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Conserved domains on  [gi|515804726|ref|WP_017235479|]
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hypothetical protein, partial [Pandoraea sp. B-6]

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]; ...
27-519 2.16e-92

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: 294.78  E-value: 2.16e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  27 LPAP-----ADPLATLRGAADGAALRLRHSDAALHRRLQPDAPLERLLFELMEQLRCETFIPAGMPGVAKNVRDRFEAWS 101
Cdd:COG4547   46 LPEPprrltAEEVAIARGAADALALRLRHHDAALHARLAPQGPEARAVFDALEQARVEALGARRMAGVAANLDAMLEDRY 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 102 RAMHIAGVADSH-------VGLLLytvaqmgWSRLTGYPVIEDTEGLIEATRMAIAPQIGGALAGMRRTCADQAAFAVYA 174
Cdd:COG4547  126 RRAGYARITDRAdapladaLALLV-------RERLTGRPPPPSARKLVDLWRDWIEEKAGADLDRLAELLDDQAAFARAV 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 175 RALAADIaGLIRAAGADQAEGDAKDDEDEKGVRNAFSLFLDIDDQEDDGITL---------AHSGDSRVLKAS------- 238
Cdd:COG4547  199 RDLLRDL-DLAEELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAedaeasgddAEEGESEAAEAEsdemaee 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 239 ------------------------AQGYCVFTQRYDRELYAGTLVRRALLTEFRERLDE------------------RIV 276
Cdd:COG4547  278 aegedseepgepwrpnapppddpaDPDYKVFTTAFDEVVAAEDLCDPEELDRLRAYLDQqlahlqgvvsrlanrlqrRLM 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 277 AQainvprlaralkaalavpQRDGWSFGEEHGRIDGRRLAQLVSSPAERRLFRLEKHTLIAESMVSLLIDCSGSMKAQ-I 355
Cdd:COG4547  358 AQ------------------QNRSWEFDLEEGILDAARLARVVADPTQPLSFKQEKDTEFRDTVVTLLIDNSGSMRGRpI 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 356 EAVAMIVDVLSRALDAAGITNEILGFTTGAWNGGRARTDWLARGKPKFPGRLNEVSHLIFKDAVTSWRRARSDIASLFKA 435
Cdd:COG4547  420 TVAAICADILARTLERCGVKVEILGFTTRAWKGGQSREKWLAAGKPANPGRLNDLRHIIYKSADAPWRRARRNLGLMMRE 499
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 436 DLFREGVDGEAVEWACERLRSRSVNRRLLIVISDGSPMDAATNQANDDHYLDHHLREVVAQQQALGDVEVLGLGVGLDLS 515
Cdd:COG4547  500 GLLKENIDGEALLWAHNRLLARPEQRRILMVISDGAPVDDSTLSVNPGNYLERHLRQVIEEIETRSPVELLAIGIGHDVT 579

                 ....
gi 515804726 516 PYYR 519
Cdd:COG4547  580 RYYR 583
 
Name Accession Description Interval E-value
CobT2 COG4547
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
27-519 2.16e-92

