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Conserved domains on  [gi|640673956|ref|WP_025098775|]
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MULTISPECIES: precorrin-4 C(11)-methyltransferase [Burkholderia]

Protein Classification

cobalt-precorrin-4/precorrin-4 C(11)-methyltransferase( domain architecture ID 10661383)

cobalt-precorrin-4/precorrin-4 C(11)-methyltransferase catalyzes the methylation of C-11 in cobalt-precorrin-4 or precorrin-4 to form cobalt-precorrin-5 or precorrin-5 in the anaerobic pathway or aerobic pathway of adenosylcobalamin biosynthesis, respectively

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
1-241 8.93e-132

Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


:

Pssm-ID: 442122 [Multi-domain]  Cd Length: 256  Bit Score: 371.70  E-value: 8.93e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   1 MTVYFIGAGPGDPELITVKGQRLVRSCPVILYAGSLVPEAVLDGHQAH-TVVNTAELDLDAIVALLGAAHARGEHVARVH 79
Cdd:COG2875    3 GTVYFVGAGPGDPDLITVKGRRLLEEADVVLYAGSLVPPELLAYCKPGaEIVDSASMTLEEIIALMKEAAAEGKDVVRLH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  80 SGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVILTRYAGKTTLPEGEALGGLAAHRATL 159
Cdd:COG2875   83 SGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAEGRTPMPEGESLASLAAHGATL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956 160 AIHLGVRHLARIVEEVRPHYGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILIGRVLDTDRFADSTLYA 239
Cdd:COG2875  163 AIYLSAHRIDEVVEELLEGYPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGPALGAEDFARSKLYD 242

                 ..
gi 640673956 240 KA 241
Cdd:COG2875  243 PG 244
 
Name Accession Description Interval E-value
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
1-241 8.93e-132

Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 442122 [Multi-domain]  Cd Length: 256  Bit Score: 371.70  E-value: 8.93e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   1 MTVYFIGAGPGDPELITVKGQRLVRSCPVILYAGSLVPEAVLDGHQAH-TVVNTAELDLDAIVALLGAAHARGEHVARVH 79
Cdd:COG2875    3 GTVYFVGAGPGDPDLITVKGRRLLEEADVVLYAGSLVPPELLAYCKPGaEIVDSASMTLEEIIALMKEAAAEGKDVVRLH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  80 SGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVILTRYAGKTTLPEGEALGGLAAHRATL 159
Cdd:COG2875   83 SGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAEGRTPMPEGESLASLAAHGATL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956 160 AIHLGVRHLARIVEEVRPHYGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILIGRVLDTDRFADSTLYA 239
Cdd:COG2875  163 AIYLSAHRIDEVVEELLEGYPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGPALGAEDFARSKLYD 242

                 ..
gi 640673956 240 KA 241
Cdd:COG2875  243 PG 244
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
6-228 1.61e-113

Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. In the aerobic pathway, CobM catalyzes the methylation of precorrin-4 at C-11 to yield precorrin-5. In the anaerobic pathway, CibF catalyzes the methylation of cobalt-precorrin-4 to cobalt-precorrin-5. Both CibF and CobM, which are homologous, are included in this model. There are about 30 enzymes involved in vitamin B12 synthetic pathway. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared in both pathways and several of these enzymes are pathway-specific.


Pssm-ID: 381168 [Multi-domain]  Cd Length: 225  Bit Score: 324.35  E-value: 1.61e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   6 IGAGPGDPELITVKGQRLVRSCPVILYAGSLVPEAVLDGHQAH-TVVNTAELDLDAIVALLGAAHARGEHVARVHSGDPS 84
Cdd:cd11641    1 VGAGPGDPELITVKGARLLEEADVVIYAGSLVPPELLAYAKPGaEIVDSAGMTLEEIIEVMREAAREGKDVVRLHTGDPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  85 LYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVILTRYAGKTTLPEGEALGGLAAHRATLAIHLG 164
Cdd:cd11641   81 LYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRLEGRTPVPEGESLRELAKHGATLAIFLS 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640673956 165 VRHLARIVEEVR-PHYGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILIGRVLD 228
Cdd:cd11641  161 AALIEEVVEELLaGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPALG 225
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
3-240 1.34e-102

precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-3B C17-methyltransferase, EC 2.1.1.131). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 200107  Cd Length: 247  Bit Score: 297.70  E-value: 1.34e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956    3 VYFIGAGPGDPELITVKGQRLVRSCPVILYAGSLVPEAVL-DGHQAHTVVNTAELDLDAIVALLGAAHARGEHVARVHSG 81
Cdd:TIGR01465   1 VYFIGAGPGDPDLITVKGRKLIESADVILYAGSLVPPELLaHCRPGAEVVNSAGMSLEEIVDIMSDAHREGKDVARLHSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   82 DPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVILTRYAGKTTLPEGEALGGLAAHRATLAI 161
Cdd:TIGR01465  81 DPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGRTPMPEGEKLADLAKHGATMAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  162 HLGVRHLARIVEEVRPH-YGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILIGRVLDTDRFADSTLYAK 240
Cdd:TIGR01465 161 FLSAHILDKVVKELIEHgYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPALDPRIGKRSKLYDP 240
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
3-240 7.17e-72

cobalt-precorrin-4 methyltransferase;


Pssm-ID: 185370  Cd Length: 257  Bit Score: 220.01  E-value: 7.17e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   3 VYFIGAGPGDPELITVKGQRLVRSCPVILYAGSLVPEAVLD----GHQAHtvvNTAELDLDAIVALLGAAHARGEHVARV 78
Cdd:PRK15473  10 VWFVGAGPGDKELITLKGYRLLQQAQVVIYAGSLINTELLDycpaQAECH---DSAELHLEQIIDLMEAGVKAGKTVVRL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  79 HSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVILTRYAGKTTLPEGEALGGLAAHRAT 158
Cdd:PRK15473  87 QTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIITRMEGRTPVPAREQLESFASHQTS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956 159 LAIHLGVRHLARIVEE-VRPHYGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILIGRVLDtDRFADSTL 237
Cdd:PRK15473 167 MAIFLSVQRIHRVAERlIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVGNFLG-EEYHYSKL 245

                 ...
gi 640673956 238 YAK 240
Cdd:PRK15473 246 YDA 248
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
2-206 2.56e-45

Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.


Pssm-ID: 425769 [Multi-domain]  Cd Length: 209  Bit Score: 150.57  E-value: 2.56e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956    2 TVYFIGAGPGDPELITVKGQRLVRSCPVILYAGSLVPEAVLD------GHQAHTVVNTAELDLDAIVALLGAAHARGEHV 75
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDllpedlYFPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   76 ARVHSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVILTRyagKTTLPEGEALGGLAAH 155
Cdd:pfam00590  81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLP---GLARIELRLLEALLAN 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 640673956  156 RATLAIHLGVRHLARIVEEVRPHYGDDCPVAVVYRASWPDETRVTGTLADI 206
Cdd:pfam00590 158 GDTVVLLYGPRRLAELAELLLELYPDTTPVAVVERAGTPDEKVVRGTLGEL 208
 
Name Accession Description Interval E-value
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
1-241 8.93e-132

Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 442122 [Multi-domain]  Cd Length: 256  Bit Score: 371.70  E-value: 8.93e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   1 MTVYFIGAGPGDPELITVKGQRLVRSCPVILYAGSLVPEAVLDGHQAH-TVVNTAELDLDAIVALLGAAHARGEHVARVH 79
Cdd:COG2875    3 GTVYFVGAGPGDPDLITVKGRRLLEEADVVLYAGSLVPPELLAYCKPGaEIVDSASMTLEEIIALMKEAAAEGKDVVRLH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  80 SGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVILTRYAGKTTLPEGEALGGLAAHRATL 159
Cdd:COG2875   83 SGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAEGRTPMPEGESLASLAAHGATL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956 160 AIHLGVRHLARIVEEVRPHYGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILIGRVLDTDRFADSTLYA 239
Cdd:COG2875  163 AIYLSAHRIDEVVEELLEGYPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGPALGAEDFARSKLYD 242

                 ..
gi 640673956 240 KA 241
Cdd:COG2875  243 PG 244
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
6-228 1.61e-113

Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. In the aerobic pathway, CobM catalyzes the methylation of precorrin-4 at C-11 to yield precorrin-5. In the anaerobic pathway, CibF catalyzes the methylation of cobalt-precorrin-4 to cobalt-precorrin-5. Both CibF and CobM, which are homologous, are included in this model. There are about 30 enzymes involved in vitamin B12 synthetic pathway. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared in both pathways and several of these enzymes are pathway-specific.


