIEEAGV-------HSGDSATVIPPQtLPKEIIDTVIDYTAKLARALNIVGlln 356
Cdd:COG1181 176 FI-DGREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPAR-LPEELEERIQELALKAFRALGCRG--- 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506213642 357 vqYA------VKDGVVYVLEANP-----RASrTVPYVSKSVGIPLAKLATKI 397
Cdd:COG1181 250 --YArvdfrlDEDGEPYLLEVNTlpgmtPTS-LLPKAAAAAGISYEELIERI 298
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
187-259 |
1.14e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 51.34 E-value: 1.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506213642 187 GVNILGTTPENINAAEDREEFSKLLKKLNIPQAEG--GTAFTKEEALKIAKRIGYPVLVRPSYVLGGRAMQIVYS 259
Cdd:PRK08591 99 GFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGsdGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRT 173
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
147-373 |
4.60e-06 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 48.50 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 147 TFEDVLNIAEREKERGELLGVIVQF-GGQTAINLAMKLKKAGVNILgTTPENINAAEDREEFSKLLKKLNIPQAEGGTAF 225
Cdd:TIGR00768 32 PPAINLTFNEGPRALAELDVVIVRIvSMFRGLAVLRYLESLGVPVI-NSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 226 TKEEALKIAKRIGYPVLVRPSYVLGGRAMQIVYSEEELIEYMEEAVRVSEEHPV-LIDKFLEDAIELDVDAVCDGESVlI 304
Cdd:TIGR00768 111 SPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQLNGPQNLfLVQEYIKKPGGRDIRVFVVGDEV-V 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506213642 305 GAIMEHIEE---AGVHSGDSATVIPpqtLPKEIidtvidytAKLA-RALNIVGLlnvQYA------VKDGVVyVLEANP 373
Cdd:TIGR00768 190 AAIYRITSGhwrSNLARGGKAEPCS---LTEEI--------EELAiKAAKALGL---DVAgvdlleSEDGLL-VNEVNA 253
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
209-380 |
2.61e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 46.64 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 209 KLLKKLNIPQAEGGTAFTKEEALKIAKRIGYPVLVRPsyVLGGR--AMQIVYSEEELIEYMEEAVRVSEEhpVLIDKFLE 286
Cdd:PRK01372 104 LVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELAFKYDDE--VLVEKYIK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 287 dAIELDVdAVCDGEsVLigAIMEhIE--------EAGVHSGDSATVIPPQtLPKEIIDTVIDYTAKLARALNIVGLLNVQ 358
Cdd:PRK01372 180 -GRELTV-AVLGGK-AL--PVIE-IVpagefydyEAKYLAGGTQYICPAG-LPAEIEAELQELALKAYRALGCRGWGRVD 252
|
170 180
....*....|....*....|...
gi 506213642 359 YAVKD-GVVYVLEANprasrTVP 380
Cdd:PRK01372 253 FMLDEdGKPYLLEVN-----TQP 270
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
179-374 |
3.08e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 47.06 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 179 LAMKLKKAGVNILGTTPENINAAEDREEFSKLLKKLNIPQAEG--GTAFTKEEALKIAKRIGYPVLVRPSYVLGGRAMQI 256
Cdd:PRK12999 95 FARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 257 VYSEEELIEYMEEAVRVSE------EhpVLIDKFLEDA--IELDVDAvcDGEsvliGAIMeH---------------IEE 313
Cdd:PRK12999 175 VRSEEELEEAFERAKREAKaafgndE--VYLEKYVENPrhIEVQILG--DKH----GNVV-HlyerdcsvqrrhqkvVEI 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506213642 314 AgvhsgdsatviPPQTLPKEIIDTVIDYTAKLARALNIVGLLNVQYAV-KDGVVYVLEANPR 374
Cdd:PRK12999 246 A-----------PAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVdADGNFYFIEVNPR 296
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
85-257 |
5.05e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 46.28 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 85 KKVIIIGSGPIrigqgiefdysSVHAVLALKEMGIEAIIVnnnpetvstdYDTSDK--LYFE----------PITFEDVL 152
Cdd:PRK08462 5 KRILIANRGEI-----------ALRAIRTIQEMGKEAIAI----------YSTADKdaLYLKyadakiciggAKSSESYL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 153 NIAEREKErGELLGVIVQFGGQTAI----NLAMKLKKAGVNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTK- 227
Cdd:PRK08462 64 NIPAIISA-AEIFEADAIFPGYGFLsenqNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKs 142
|
170 180 190
....*....|....*....|....*....|.
