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Conserved domains on  [gi|1242931446|ref|WP_095868589|]
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cobalt chelatase [Rhodococcus sp. ACPA1]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CobT2 super family cl34772
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
22-544 1.18e-98

Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


The actual alignment was detected with superfamily member COG4547:

Pssm-ID: 443611 [Multi-domain]  Cd Length: 608  Bit Score: 311.73  E-value: 1.18e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446  22 AGTIRALAGQSEL----HFRGPELHRGHRRVPMPAPHLHPsldgADFASFRGAADGMASRLLHTDPVLHRSLCPDGTADR 97
Cdd:COG4547    16 AATLRAIAGDPELevsfSADRPGLSGDRARLPEPPRRLTA----EEVAIARGAADALALRLRHHDAALHARLAPQGPEAR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446  98 LIFEILEQFRVESLAADAWGGVRANLSHRFtqwSQDYVASGLT----------ETVHGMllftvtqMCRARITAEPIPEA 167
Cdd:COG4547    92 AVFDALEQARVEALGARRMAGVAANLDAML---EDRYRRAGYAritdradaplADALAL-------LVRERLTGRPPPPS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 168 TEDLIESTRFALASVLGGHLPWLRRTRFSQNDFgvhAQAVAELIgRHLE------------------------------- 216
Cdd:COG4547   162 ARKLVDLWRDWIEEKAGADLDRLAELLDDQAAF---ARAVRDLL-RDLDlaeelgededeededdeddsgeqeedeedge 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 217 ----------SPTDTDVSADDRSDGRAAFSLLFDFEPDDDEAFQTAVSG-------RSRALGEGGDGYRVFTRAYDETRQ 279
Cdd:COG4547   238 dedeesdegaEAEDAEASGDDAEEGESEAAEAESDEMAEEAEGEDSEEPgepwrpnAPPPDDPADPDYKVFTTAFDEVVA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 280 IASLVRPELLQEYRRRLDLgiDLQHLN--VRKLG----RQLKALLSKpvpdGWEGGREEGYLDGRRLAQLVTSPTERRLF 353
Cdd:COG4547   318 AEDLCDPEELDRLRAYLDQ--QLAHLQgvVSRLAnrlqRRLMAQQNR----SWEFDLEEGILDAARLARVVADPTQPLSF 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 354 RAERTEPQTDTTVTFLIDCSGSMKefSEPV---AVLVDVFARALEladaRC----EILGFTTAAWNGGRARRDWLRSGRP 426
Cdd:COG4547   392 KQEKDTEFRDTVVTLLIDNSGSMR--GRPItvaAICADILARTLE----RCgvkvEILGFTTRAWKGGQSREKWLAAGKP 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 427 RNPGRLNEVRQLVFKDAETTWRRARPAIAGLLKNDLFKEGVDGEAVDWACSRMRG-TQGRRLLFVISDGSPLDGATALAN 505
Cdd:COG4547   466 ANPGRLNDLRHIIYKSADAPWRRARRNLGLMMREGLLKENIDGEALLWAHNRLLArPEQRRILMVISDGAPVDDSTLSVN 545
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 1242931446 506 DEFYLDHHLQDVVERHEDERAVEVYGLGVGLDLSPYYDR 544
Cdd:COG4547   546 PGNYLERHLRQVIEEIETRSPVELLAIGIGHDVTRYYRR 584
 
Name Accession Description Interval E-value
CobT2 COG4547
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
22-544 1.18e-98

Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 443611 [Multi-domain]  Cd Length: 608  Bit Score: 311.73  E-value: 1.18e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446  22 AGTIRALAGQSEL----HFRGPELHRGHRRVPMPAPHLHPsldgADFASFRGAADGMASRLLHTDPVLHRSLCPDGTADR 97
Cdd:COG4547    16 AATLRAIAGDPELevsfSADRPGLSGDRARLPEPPRRLTA----EEVAIARGAADALALRLRHHDAALHARLAPQGPEAR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446  98 LIFEILEQFRVESLAADAWGGVRANLSHRFtqwSQDYVASGLT----------ETVHGMllftvtqMCRARITAEPIPEA 167
Cdd:COG4547    92 AVFDALEQARVEALGARRMAGVAANLDAML---EDRYRRAGYAritdradaplADALAL-------LVRERLTGRPPPPS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 168 TEDLIESTRFALASVLGGHLPWLRRTRFSQNDFgvhAQAVAELIgRHLE------------------------------- 216
Cdd:COG4547   162 ARKLVDLWRDWIEEKAGADLDRLAELLDDQAAF---ARAVRDLL-RDLDlaeelgededeededdeddsgeqeedeedge 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 217 ----------SPTDTDVSADDRSDGRAAFSLLFDFEPDDDEAFQTAVSG-------RSRALGEGGDGYRVFTRAYDETRQ 279
Cdd:COG4547   238 dedeesdegaEAEDAEASGDDAEEGESEAAEAESDEMAEEAEGEDSEEPgepwrpnAPPPDDPADPDYKVFTTAFDEVVA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 280 IASLVRPELLQEYRRRLDLgiDLQHLN--VRKLG----RQLKALLSKpvpdGWEGGREEGYLDGRRLAQLVTSPTERRLF 353
Cdd:COG4547   318 AEDLCDPEELDRLRAYLDQ--QLAHLQgvVSRLAnrlqRRLMAQQNR----SWEFDLEEGILDAARLARVVADPTQPLSF 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 354 RAERTEPQTDTTVTFLIDCSGSMKefSEPV---AVLVDVFARALEladaRC----EILGFTTAAWNGGRARRDWLRSGRP 426
Cdd:COG4547   392 KQEKDTEFRDTVVTLLIDNSGSMR--GRPItvaAICADILARTLE----RCgvkvEILGFTTRAWKGGQSREKWLAAGKP 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 427 RNPGRLNEVRQLVFKDAETTWRRARPAIAGLLKNDLFKEGVDGEAVDWACSRMRG-TQGRRLLFVISDGSPLDGATALAN 505
Cdd:COG4547   466 ANPGRLNDLRHIIYKSADAPWRRARRNLGLMMREGLLKENIDGEALLWAHNRLLArPEQRRILMVISDGAPVDDSTLSVN 545
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 1242931446 506 DEFYLDHHLQDVVERHEDERAVEVYGLGVGLDLSPYYDR 544
Cdd:COG4547   546 PGNYLERHLRQVIEEIETRSPVELLAIGIGHDVTRYYRR 584
CobT TIGR01651
cobaltochelatase, CobT subunit; This model describes Pseudomonas denitrificans CobT gene ...
22-548 8.93e-85