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: 294.78  E-value: 2.16e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  27 LPAP-----ADPLATLRGAADGAALRLRHSDAALHRRLQPDAPLERLLFELMEQLRCETFIPAGMPGVAKNVRDRFEAWS 101
Cdd:COG4547   46 LPEPprrltAEEVAIARGAADALALRLRHHDAALHARLAPQGPEARAVFDALEQARVEALGARRMAGVAANLDAMLEDRY 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 102 RAMHIAGVADSH-------VGLLLytvaqmgWSRLTGYPVIEDTEGLIEATRMAIAPQIGGALAGMRRTCADQAAFAVYA 174
Cdd:COG4547  126 RRAGYARITDRAdapladaLALLV-------RERLTGRPPPPSARKLVDLWRDWIEEKAGADLDRLAELLDDQAAFARAV 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 175 RALAADIaGLIRAAGADQAEGDAKDDEDEKGVRNAFSLFLDIDDQEDDGITL---------AHSGDSRVLKAS------- 238
Cdd:COG4547  199 RDLLRDL-DLAEELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAedaeasgddAEEGESEAAEAEsdemaee 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 239 ------------------------AQGYCVFTQRYDRELYAGTLVRRALLTEFRERLDE------------------RIV 276
Cdd:COG4547  278 aegedseepgepwrpnapppddpaDPDYKVFTTAFDEVVAAEDLCDPEELDRLRAYLDQqlahlqgvvsrlanrlqrRLM 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 277 AQainvprlaralkaalavpQRDGWSFGEEHGRIDGRRLAQLVSSPAERRLFRLEKHTLIAESMVSLLIDCSGSMKAQ-I 355
Cdd:COG4547  358 AQ------------------QNRSWEFDLEEGILDAARLARVVADPTQPLSFKQEKDTEFRDTVVTLLIDNSGSMRGRpI 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 356 EAVAMIVDVLSRALDAAGITNEILGFTTGAWNGGRARTDWLARGKPKFPGRLNEVSHLIFKDAVTSWRRARSDIASLFKA 435
Cdd:COG4547  420 TVAAICADILARTLERCGVKVEILGFTTRAWKGGQSREKWLAAGKPANPGRLNDLRHIIYKSADAPWRRARRNLGLMMRE 499
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 436 DLFREGVDGEAVEWACERLRSRSVNRRLLIVISDGSPMDAATNQANDDHYLDHHLREVVAQQQALGDVEVLGLGVGLDLS 515
Cdd:COG4547  500 GLLKENIDGEALLWAHNRLLARPEQRRILMVISDGAPVDDSTLSVNPGNYLERHLRQVIEEIETRSPVELLAIGIGHDVT 579

                 ....
gi 515804726 516 PYYR 519
Cdd:COG4547  580 RYYR 583
CobT TIGR01651
cobaltochelatase, CobT subunit; This model describes Pseudomonas denitrificans CobT gene ...
22-524 1.07e-86

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: 279.91  E-value: 1.07e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726   22 PHLQTLPAPADpLATLRGAADGAALRLRHSDAALHRRLQPDAPLERLLFELMEQLRCETFIPAGMPGVAKNVRDRFEAWS 101
Cdd:TIGR01651  39 PELPKDLSSRE-AARTRGLGDSMALRLACHDARIHARARPSGPDARAIFDAVEQARVEAIGSNAMGGVAANLTAMLEAKY 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  102 RAMHIAGVADSHVGLLLYTVAQMGWSRLTGYPVIEDTEGLIEATRMAIAPQIGGALAGMRRTCADQAAFAVYARALAADI 181
Cdd:TIGR01651 118 AKANLTVATDRADAPMAEALALMVREKLTGDAPPHSAKALVDLWRNDIEAKAGKDLDRLSAAIDDQQAFARVVREMLRSM 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  182 AgLIRAAGADQAEGDAKDDEDEKGVRNAFSLFLDIDDQEDDGITL---------AHSGDSRVLKASAQG----------- 241
Cdd:TIGR01651 198 E-LAEEMGDDTESEDEEDGDDDQPTENEQEEQGEGEGEGQEGSAPqeseatdreSESGEEEMVQSDQDDlpdesdddset 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  242 -------------------YCVFTQRYDRELYAGTLVRRALLTEFRERLDERIVAQAINVPRLARALKAALAVPQRDGWS 302
Cdd:TIGR01651 277 pgegarparpftstggepdYKVFTTAFDETVDAEELCDEEELDRLRAFLDKQLAALSGVVGRLANRLQRRLMAQQNRSWT 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  303 FGEEHGRIDGRRLAQLVSSPAERRLFRLEKHTLIAESMVSLLIDCSGSMKAQ-IEAVAMIVDVLSRALDAAGITNEILGF 381
Cdd:TIGR01651 357 FDLEEGYLDVARLTRVIIDPMQPLSFKQEEDTEFRDTVVTLLIDNSGSMRGRpITVAATCADILARTLERCGVKVEILGF 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  382 TTGAWNGGRARTDWLARGKPKFPGRLNEVSHLIFKDAVTSWRRARSDIASLFKADLFREGVDGEAVEWACERLRSRSVNR 461
Cdd:TIGR01651 437 TTRAWKGGQSREKWLKAGKPAAPGRLNDLRHIIYKSADAPWRRARRNLGLMMREGLLKENIDGEALMWAHQRLIARPEQR 516
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515804726  462 RLLIVISDGSPMDAATNQANDDHYLDHHLREVVAQQQALGDVEVLGLGVGLDLSPYYRNSLAL 524
Cdd:TIGR01651 517 RILMMISDGAPVDDSTLSVNPGNYLERHLRAVIEEIETRSPVELLAIGIGHDVTRYYRRAVTI 579
CobT_C pfam11775
Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial ...
328-539 4.84e-49