gi 506213642 228 -EEALKIAKRIGYPVLVRPSYVLGGRAMQIV 257
Cdd:PRK08462 143 yEEAKKIAKEIGYPVILKAAAGGGGRGMRVV 173
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
201-247 |
5.35e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 46.30 E-value: 5.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 506213642 201 AEDREEFSKLLKKLNIPQAEGGTAFTKEEALKIAKRIGYPVLVRPSY 247
Cdd:PRK14016 212 ACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLD 258
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
7-26 |
7.55e-05 |
|
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: 41.21 E-value: 7.55e-05
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
201-374 |
1.47e-04 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 42.76 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 201 AEDREEFSKLLKKLNIPQAEGGTAFTKEealkiakRIGYPVLVRPSYVLGGRAMQIVYSEEELIEYMEeavrvseehPVL 280
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTPETLQAEELL-------REEKKYVVKPRDGCGGEGVRKVENGREDEAFIE---------NVL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 281 IDKFLEdAIELDVDAVCDGESVLIGAI-MEHIEEAGVHSGDSATVIP-PQTLPKEIIDTVIDYTAKLAralNIVGLLNVQ 358
Cdd:pfam02655 65 VQEFIE-GEPLSVSLLSDGEKALPLSVnRQYIDNGGSGFVYAGNVTPsRTELKEEIIELAEEVVECLP---GLRGYVGVD 140
|
170
....*....|....*.
gi 506213642 359 YAVKDGVVYVLEANPR 374
Cdd:pfam02655 141 LVLKDNEPYVIEVNPR 156
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
210-397 |
2.58e-04 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 42.69 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 210 LLKKLNIPQA-------EGGTAFTKEEALKIAKRIGYPVLVRPSyVLGGR-AMQIVYSEEELIEYMEEAVRVSEEhpVLI 281
Cdd:pfam07478 1 LLKAAGLPVVpfvtftrADWKLNPKEWCAQVEEALGYPVFVKPA-RLGSSvGVSKVESREELQAAIEEAFQYDEK--VLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 282 DKFLEdAIELDVdAVCDGESVLIGAIMEHIEEAGV------HSGDSATVIPPQTLPKEIIDTVIDYTAKLARALNIVGLL 355
Cdd:pfam07478 78 EEGIE-GREIEC-AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506213642 356 NVQYAV-KDGVVYVLEANPRASRT----VPYVSKSVGIPLAKLATKI 397
Cdd:pfam07478 156 RVDFFLtEDGEIVLNEVNTIPGFTsismFPKLAAAAGVSFPDLVDQL 202
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
85-252 |
3.59e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 43.55 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 85 KKVIIIGSGPIrigqgiefdysSVHAVLALKEMGIEAIIVNNNPETVSTDYDTSDKLYF---EPIT-FEDVLNIAEREKE 160
Cdd:PRK07178 3 KKILIANRGEI-----------AVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSigaDPLAgYLNPRRLVNLAVE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 161 RG-ELLGVIVQFGGQTAiNLAMKLKKAGVNILGTTPENINAAEDREEFSKLLKKLNIPQAEG--GTAFTKEEALKIAKRI 237
Cdd:PRK07178 72 TGcDALHPGYGFLSENA-ELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGseGNLADLDEALAEAERI 150
|
170
....*....|....*
gi 506213642 238 GYPVLVRPSYVLGGR 252
Cdd:PRK07178 151 GYPVMLKATSGGGGR 165
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
206-374 |
4.04e-04 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 41.88 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 206 EFSK-LLKKLNIPQAEGGTaFTK-EEALKIAKRIGYPVLV-RPSYVLGGRAMQIVYSeeelieyMEEAVRVSEE------ 276
Cdd:pfam01071 4 SFAKdFMKRYGIPTAEYET-FTDpEEAKSYIQEAGFPAIVvKADGLAAGKGVIVASS-------NEEAIKAVDEileqkk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 277 -----HPVLIDKFLEdAIELDVDAVCDGESV---LIGAIMEHIEEA--GVHSG-----DSATVIPPQTLpKEIIDTVIDY 341
Cdd:pfam01071 76 fgeagETVVIEEFLE-GEEVSVLAFVDGKTVkplPPAQDHKRAGEGdtGPNTGgmgaySPAPVITPELL-ERIKETIVEP 153
|
170 180 190
....*....|....*....|....*....|....*
gi 506213642 342 TAKLARALNI--VGLLNVQYAVKDGVVYVLEANPR 374
Cdd:pfam01071 154 TVDGLRKEGIpfKGVLYAGLMLTKDGPKVLEFNCR 188
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
209-252 |
6.74e-04 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 41.48 E-value: 6.74e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 506213642 209 KLLKKLNIPQAEGGTAFTKEEALKIAKRIGYPVLVRPSYVL-GGR 252
Cdd:pfam08442 9 EIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLaGGR 53
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
180-258 |
1.04e-03 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 42.11 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 180 AMKLKKAGVNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTKE--EALKI-AKRIGYPVLVRPSYVLGGRAMQI 256
Cdd:PRK08463 91 AKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSEsmEEIKIfARKIGYPVILKASGGGGGRGIRV 170
|
..