cobaltochelatase, CobT subunit; This model describes Pseudomonas denitrificans CobT gene product, which is a cobalt chelatase subunit that functions in cobalamin biosynthesis. Cobalamin (vitamin B12) can be synthesized via several pathways, including an aerobic pathway (found in Pseudomonas denitrificans) and an anaerobic pathway (found in P. shermanii and Salmonella typhimurium). These pathways differ in the point of cobalt insertion during corrin ring formation. There are apparently a number of variations on these two pathways, where the major differences seem to be concerned with the process of ring contraction. Confusion regarding the functions of enzymes found in the aerobic vs. anaerobic pathways has arisen because nonhomologous genes in these different pathways were given the same gene symbols. Thus, cobT in the aerobic pathway (P. denitrificans) is not a homolog of cobT in the anaerobic pathway (S. typhimurium). It should be noted that E. coli synthesizes cobalamin only when it is supplied with the precursor cobinamide, which is a complex intermediate. Additionally, all E. coli cobalamin synthesis genes (cobU, cobS and cobT) were named after their Salmonella typhimurium homologs which function in the anaerobic cobalamin synthesis pathway. This model describes the aerobic cobalamin pathway Pseudomonas denitrificans CobT gene product, which is a cobalt chelatase subunit, with a MW ~70 kDa. The aerobic pathway cobalt chelatase is a heterotrimeric, ATP-dependent enzyme that catalyzes cobalt insertion during cobalamin biosynthesis. The other two subunits are the P. denitrificans CobS (TIGR01650) and CobN (pfam02514 CobN/Magnesium Chelatase) proteins. To avoid potential confusion with the nonhomologous Salmonella typhimurium/E.coli cobT gene product, the P. denitrificans gene symbol is not used in the name of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 130712 [Multi-domain]  Cd Length: 600  Bit Score: 275.28  E-value: 8.93e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446  22 AGTIRALAGQSELHF----RGPELhRGHRRVpmpAPHLHPSLDGADFASFRGAADGMASRLLHTDPVLHRSLCPDGTADR 97
Cdd:TIGR01651   8 AHCARSIAGDPDLEVvfagDRPQL-LGNRAR---LPELPKDLSSREAARTRGLGDSMALRLACHDARIHARARPSGPDAR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446  98 LIFEILEQFRVESLAADAWGGVRANLShrfTQWSQDYVASGLT---ETVHGMLLFTVTQMCRARITAEPIPEATEDLIES 174
Cdd:TIGR01651  84 AIFDAVEQARVEAIGSNAMGGVAANLT---AMLEAKYAKANLTvatDRADAPMAEALALMVREKLTGDAPPHSAKALVDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 175 TRFALASVLGGHLPWLRRTRFSQNDFG------VHAQAVAELIGRHLES------------------------------- 217
Cdd:TIGR01651 161 WRNDIEAKAGKDLDRLSAAIDDQQAFArvvremLRSMELAEEMGDDTESedeedgdddqpteneqeeqgegegegqegsa 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 218 PTDTDVSADDRSDG--RAAFSLLFDFEPDDDEAFQTAVSGRSRA-----LGEGGDgYRVFTRAYDETRQIASLVRPELLQ 290
Cdd:TIGR01651 241 PQESEATDRESESGeeEMVQSDQDDLPDESDDDSETPGEGARPArpftsTGGEPD-YKVFTTAFDETVDAEELCDEEELD 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 291 EYRRRLDLgiDLQHLN--VRKLGRQLKALLSKPVPDGWEGGREEGYLDGRRLAQLVTSPTERRLFRAERTEPQTDTTVTF 368
Cdd:TIGR01651 320 RLRAFLDK--QLAALSgvVGRLANRLQRRLMAQQNRSWTFDLEEGYLDVARLTRVIIDPMQPLSFKQEEDTEFRDTVVTL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 369 LIDCSGSMKefSEPV---AVLVDVFARALELADARCEILGFTTAAWNGGRARRDWLRSGRPRNPGRLNEVRQLVFKDAET 445
Cdd:TIGR01651 398 LIDNSGSMR--GRPItvaATCADILARTLERCGVKVEILGFTTRAWKGGQSREKWLKAGKPAAPGRLNDLRHIIYKSADA 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 446 TWRRARPAIAGLLKNDLFKEGVDGEAVDWACSR-MRGTQGRRLLFVISDGSPLDGATALANDEFYLDHHLQDVVERHEDE 524
Cdd:TIGR01651 476 PWRRARRNLGLMMREGLLKENIDGEALMWAHQRlIARPEQRRILMMISDGAPVDDSTLSVNPGNYLERHLRAVIEEIETR 555
                         570       580
                  ....*....|....*....|....
gi 1242931446 525 RAVEVYGLGVGLDLSPYYDRCRTL 548
Cdd:TIGR01651 556 SPVELLAIGIGHDVTRYYRRAVTI 579
CobT_C pfam11775
Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial ...
353-548 1.18e-41

Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial cobalamin biosynthesis (CobT) proteins. CobT is involved in the transformation of precorrin-3 into cobyrinic acid.