Pssm-ID: 381168 [Multi-domain]  Cd Length: 225  Bit Score: 324.35  E-value: 1.61e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   6 IGAGPGDPELITVKGQRLVRSCPVILYAGSLVPEAVLDGHQAH-TVVNTAELDLDAIVALLGAAHARGEHVARVHSGDPS 84
Cdd:cd11641    1 VGAGPGDPELITVKGARLLEEADVVIYAGSLVPPELLAYAKPGaEIVDSAGMTLEEIIEVMREAAREGKDVVRLHTGDPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  85 LYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVILTRYAGKTTLPEGEALGGLAAHRATLAIHLG 164
Cdd:cd11641   81 LYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRLEGRTPVPEGESLRELAKHGATLAIFLS 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640673956 165 VRHLARIVEEVR-PHYGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILIGRVLD 228
Cdd:cd11641  161 AALIEEVVEELLaGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPALG 225
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
3-240 1.34e-102

precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-3B C17-methyltransferase, EC 2.1.1.131). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 200107  Cd Length: 247  Bit Score: 297.70  E-value: 1.34e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956    3 VYFIGAGPGDPELITVKGQRLVRSCPVILYAGSLVPEAVL-DGHQAHTVVNTAELDLDAIVALLGAAHARGEHVARVHSG 81
Cdd:TIGR01465   1 VYFIGAGPGDPDLITVKGRKLIESADVILYAGSLVPPELLaHCRPGAEVVNSAGMSLEEIVDIMSDAHREGKDVARLHSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   82 DPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVILTRYAGKTTLPEGEALGGLAAHRATLAI 161
Cdd:TIGR01465  81 DPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGRTPMPEGEKLADLAKHGATMAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  162 HLGVRHLARIVEEVRPH-YGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILIGRVLDTDRFADSTLYAK 240
Cdd:TIGR01465 161 FLSAHILDKVVKELIEHgYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPALDPRIGKRSKLYDP 240
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
3-240 7.17e-72

cobalt-precorrin-4 methyltransferase;


Pssm-ID: 185370  Cd Length: 257  Bit Score: 220.01  E-value: 7.17e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   3 VYFIGAGPGDPELITVKGQRLVRSCPVILYAGSLVPEAVLD----GHQAHtvvNTAELDLDAIVALLGAAHARGEHVARV 78
Cdd:PRK15473  10 VWFVGAGPGDKELITLKGYRLLQQAQVVIYAGSLINTELLDycpaQAECH---DSAELHLEQIIDLMEAGVKAGKTVVRL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  79 HSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVILTRYAGKTTLPEGEALGGLAAHRAT 158
Cdd:PRK15473  87 QTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIITRMEGRTPVPAREQLESFASHQTS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956 159 LAIHLGVRHLARIVEE-VRPHYGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILIGRVLDtDRFADSTL 237
Cdd:PRK15473 167 MAIFLSVQRIHRVAERlIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVGNFLG-EEYHYSKL 245

                 ...
gi 640673956 238 YAK 240
Cdd:PRK15473 246 YDA 248
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
6-226 9.04e-47

Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SUMT); SUMT is an enzyme of the cobalamin and siroheme biosynthetic pathway. It catalyzes the first of three steps leading to the formation of siroheme from uroporphyrinogen III; it transfers two methyl groups from S-adenosyl-L-methionine to the C-2 and C-7 atoms of uroporphyrinogen III to yield precorrin-2 via the intermediate formation of precorrin-1. Precorrin-2 is also a precursor for the biosynthesis of vitamin B12, coenzyme F430, siroheme and heme d1. This family includes proteins in which the SUMT domain is fused to other functional domains, such as to a uroporphyrinogen-III synthase domain to form bifunctional uroporphyrinogen-III methylase/uroporphyrinogen-III synthase, or to a dual function dehydrogenase-chelatase domain, as in the case of the multifunctional S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase/dehydrogenase/ferrochelatase CysG, which catalyzes all three steps that transform uroporphyrinogen III into siroheme.