gi 506213642 257 VY 258
Cdd:PRK08463 171 VH 172
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
174-374 |
1.38e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 41.76 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 174 QTAINLAMKLkkagvNILGTTPENINAAEDREEFSKLLKKLNIPQAEGGTAFTKEEALKIAKRIGYPVLVRPSYVLGGRA 253
Cdd:PRK02186 83 EVASEVARRL-----GLPAANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 254 MQIVYSEEELIEYMEEAVRVSEEHpVLIDKFLEDAiELDVDAVCDGESVLIGAIME-------HIEEAGvHSGdSATVIP 326
Cdd:PRK02186 158 VRLCASVAEAAAHCAALRRAGTRA-ALVQAYVEGD-EYSVETLTVARGHQVLGITRkhlgpppHFVEIG-HDF-PAPLSA 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506213642 327 PQTlpKEIIDTVIdytaklaRALNIVGL----LNVQYAVKDGVVYVLEANPR 374
Cdd:PRK02186 234 PQR--ERIVRTVL-------RALDAVGYafgpAHTELRVRGDTVVIIEINPR 276
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
228-374 |
2.25e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 41.22 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 228 EEALKIAKRIGYPVLVRPSYVLGGRAMQIVYSEEELIEYMEEAVRVSE------EhpVLIDKFLEDA--IELDVDAVCDG 299
Cdd:COG1038 145 EEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafgddE--VFLEKYIERPkhIEVQILGDKHG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 300 ESVligaimeH---------------IEEAgvhsgdsatviPPQTLPKEIIDTVIDYTAKLARALNIVGLLNVQYAV-KD 363
Cdd:COG1038 223 NIV-------HlferdcsvqrrhqkvVEIA-----------PAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVdDD 284
|
170
....*....|.
gi 506213642 364 GVVYVLEANPR 374
Cdd:COG1038 285 GNFYFIEVNPR 295
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
209-373 |
3.07e-03 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 40.10 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 209 KLLKKLNIPQAEGgTAFTKEEALK-----IAKRIGYPVLVRPSyvlggRA-----MQIVYSEEELIEYMEEAVRVSEEhp 278
Cdd:PRK01966 129 RLLAAAGIPVAPY-VVLTRGDWEEaslaeIEAKLGLPVFVKPA-----NLgssvgISKVKNEEELAAALDLAFEYDRK-- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213642 279 VLIDKFLeDAIELDVdAVC--DGESVLIGAIMEHIE----EAGVHSGDSATVIPPQtLPKEIIDTVIDYTAKLARALNIV 352
Cdd:PRK01966 201 VLVEQGI-KGREIEC-AVLgnDPKASVPGEIVKPDDfydyEAKYLDGSAELIIPAD-LSEELTEKIRELAIKAFKALGCS 277
|
170 180
....*....|....*....|..
gi 506213642 353 GLLNVQYAV-KDGVVYVLEANP 373
Cdd:PRK01966 278 GLARVDFFLtEDGEIYLNEINT 299
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
209-241 |
3.19e-03 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 40.49 E-value: 3.19e-03
10 20 30
....*....|....*....|....*....|...
gi 506213642 209 KLLKKLNIPQAEGGTAFTKEEALKIAKRIGYPV 241
Cdd:COG1042 495 ALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPV 527
|
|
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