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: 169.05  E-value: 4.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  328 FRLEKHTLIAESMVSLLIDCSGSMKAQ-IEAVAMIVDVLSRALDAAGITNEILGFTTGAWNGGRARTDWLARGKPKFPGR 406
Cdd:pfam11775   2 FMHEEDARARDACVQLLIDLSGSMGGRkIQLAAACADIIADALDRCGVKNEILGFTTFAWKGGPDREAMLAAGFPAFEAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  407 LNEVSHLIFKDAVTSWRRARSDIASLFKADLFREGVDGEAVEWACERLRSRSVNRRLLIVISDGSPMDAATNQANDDHYL 486
Cdd:pfam11775  82 LLDIIHIINEKADAPEIRARKNLGCMCEEFLLKENIDGEALAQAAKLFAGRMEDKKILLMISDGAPCDDSTLSVAAGDGF 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515804726  487 DHHLREVVAQQQALGDVEVLGLGVGLDLS-PYYRNSLAL---DLTSPPDMTMLSRLV 539
Cdd:pfam11775 162 EEHLRHIIEEIETLSDIDLIAIGIGHDAPrRYYKNAALIndaEELGGAITEELAEIF 218
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
341-516 8.25e-30

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: 115.12  E-value: 8.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 341 VSLLIDCSGSMKAQ--IEAVAMIVDVLSRALDAAGITNEILGFTTGAwnGGRARTDWLArgkpkfPGRLNEVSHlifkda 418
Cdd:cd01454    3 VTLLLDLSGSMRSDrrIDVAKKAAVLLAEALEACGVPHAILGFTTDA--GGRERVRWIK------IKDFDESLH------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 419 vtswRRARSDIASLFKADlfrEGVDGEAVEWACERLRSRSVNRRLLIVISDGSPMDAATNQANDDhYLDHHLREVvaqQQ 498
Cdd:cd01454   69 ----ERARKRLAALSPGG---NTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYEGNVF-ATEDALRAV---IE 137
                        170
                 ....*....|....*....
gi 515804726 499 ALGD-VEVLGLGVGLDLSP 516
Cdd:cd01454  138 ARKLgIEVFGITIDRDATT 156
 
Name Accession Description Interval E-value
CobT2 COG4547
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
27-519 2.16e-92

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: 294.78  E-value: 2.16e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  27 LPAP-----ADPLATLRGAADGAALRLRHSDAALHRRLQPDAPLERLLFELMEQLRCETFIPAGMPGVAKNVRDRFEAWS 101
Cdd:COG4547   46 LPEPprrltAEEVAIARGAADALALRLRHHDAALHARLAPQGPEARAVFDALEQARVEALGARRMAGVAANLDAMLEDRY 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 102 RAMHIAGVADSH-------VGLLLytvaqmgWSRLTGYPVIEDTEGLIEATRMAIAPQIGGALAGMRRTCADQAAFAVYA 174
Cdd:COG4547  126 RRAGYARITDRAdapladaLALLV-------RERLTGRPPPPSARKLVDLWRDWIEEKAGADLDRLAELLDDQAAFARAV 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 175 RALAADIaGLIRAAGADQAEGDAKDDEDEKGVRNAFSLFLDIDDQEDDGITL---------AHSGDSRVLKAS------- 238
Cdd:COG4547  199 RDLLRDL-DLAEELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAedaeasgddAEEGESEAAEAEsdemaee 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 239 ------------------------AQGYCVFTQRYDRELYAGTLVRRALLTEFRERLDE------------------RIV 276
Cdd:COG4547  278 aegedseepgepwrpnapppddpaDPDYKVFTTAFDEVVAAEDLCDPEELDRLRAYLDQqlahlqgvvsrlanrlqrRLM 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 277 AQainvprlaralkaalavpQRDGWSFGEEHGRIDGRRLAQLVSSPAERRLFRLEKHTLIAESMVSLLIDCSGSMKAQ-I 355
Cdd:COG4547  358 AQ------------------QNRSWEFDLEEGILDAARLARVVADPTQPLSFKQEKDTEFRDTVVTLLIDNSGSMRGRpI 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 356 EAVAMIVDVLSRALDAAGITNEILGFTTGAWNGGRARTDWLARGKPKFPGRLNEVSHLIFKDAVTSWRRARSDIASLFKA 435
Cdd:COG4547  420 TVAAICADILARTLERCGVKVEILGFTTRAWKGGQSREKWLAAGKPANPGRLNDLRHIIYKSADAPWRRARRNLGLMMRE 499
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 436 DLFREGVDGEAVEWACERLRSRSVNRRLLIVISDGSPMDAATNQANDDHYLDHHLREVVAQQQALGDVEVLGLGVGLDLS 515
Cdd:COG4547  500 GLLKENIDGEALLWAHNRLLARPEQRRILMVISDGAPVDDSTLSVNPGNYLERHLRQVIEEIETRSPVELLAIGIGHDVT 579