Pssm-ID: 381169  Cd Length: 228  Bit Score: 154.90  E-value: 9.04e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   6 IGAGPGDPELITVKGQRLVRSCPVILYaGSLVPEAVLDGHQAHTVV-------NTAELDLDAIVALLgAAHAR-GEHVAR 77
Cdd:cd11642    1 VGAGPGDPDLLTLKALRALQQADVVLY-DRLVSPEILALAPPGAELiyvgkrpGRHSVPQEEINELL-VELAReGKRVVR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  78 VHSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTV-ILTRYAGKTTLPEGEAlgGLAAHR 156
Cdd:cd11642   79 LKGGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVtFVTGHEADGKLPDDDA--ALARPG 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640673956 157 ATLAIHLGVRHLARIVEEVRPHYGD-DCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILIGRV 226
Cdd:cd11642  157 GTLVIYMGVSNLEEIAERLIAAGLPpDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGEV 227
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
2-206 2.56e-45

Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.


Pssm-ID: 425769 [Multi-domain]  Cd Length: 209  Bit Score: 150.57  E-value: 2.56e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956    2 TVYFIGAGPGDPELITVKGQRLVRSCPVILYAGSLVPEAVLD------GHQAHTVVNTAELDLDAIVALLGAAHARGEHV 75
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDllpedlYFPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   76 ARVHSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVILTRyagKTTLPEGEALGGLAAH 155
Cdd:pfam00590  81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLP---GLARIELRLLEALLAN 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 640673956  156 RATLAIHLGVRHLARIVEEVRPHYGDDCPVAVVYRASWPDETRVTGTLADI 206
Cdd:pfam00590 158 GDTVVLLYGPRRLAELAELLLELYPDTTPVAVVERAGTPDEKVVRGTLGEL 208
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
2-226 7.26e-43

Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; Uroporphyrinogen-III methylase (siroheme synthase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 439778 [Multi-domain]  Cd Length: 245  Bit Score: 145.22  E-value: 7.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   2 TVYFIGAGPGDPELITVKGQRLVRSCPVILYaGSLVPEAVLD---------------GHQAHTVvntaeldlDAIVALLg 66
Cdd:COG0007    3 KVYLVGAGPGDPDLLTLKALRALQQADVVLY-DRLVSPEILAlarpdaeliyvgkrgGRHSLPQ--------EEINALL- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  67 AAHAR-GEHVARVHSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVIL---TRYAGKTT 142
Cdd:COG0007   73 VELARaGKRVVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFvtgHEKDGKLD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956 143 LPegeaLGGLAAHRATLAIHLGVRHLARIVEEVRPH-YGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALI 221
Cdd:COG0007  153 LD----WAALARPGGTLVIYMGVKNLPEIAAALIAAgRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALI 228

                 ....*
gi 640673956 222 LIGRV 226
Cdd:COG0007  229 VVGEV 233
PRK06136 PRK06136
uroporphyrinogen-III C-methyltransferase;
1-228 3.11e-41

uroporphyrinogen-III C-methyltransferase;


Pssm-ID: 235711  Cd Length: 249  Bit Score: 141.12  E-value: 3.11e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   1 MTVYFIGAGPGDPELITVKGQRLVRSCPVILYaGSLVPEAVLD---------------GHQAHTvvntaeldLDAIVALL 65
Cdd:PRK06136   3 GKVYLVGAGPGDPDLITLKGVRLLEQADVVLY-DDLVSPEILAyakpdaeliyvgkraGRHSTK--------QEEINRLL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  66 GAAHARGEHVARVHSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVILTRYAGKTTLPE 145
Cdd:PRK06136  74 VDYARKGKVVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956 146 GE-ALGGLAAHRATLAIHLGVRHLARIVEEVRPH-YGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILI 223
Cdd:PRK06136 154 PEvNWSALADGADTLVIYMGVRNLPYIAAQLLAAgRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIQSPAIIVI 233