Pssm-ID: 288608 [Multi-domain]  Cd Length: 220  Bit Score: 149.41  E-value: 1.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 353 FRAERTEPQTDTTVTFLIDCSGSMKEFSEPVAVL-VDVFARALELADARCEILGFTTAAWNGGRARRDWLRSGRPRNPGR 431
Cdd:pfam11775   2 FMHEEDARARDACVQLLIDLSGSMGGRKIQLAAAcADIIADALDRCGVKNEILGFTTFAWKGGPDREAMLAAGFPAFEAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 432 LNEVRQLVFKDAETTWRRARPAIAGLLKNDLFKEGVDGEAVDWACSRMRG-TQGRRLLFVISDGSPLDGATALANDEFYL 510
Cdd:pfam11775  82 LLDIIHIINEKADAPEIRARKNLGCMCEEFLLKENIDGEALAQAAKLFAGrMEDKKILLMISDGAPCDDSTLSVAAGDGF 161
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1242931446 511 DHHLQDVVERHEDERAVEVYGLGVGLDLS-PYYDRCRTL 548
Cdd:pfam11775 162 EEHLRHIIEEIETLSDIDLIAIGIGHDAPrRYYKNAALI 200
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
364-544 1.79e-24

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 100.09  E-value: 1.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 364 TTVTFLIDCSGSMKEFS--EPVAVLVDVFARALELADARCEILGFTTAAwnGGRARRDWLrsgrprNPGRLNEVRQlvfk 441
Cdd:cd01454     1 LAVTLLLDLSGSMRSDRriDVAKKAAVLLAEALEACGVPHAILGFTTDA--GGRERVRWI------KIKDFDESLH---- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 442 daettwRRARPAIAGLLKNDlfkEGVDGEAVDWACSR-MRGTQGRRLLFVISDGSPLDGATaLANDEFYLDHHLQDVVER 520
Cdd:cd01454    69 ------ERARKRLAALSPGG---NTRDGAAIRHAAERlLARPEKRKILLVISDGEPNDLDY-YEGNVFATEDALRAVIEA 138
                         170       180
                  ....*....|....*....|....
gi 1242931446 521 HedERAVEVYGLGVGLDLSPYYDR 544
Cdd:cd01454   139 R--KLGIEVFGITIDRDATTVDKE 160
 
Name Accession Description Interval E-value
CobT2 COG4547
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
22-544 1.18e-98

Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 443611 [Multi-domain]  Cd Length: 608  Bit Score: 311.73  E-value: 1.18e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446  22 AGTIRALAGQSEL----HFRGPELHRGHRRVPMPAPHLHPsldgADFASFRGAADGMASRLLHTDPVLHRSLCPDGTADR 97
Cdd:COG4547    16 AATLRAIAGDPELevsfSADRPGLSGDRARLPEPPRRLTA----EEVAIARGAADALALRLRHHDAALHARLAPQGPEAR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446  98 LIFEILEQFRVESLAADAWGGVRANLSHRFtqwSQDYVASGLT----------ETVHGMllftvtqMCRARITAEPIPEA 167
Cdd:COG4547    92 AVFDALEQARVEALGARRMAGVAANLDAML---EDRYRRAGYAritdradaplADALAL-------LVRERLTGRPPPPS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 168 TEDLIESTRFALASVLGGHLPWLRRTRFSQNDFgvhAQAVAELIgRHLE------------------------------- 216
Cdd:COG4547   162 ARKLVDLWRDWIEEKAGADLDRLAELLDDQAAF---ARAVRDLL-RDLDlaeelgededeededdeddsgeqeedeedge 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 217 ----------SPTDTDVSADDRSDGRAAFSLLFDFEPDDDEAFQTAVSG-------RSRALGEGGDGYRVFTRAYDETRQ 279
Cdd:COG4547   238 dedeesdegaEAEDAEASGDDAEEGESEAAEAESDEMAEEAEGEDSEEPgepwrpnAPPPDDPADPDYKVFTTAFDEVVA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 280 IASLVRPELLQEYRRRLDLgiDLQHLN--VRKLG----RQLKALLSKpvpdGWEGGREEGYLDGRRLAQLVTSPTERRLF 353
Cdd:COG4547   318 AEDLCDPEELDRLRAYLDQ--QLAHLQgvVSRLAnrlqRRLMAQQNR----SWEFDLEEGILDAARLARVVADPTQPLSF 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 354 RAERTEPQTDTTVTFLIDCSGSMKefSEPV---AVLVDVFARALEladaRC----EILGFTTAAWNGGRARRDWLRSGRP 426
Cdd:COG4547   392 KQEKDTEFRDTVVTLLIDNSGSMR--GRPItvaAICADILARTLE----RCgvkvEILGFTTRAWKGGQSREKWLAAGKP 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 427 RNPGRLNEVRQLVFKDAETTWRRARPAIAGLLKNDLFKEGVDGEAVDWACSRMRG-TQGRRLLFVISDGSPLDGATALAN 505
Cdd:COG4547   466 ANPGRLNDLRHIIYKSADAPWRRARRNLGLMMREGLLKENIDGEALLWAHNRLLArPEQRRILMVISDGAPVDDSTLSVN 545
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 1242931446 506 DEFYLDHHLQDVVERHEDERAVEVYGLGVGLDLSPYYDR 544
Cdd:COG4547   546 PGNYLERHLRQVIEEIETRSPVELLAIGIGHDVTRYYRR 584
CobT TIGR01651
cobaltochelatase, CobT subunit; This model describes Pseudomonas denitrificans CobT gene ...
22-548 8.93e-85