                 ....
gi 515804726 516 PYYR 519
Cdd:COG4547  580 RYYR 583
CobT TIGR01651
cobaltochelatase, CobT subunit; This model describes Pseudomonas denitrificans CobT gene ...
22-524 1.07e-86

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: 279.91  E-value: 1.07e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726   22 PHLQTLPAPADpLATLRGAADGAALRLRHSDAALHRRLQPDAPLERLLFELMEQLRCETFIPAGMPGVAKNVRDRFEAWS 101
Cdd:TIGR01651  39 PELPKDLSSRE-AARTRGLGDSMALRLACHDARIHARARPSGPDARAIFDAVEQARVEAIGSNAMGGVAANLTAMLEAKY 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  102 RAMHIAGVADSHVGLLLYTVAQMGWSRLTGYPVIEDTEGLIEATRMAIAPQIGGALAGMRRTCADQAAFAVYARALAADI 181
Cdd:TIGR01651 118 AKANLTVATDRADAPMAEALALMVREKLTGDAPPHSAKALVDLWRNDIEAKAGKDLDRLSAAIDDQQAFARVVREMLRSM 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  182 AgLIRAAGADQAEGDAKDDEDEKGVRNAFSLFLDIDDQEDDGITL---------AHSGDSRVLKASAQG----------- 241
Cdd:TIGR01651 198 E-LAEEMGDDTESEDEEDGDDDQPTENEQEEQGEGEGEGQEGSAPqeseatdreSESGEEEMVQSDQDDlpdesdddset 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  242 -------------------YCVFTQRYDRELYAGTLVRRALLTEFRERLDERIVAQAINVPRLARALKAALAVPQRDGWS 302
Cdd:TIGR01651 277 pgegarparpftstggepdYKVFTTAFDETVDAEELCDEEELDRLRAFLDKQLAALSGVVGRLANRLQRRLMAQQNRSWT 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  303 FGEEHGRIDGRRLAQLVSSPAERRLFRLEKHTLIAESMVSLLIDCSGSMKAQ-IEAVAMIVDVLSRALDAAGITNEILGF 381
Cdd:TIGR01651 357 FDLEEGYLDVARLTRVIIDPMQPLSFKQEEDTEFRDTVVTLLIDNSGSMRGRpITVAATCADILARTLERCGVKVEILGF 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  382 TTGAWNGGRARTDWLARGKPKFPGRLNEVSHLIFKDAVTSWRRARSDIASLFKADLFREGVDGEAVEWACERLRSRSVNR 461
Cdd:TIGR01651 437 TTRAWKGGQSREKWLKAGKPAAPGRLNDLRHIIYKSADAPWRRARRNLGLMMREGLLKENIDGEALMWAHQRLIARPEQR 516
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515804726  462 RLLIVISDGSPMDAATNQANDDHYLDHHLREVVAQQQALGDVEVLGLGVGLDLSPYYRNSLAL 524
Cdd:TIGR01651 517 RILMMISDGAPVDDSTLSVNPGNYLERHLRAVIEEIETRSPVELLAIGIGHDVTRYYRRAVTI 579
CobT_C pfam11775
Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial ...
328-539 4.84e-49