                 ....*
gi 640673956 224 GRVLD 228
Cdd:PRK06136 234 GEVVA 238
cobA_cysG_Cterm TIGR01469
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ...
3-226 1.97e-37

uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with uroporphyrin-III C-methyltransferase activity. This enzyme catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). Cobalamin contains cobalt while siroheme contains iron. Siroheme is a cofactor for nitrite and sulfite reductases and therefore plays a role in cysteine biosynthesis; many members of this family are CysG, siroheme synthase, with an additional N-terminal domain and with additional oxidation and iron insertion activities. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273643  Cd Length: 236  Bit Score: 131.19  E-value: 1.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956    3 VYFIGAGPGDPELITVKGQRLVRSCPVILYaGSLVPEAVLDghqahTVVNTAEL------------DLDAIVALLGAAHA 70
Cdd:TIGR01469   2 VYLVGAGPGDPELLTLKALRLLQEADVVLY-DALVSPEILA-----YAPPQAELidvgkrpgchskKQEEINRLLVELAR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   71 RGEHVARVHSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQ--TVILTRYAGKTTLPEGEA 148
Cdd:TIGR01469  76 EGKKVVRLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASsvTFVTGHEADDKALEVDWE 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640673956  149 lgGLAAHRATLAIHLGVRHLARIVEEVRPH-YGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILIGRV 226
Cdd:TIGR01469 156 --ALAKGAGTLVIYMGVRNLPEIAKELIEHgRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGEV 232
PLN02625 PLN02625
uroporphyrin-III C-methyltransferase
2-226 8.43e-33

uroporphyrin-III C-methyltransferase


Pssm-ID: 178232 [Multi-domain]  Cd Length: 263  Bit Score: 119.74  E-value: 8.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   2 TVYFIGAGPGDPELITVKGQRLVRSCPVILYaGSLVPEAVLDGHQAHTVV-------NTAELDLDAIVALLGAAHARGEH 74
Cdd:PLN02625  16 NVFLVGTGPGDPDLLTLKALRLLQTADVVLY-DRLVSPDILDLVPPGAELlyvgkrgGYHSRTQEEIHELLLSFAEAGKT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  75 VARVHSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTV-ILTRYAGKTTLPEGEALGGLA 153
Cdd:PLN02625  95 VVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVrFLTGHDREGGTDPLDVAEAAA 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640673956 154 AHRATLAIHLGVRHLARIVEE-VRPHYGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILIGRV 226
Cdd:PLN02625 175 DPDTTLVVYMGLGTLPSLAEKlIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAGLVSPTVIVVGEV 248
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
3-224 3.88e-32

uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily use S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and Ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.


Pssm-ID: 381178 [Multi-domain]  Cd Length: 243  Bit Score: 117.66  E-value: 3.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   3 VYFIGAGPGDPELITVKGQRLVRSCPVIL--------YAGSLVPEAVLDG------HQAHTVVNTAELDL---------D 59
Cdd:cd11724    2 LYLVGVGPGDPDLITLRALKAIKKADVVFappdlrkrFAEYLAGKEVLDDphglftYYGKKCSPLEEAEKeceelekqrA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  60 AIVALLGAAHARGEHVARVHSGDPSLYGAigeQIRRLKALG--IPyEIVPGVTATAACAATLGVELTLPEVAQTVILTry 137
Cdd:cd11724   82 EIVQKIREALAQGKNVALLDSGDPTIYGP---WIWYLEEFAdlNP-EVIPGVSSFNAANAALKRSLTGGGDSRSVILT-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956 138 AGKTTLPEGEALGGLAAHRATLAIHLGVRHLARIVEEVRPHYGDDCPVAVVYRASWPDETRV-TGTLADIVGKIAGTAIE 216
Cdd:cd11724  156 APFALKENEDLLEDLAATGDTLVIFMMRLDLDELVEKLKKHYPPDTPVAIVYHAGYSEKEKViRGTLDDILEKLGGEKEP 235

                 ....*...
gi 640673956 217 RTALILIG 224
Cdd:cd11724  236 FLGLIYVG 243
PRK07168 PRK07168
uroporphyrin-III C-methyltransferase;
3-227 2.83e-25

uroporphyrin-III C-methyltransferase;