cobaltochelatase, CobT subunit; This model describes Pseudomonas denitrificans CobT gene product, which is a cobalt chelatase subunit that functions in cobalamin biosynthesis. Cobalamin (vitamin B12) can be synthesized via several pathways, including an aerobic pathway (found in Pseudomonas denitrificans) and an anaerobic pathway (found in P. shermanii and Salmonella typhimurium). These pathways differ in the point of cobalt insertion during corrin ring formation. There are apparently a number of variations on these two pathways, where the major differences seem to be concerned with the process of ring contraction. Confusion regarding the functions of enzymes found in the aerobic vs. anaerobic pathways has arisen because nonhomologous genes in these different pathways were given the same gene symbols. Thus, cobT in the aerobic pathway (P. denitrificans) is not a homolog of cobT in the anaerobic pathway (S. typhimurium). It should be noted that E. coli synthesizes cobalamin only when it is supplied with the precursor cobinamide, which is a complex intermediate. Additionally, all E. coli cobalamin synthesis genes (cobU, cobS and cobT) were named after their Salmonella typhimurium homologs which function in the anaerobic cobalamin synthesis pathway. This model describes the aerobic cobalamin pathway Pseudomonas denitrificans CobT gene product, which is a cobalt chelatase subunit, with a MW ~70 kDa. The aerobic pathway cobalt chelatase is a heterotrimeric, ATP-dependent enzyme that catalyzes cobalt insertion during cobalamin biosynthesis. The other two subunits are the P. denitrificans CobS (TIGR01650) and CobN (pfam02514 CobN/Magnesium Chelatase) proteins. To avoid potential confusion with the nonhomologous Salmonella typhimurium/E.coli cobT gene product, the P. denitrificans gene symbol is not used in the name of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 130712 [Multi-domain]  Cd Length: 600  Bit Score: 275.28  E-value: 8.93e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446  22 AGTIRALAGQSELHF----RGPELhRGHRRVpmpAPHLHPSLDGADFASFRGAADGMASRLLHTDPVLHRSLCPDGTADR 97
Cdd:TIGR01651   8 AHCARSIAGDPDLEVvfagDRPQL-LGNRAR---LPELPKDLSSREAARTRGLGDSMALRLACHDARIHARARPSGPDAR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446  98 LIFEILEQFRVESLAADAWGGVRANLShrfTQWSQDYVASGLT---ETVHGMLLFTVTQMCRARITAEPIPEATEDLIES 174
Cdd:TIGR01651  84 AIFDAVEQARVEAIGSNAMGGVAANLT---AMLEAKYAKANLTvatDRADAPMAEALALMVREKLTGDAPPHSAKALVDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 175 TRFALASVLGGHLPWLRRTRFSQNDFG------VHAQAVAELIGRHLES------------------------------- 217
Cdd:TIGR01651 161 WRNDIEAKAGKDLDRLSAAIDDQQAFArvvremLRSMELAEEMGDDTESedeedgdddqpteneqeeqgegegegqegsa 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 218 PTDTDVSADDRSDG--RAAFSLLFDFEPDDDEAFQTAVSGRSRA-----LGEGGDgYRVFTRAYDETRQIASLVRPELLQ 290
Cdd:TIGR01651 241 PQESEATDRESESGeeEMVQSDQDDLPDESDDDSETPGEGARPArpftsTGGEPD-YKVFTTAFDETVDAEELCDEEELD 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 291 EYRRRLDLgiDLQHLN--VRKLGRQLKALLSKPVPDGWEGGREEGYLDGRRLAQLVTSPTERRLFRAERTEPQTDTTVTF 368
Cdd:TIGR01651 320 RLRAFLDK--QLAALSgvVGRLANRLQRRLMAQQNRSWTFDLEEGYLDVARLTRVIIDPMQPLSFKQEEDTEFRDTVVTL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 369 LIDCSGSMKefSEPV---AVLVDVFARALELADARCEILGFTTAAWNGGRARRDWLRSGRPRNPGRLNEVRQLVFKDAET 445
Cdd:TIGR01651 398 LIDNSGSMR--GRPItvaATCADILARTLERCGVKVEILGFTTRAWKGGQSREKWLKAGKPAAPGRLNDLRHIIYKSADA 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 446 TWRRARPAIAGLLKNDLFKEGVDGEAVDWACSR-MRGTQGRRLLFVISDGSPLDGATALANDEFYLDHHLQDVVERHEDE 524
Cdd:TIGR01651 476 PWRRARRNLGLMMREGLLKENIDGEALMWAHQRlIARPEQRRILMMISDGAPVDDSTLSVNPGNYLERHLRAVIEEIETR 555
                         570       580
                  ....*....|....*....|....
gi 1242931446 525 RAVEVYGLGVGLDLSPYYDRCRTL 548
Cdd:TIGR01651 556 SPVELLAIGIGHDVTRYYRRAVTI 579
CobT_C pfam11775
Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial ...
353-548 1.18e-41

Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial cobalamin biosynthesis (CobT) proteins. CobT is involved in the transformation of precorrin-3 into cobyrinic acid.


Pssm-ID: 288608 [Multi-domain]  Cd Length: 220  Bit Score: 149.41  E-value: 1.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 353 FRAERTEPQTDTTVTFLIDCSGSMKEFSEPVAVL-VDVFARALELADARCEILGFTTAAWNGGRARRDWLRSGRPRNPGR 431
Cdd:pfam11775   2 FMHEEDARARDACVQLLIDLSGSMGGRKIQLAAAcADIIADALDRCGVKNEILGFTTFAWKGGPDREAMLAAGFPAFEAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 432 LNEVRQLVFKDAETTWRRARPAIAGLLKNDLFKEGVDGEAVDWACSRMRG-TQGRRLLFVISDGSPLDGATALANDEFYL 510
Cdd:pfam11775  82 LLDIIHIINEKADAPEIRARKNLGCMCEEFLLKENIDGEALAQAAKLFAGrMEDKKILLMISDGAPCDDSTLSVAAGDGF 161
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1242931446 511 DHHLQDVVERHEDERAVEVYGLGVGLDLS-PYYDRCRTL 548
Cdd:pfam11775 162 EEHLRHIIEEIETLSDIDLIAIGIGHDAPrRYYKNAALI 200
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
364-544 1.79e-24