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: 169.05  E-value: 4.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  328 FRLEKHTLIAESMVSLLIDCSGSMKAQ-IEAVAMIVDVLSRALDAAGITNEILGFTTGAWNGGRARTDWLARGKPKFPGR 406
Cdd:pfam11775   2 FMHEEDARARDACVQLLIDLSGSMGGRkIQLAAACADIIADALDRCGVKNEILGFTTFAWKGGPDREAMLAAGFPAFEAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  407 LNEVSHLIFKDAVTSWRRARSDIASLFKADLFREGVDGEAVEWACERLRSRSVNRRLLIVISDGSPMDAATNQANDDHYL 486
Cdd:pfam11775  82 LLDIIHIINEKADAPEIRARKNLGCMCEEFLLKENIDGEALAQAAKLFAGRMEDKKILLMISDGAPCDDSTLSVAAGDGF 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515804726  487 DHHLREVVAQQQALGDVEVLGLGVGLDLS-PYYRNSLAL---DLTSPPDMTMLSRLV 539
Cdd:pfam11775 162 EEHLRHIIEEIETLSDIDLIAIGIGHDAPrRYYKNAALIndaEELGGAITEELAEIF 218
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
341-516 8.25e-30

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: 115.12  E-value: 8.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 341 VSLLIDCSGSMKAQ--IEAVAMIVDVLSRALDAAGITNEILGFTTGAwnGGRARTDWLArgkpkfPGRLNEVSHlifkda 418
Cdd:cd01454    3 VTLLLDLSGSMRSDrrIDVAKKAAVLLAEALEACGVPHAILGFTTDA--GGRERVRWIK------IKDFDESLH------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 419 vtswRRARSDIASLFKADlfrEGVDGEAVEWACERLRSRSVNRRLLIVISDGSPMDAATNQANDDhYLDHHLREVvaqQQ 498
Cdd:cd01454   69 ----ERARKRLAALSPGG---NTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYEGNVF-ATEDALRAV---IE 137
                        170
                 ....*....|....*....
gi 515804726 499 ALGD-VEVLGLGVGLDLSP 516
Cdd:cd01454  138 ARKLgIEVFGITIDRDATT 156
CobT pfam06213
Cobalamin biosynthesis protein CobT; This family consists of several bacterial cobalamin ...
27-203 2.40e-23

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: 99.61  E-value: 2.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726   27 LPAPADPL-----ATLRGAADGAALRLRHSDAALHRRLQPDAPLERLLFELMEQLRCETFIPAGMPGVAKNVRDRFEAWS 101
Cdd:pfam06213  42 LPQPPRKLtaeevARARGFADSLALRLRHHDAAVHARYAPAGPAARAAYDALEQARVEALGARRMAGVAANLDAALEDRY 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726  102 RAMHIAGVAD-------SHVGLLLYtvaqmgwSRLTGYPVIEDTEGLIEATRMAIAPQIGGALAGMRRTCADQAAFAVYA 174
Cdd:pfam06213 122 RRAGYDRATSradaplaEALALLVR-------ERLTGQPPPAAARHVVDLWRPWIEEKAGADLDRLAEALDDQAAFARAA 194
                         170       180
                  ....*....|....*....|....*....
gi 515804726  175 RALAADIaGLIRAAGADQAEGDAKDDEDE 203
Cdd:pfam06213 195 RDLLTDL-DLGDELGDDPEDDDDEEEEDD 222
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
341-492 5.32e-06

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


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 48.95  E-value: 5.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 341 VSLLIDCSGSMKAQIEAVAMIVDV-------LSRALDAAGITNEILGFTtgawngGRARtdwlargkpkfpgrlNEVSHL 413
Cdd:COG4548  251 VLLLLDLSLSTDAWVGSGRRVLDVerealllLAEALEALGDPFAIYGFS------SDGR---------------HRVRYY 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515804726 414 IFKDAVTSW-RRARSDIASLFKADLFRegvDGEAVEWACERLRSRSVNRRLLIVISDGSPmdaatnqaND-DHYLDHHLR 491
Cdd:COG4548  310 RIKDFDEPYdDAVRARIAGLEPGYYTR---MGAAIRHATALLAAQPARRRLLLVLTDGKP--------NDiDVYEGRYGI 378

                 .
gi 515804726 492 E 492
Cdd:COG4548  379 E 379
 
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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