Pssm-ID: 180864 [Multi-domain]  Cd Length: 474  Bit Score: 103.15  E-value: 2.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   3 VYFIGAGPGDPELITVKGQRLVRSCPVILYAGSLVPEAVLDGHQAHTVVNTAELDLDAIV------ALLGAAHARGEHVA 76
Cdd:PRK07168   5 VYLVGAGPGDEGLITKKAIECLKRADIVLYDRLLNPFFLSYTKQTCELMYCGKMPKNHIMrqeminAHLLQFAKEGKIVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  77 RVHSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEvaqtviltrYAGKTTLPEGEALGGLAAH- 155
Cdd:PRK07168  85 RLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRN---------YSNSVTLLTGHAKGPLTDHg 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956 156 -------RATLAIHLGVRHLARIVEEVR-PHYGDDCPVAVVYRASWPDETRVTGTLADIVGKIAGTAIERTALILIGRVL 227
Cdd:PRK07168 156 kynsshnSDTIAYYMGIKNLPTICENLRqAGKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSIVKNENISNPSMTIVGDVV 235
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
6-211 8.45e-22

S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.


Pssm-ID: 381167 [Multi-domain]  Cd Length: 219  Bit Score: 89.76  E-value: 8.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   6 IGAGPGDPELITVKGQRLVRSCPVILYAGSLVPEAVLDGHQ-----AHTVVNTAELDLDAIVALLGAAHARGEHVARVHS 80
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAilkdgKRIYDLHDPNVEEEMAELLLEEARQGKDVAFLSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  81 GDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELtlpevAQTVILTRYAGKTTLPEGEALGGLAAHRATLA 160
Cdd:cd09815   81 GDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDL-----GESFLFVTASDLLENPRLLVLKALAKERRHLV 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 640673956 161 IHLGV----RHLARIVEEVRPhygDDCPVAVVYRASWPDETRVTGTLADIVGKIA 211
Cdd:cd09815  156 LFLDGhrflKALERLLKELGE---DDTPVVLVANAGSEGEVIRTGTVKELRAERT 207
cysG PRK10637
siroheme synthase CysG;
3-227 1.14e-18

siroheme synthase CysG;


Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 84.42  E-value: 1.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   3 VYFIGAGPGDPELITVKGQRLVRSCPVILYaGSLVPEAVLD-----------GHQA--HTVVNtaeldlDAIVALLGAAH 69
Cdd:PRK10637 218 VVLVGAGPGDAGLLTLKGLQQIQQADVVVY-DRLVSDDIMNlvrrdadrvfvGKRAgyHCVPQ------EEINQILLREA 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  70 ARGEHVARVHSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVILTRYAGKTtlpEGEA- 148
Cdd:PRK10637 291 QKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKT---GGELd 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956 149 LGGLAAHRATLAIHLGVRHLARIVEEVRPH-YGDDCPVAVVYRASWPDETRVTGTLADIvGKIAgTAIERTALILIGRVL 227
Cdd:PRK10637 368 WENLAAEKQTLVFYMGLNQAATIQQKLIEHgMPADMPVALVENGTSVTQRVVSGTLTQL-GELA-QQVNSPSLIIVGRVV 445
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
1-212 3.53e-16

Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441844 [Multi-domain]  Cd Length: 229  Bit Score: 74.75  E-value: 3.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   1 MTVYFIGAGPGDPELITVKGQRLVRSCPVILY----------AGSLVpEAVLDGHQAHTVV-------NTAELDLDAIVA 63
Cdd:COG2243    3 GKLYGVGVGPGDPELLTLKAVRALREADVIAYpakgagkaslAREIV-APYLPPARIVELVfpmttdyEALVAAWDEAAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  64 LLGAAHARGEHVARVHSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTlpEVAQTV-ILTRyagktT 142
Cdd:COG2243   82 RIAEELEAGRDVAFLTEGDPSLYSTFMYLLERLRERGFEVEVIPGITSFSAAAAALGIPLA--EGDEPLtVLPG-----T 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956 143 LPEGEALGGLAAHRATLAIHLGvRHLARIVEEVRPHyGDDCPVAVVYRASWPDEtRVTGTLADIVGKIAG 212
Cdd:COG2243  155 LLEEELERALDDFDTVVIMKVG-RNFPKVREALEEA-GLLDRAWYVERAGMPDE-RIVPGLAEVDIEEAP 221
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
3-205 1.28e-14

cobalt-precorrin-7 (C(5))-methyltransferase;