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 100.09  E-value: 1.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 364 TTVTFLIDCSGSMKEFS--EPVAVLVDVFARALELADARCEILGFTTAAwnGGRARRDWLrsgrprNPGRLNEVRQlvfk 441
Cdd:cd01454     1 LAVTLLLDLSGSMRSDRriDVAKKAAVLLAEALEACGVPHAILGFTTDA--GGRERVRWI------KIKDFDESLH---- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 442 daettwRRARPAIAGLLKNDlfkEGVDGEAVDWACSR-MRGTQGRRLLFVISDGSPLDGATaLANDEFYLDHHLQDVVER 520
Cdd:cd01454    69 ------ERARKRLAALSPGG---NTRDGAAIRHAAERlLARPEKRKILLVISDGEPNDLDY-YEGNVFATEDALRAVIEA 138
                         170       180
                  ....*....|....*....|....
gi 1242931446 521 HedERAVEVYGLGVGLDLSPYYDR 544
Cdd:cd01454   139 R--KLGIEVFGITIDRDATTVDKE 160
CobT pfam06213
Cobalamin biosynthesis protein CobT; This family consists of several bacterial cobalamin ...
22-230 4.84e-22

Cobalamin biosynthesis protein CobT; This family consists of several bacterial cobalamin biosynthesis (CobT) proteins. CobT is involved in the transformation of precorrin-3 into cobyrinic acid.


Pssm-ID: 428829  Cd Length: 274  Bit Score: 96.15  E-value: 4.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446  22 AGTIRALAGQSELH--FRG--PELHRGHRRVPMPAPHLHPsldgADFASFRGAADGMASRLLHTDPVLHRSLCPDGTADR 97
Cdd:pfam06213  12 AGAVRAIAGDPELEvaFSAdpPGLSGDRARLPQPPRKLTA----EEVARARGFADSLALRLRHHDAAVHARYAPAGPAAR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446  98 LIFEILEQFRVESLAADAWGGVRANLSHRFtqwSQDYVASGLTETVHGM---LLFTVTQMCRARITAEPIPEATEDLIES 174
Cdd:pfam06213  88 AAYDALEQARVEALGARRMAGVAANLDAAL---EDRYRRAGYDRATSRAdapLAEALALLVRERLTGQPPPAAARHVVDL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1242931446 175 TRFALASVLGGHLPWLRRTRFSQNDFgvhAQAVAELIgRHLESPTDTDVSADDRSD 230
Cdd:pfam06213 165 WRPWIEEKAGADLDRLAEALDDQAAF---ARAARDLL-TDLDLGDELGDDPEDDDD 216
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
176-498 9.51e-05

Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 45.09  E-value: 9.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 176 RFALASVLGGHLPWLRRTRFSQNDFGVHAQAVAELIGRHLESPTDTDVSADDRSDGRAAFSLLFDFEPDDDEAFQTAVSG 255
Cdd:COG4548    56 ALLREAAARALALLLGALRLAALLSAGLLELALDALPLGRAEPEADAADALDALRDERALDAAADELGDEAPEALGEEPE 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 256 RSRALGEGGDG-------YRVFTRAYDETRQIASLVRPELLQEYRRRLDLGIDLqhlnVRKLGRQLKALLSKPVpdgWEG 328
Cdd:COG4548   136 APDAAASELSAagypewdYRKQRYRPDWCTVLERRPPEGDPAFLDATLARHRRL----IRRLRRQFEALRPQRV---RLR 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 329 GREEG-YLDgrrLAQLVTSPTER--------RLFRAERTEPQtDTTVTFLIDCSGSMKEFSEPVAVLVDV-------FAR 392
Cdd:COG4548   209 RQEDGdELD---LDAAIRALADRraggepdpRIYMRRRRKER-DLAVLLLLDLSLSTDAWVGSGRRVLDVerealllLAE 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242931446 393 ALELADARCEILGFTtaawngGRARrdwlrsgrprnpgrlNEVRQLVFKDAETTW-RRARPAIAGLlkndlfkEGVD--- 468
Cdd:COG4548   285 ALEALGDPFAIYGFS------SDGR---------------HRVRYYRIKDFDEPYdDAVRARIAGL-------EPGYytr 336
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1242931446 469 -GEAVDWACSRMRG-TQGRRLLFVISDGSPLD 498
Cdd:COG4548   337 mGAAIRHATALLAAqPARRRLLLVLTDGKPND 368
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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