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 70.28  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   3 VYFIGAGPGDPELITVKGQRLVRSCPVIlyAGSlvpEAVLDG----HQAHTVVNTAEL-DLDAIVALlgaaHARGEHVAR 77
Cdd:PRK05787   2 IYIVGIGPGDPEYLTLKALEAIRKADVV--VGS---KRVLELfpelIDGEAFVLTAGLrDLLEWLEL----AAKGKNVVV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  78 VHSGDPSLYGaIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTlpevaQTVILTRYaGKTTLPEgEALGGLAAHRA 157
Cdd:PRK05787  73 LSTGDPLFSG-LGKLLKVRRAVAEDVEVIPGISSVQYAAARLGIDMN-----DVVFTTSH-GRGPNFE-ELEDLLKNGRK 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 640673956 158 TLAI---HLGVRHLARIVEEvrphYGD-DCPVAVVYRASWPDETRVTGTLAD 205
Cdd:PRK05787 145 VIMLpdpRFGPKEIAAELLE----RGKlERRIVVGENLSYPDERIHKLTLSE 192
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
1-133 1.01e-13

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 68.02  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   1 MTVYFIGAGPGDPELITVKGQRLVRSCPVIlYA-------GSLVPEAVLDGHQAHTVV-----------NTAELDLDAIV 62
Cdd:PRK05576   2 GKLYGIGLGPGDPELLTVKAARILEEADVV-YApasrkggGSLALNIVRPYLKEETEIvelhfpmskdeEEKEAVWKENA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640673956  63 ALLGAAHARGEHVARVHSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQTVI 133
Cdd:PRK05576  81 EEIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSFTAIASRAGVPLAMGDESLAII 151
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
6-109 2.18e-13

Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase (also known as S-adenosyl-L-methionine--precorrin-2 methyltransferase) participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. Precorrin-2 C20-methyltransferase catalyzes methylation at the C-20 position of a cyclic tetrapyrrole ring of precorrin-2 using S-adenosylmethionine as a methyl group source to produce precorrin-3A. In the anaerobic pathway, cobalt is inserted into precorrin-2 by CbiK to generate cobalt-precorrin-2, which is the substrate for CbiL, a C20 methyltransferase. In Clostridium difficile, CbiK and CbiL are fused into a bifunctional enzyme. In the aerobic pathway, the precorrin-2 C20-methyltransferase is named CobI. This family includes CbiL and CobI precorrin-2 C20-methyltransferases, both as stand-alone enzymes and when CbiL forms part of a bifunctional enzyme.


Pssm-ID: 381172 [Multi-domain]  Cd Length: 223  Bit Score: 67.15  E-value: 2.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   6 IGAGPGDPELITVKGQRLVRSCPVILY----------AGSLVPEAVLDGHQAHTVV-------NTAELDLDAIVALLGAA 68
Cdd:cd11645    1 VGVGPGDPELLTLKAVRILKEADVIFVpvskggegsaALIIAAALLIPDKEIIPLEfpmtkdrEELEEAWDEAAEEIAEE 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 640673956  69 HARGEHVARVHSGDPSLYGAIGEQIRRLKALGIPYEIVPGV 109
Cdd:cd11645   81 LKEGKDVAFLTLGDPSLYSTFSYLLERLRAPGVEVEIIPGI 121
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
1-124 1.05e-12

precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, one of several closely related S-adenosylmethionine-dependent methyltransferases involved in cobalamin (vitamin B12) biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273642 [Multi-domain]  Cd Length: 230  Bit Score: 65.41  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956    1 MTVYFIGAGPGDPELITVKGQRLVRSCPVILY------AGSLVPEAVLDGHQAHTVVNTA------------ELDLDAIV 62
Cdd:TIGR01467   1 GKLYGVGVGPGDPELITVKALEALRSADVIAVpaskkgRESLARKIVEDYLKPNDTRILElvfpmtkdrdelEKAWDEAA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640673956   63 ALLGAAHARGEHVARVHSGDPSLYGAIGEQIRRLKALGIPYEIVPGVTATAACAATLGVELT 124
Cdd:TIGR01467  81 EAVAAELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAGLPLV 142
PRK05948 PRK05948
precorrin-2 C(20)-methyltransferase;
2-125 5.32e-10

precorrin-2 C(20)-methyltransferase;


Pssm-ID: 180320  Cd Length: 238  Bit Score: 57.73  E-value: 5.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   2 TVYFIGAGPGDPELITVKGQRLVRSCPVILYAgslvpeAVLDGHQ--AHTVVN-----------------TAELDLDAiv 62
Cdd:PRK05948   5 TLYGISVGPGDPELITLKGLRLLQSAPVVAFP------AGLAGQPglAEQIIApwlspqqiklplyfpyvQDEEQLEQ-- 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640673956  63 ALLGAAH------ARGEHVARVHSGDPSLYGAIGEQIRRLKAL--GIPYEIVPGVTATAACAATLGVELTL 125
Cdd:PRK05948  77 AWQAAADqvwhylEQGEDVAFACEGDVSFYSTFTYLAQTLQELypQVAIQTIPGVCSPLAAAAALGIPLTL 147
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
3-205 7.73e-10

precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-4 C11-methyltransferase, EC 2.1.1.133). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. Members of this family may appear as fusion proteins with other enzymes of cobalamin biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273641 [Multi-domain]  Cd Length: 239  Bit Score: 57.31  E-value: 7.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956    3 VYFIGAGPGDPELITVKGQRLVRSCPVI----LYAgSLVpEAVLDGHQAHTVVNTAELDlDAIVALlgAAHARGEHVARV 78
Cdd:TIGR01466   1 LYVVGIGPGAEELMTPEAKEALAEADVIvgykTYL-DLI-EDLIPGKEVVTSGMREEIA-RAELAI--ELAAEGRTVALV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   79 HSGDPSLYGAIGE--QIRRLKALGIPYEIVPGVTATAACAATLGVELTLPEVAQT---------VILTRYagkttlpege 147
Cdd:TIGR01466  76 SSGDPGIYGMAALvfEALEKKGAEVDIEVIPGITAASAAASLLGAPLGHDFCVISlsdlltpwpEIEKRL---------- 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640673956  148 alggLAAHRATLAIHL-------GVRHLARIVEEVRPHYGDDCPVAVVYRASWPDETRVTGTLAD 205
Cdd:TIGR01466 146 ----RAAAEADFVIAIynprskrRPEQFRRAMEILLEHRKPDTPVGIVRNAGREGEEVEITTLAE 206
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
6-209 1.31e-09

Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also known as cobalt-precorrin-7 C(5)-methyltransferase, also known as cobalt-precorrin-6Y C(5)-methyltransferase) catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8. It participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. CbiE functions in the anaerobic pathway, it is a subunit of precorrin-6Y C5,15-methyltransferase, a bifunctional enzyme: cobalt-precorrin-7 C(5)-methyltransferase (CbiE)/cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (CbiT), that catalyzes two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. CbiE and CbiT can be found fused (CbiET, also called CobL), or on separate protein chains (CbiE and CbiT). In the aerobic pathway, a single enzyme called CobL catalyzes the methylations at C-5 and C-15, and the decarboxylation of the C-12 acetate side chain of precorrin-6B.


Pssm-ID: 381171 [Multi-domain]  Cd Length: 198  Bit Score: 55.96  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   6 IGAGPGDPELITVKGQRLVRSCPVILYAGSLVpeAVLDGHQAHTVVntaeLDLDAIVALLGAAHARGEHVARVHSGDPSL 85
Cdd:cd11644    1 IGIGPGGPEYLTPEAREAIEEADVVIGAKRLL--ELFPDLGAEKIP----LPSEDIAELLEEIAEAGKRVVVLASGDPGF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  86 YGaIGEQIRRlKALGIPYEIVPGVTATAACAATLGVELtlpevaQTVILTRYAGKttlpEGEALGGLAAHRATLAIHLGV 165
Cdd:cd11644   75 YG-IGKTLLR-RLGGEEVEVIPGISSVQLAAARLGLPW------EDARLVSLHGR----DLENLRRALRRGRKVFVLTDG 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 640673956 166 RH-LARIVEEVRPHYGDDCPVAVVYRASWPDETRVTGTLADIVGK 209
Cdd:cd11644  143 KNtPAEIARLLLERGLGDSRVTVGENLGYPDERITEGTAEELAEE 187
PRK05765 PRK05765
precorrin-3B C17-methyltransferase; Provisional
1-224 1.88e-07

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 235597  Cd Length: 246  Bit Score: 50.55  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   1 MTVYFIGAGPGDPELITVKGQRLVRSCPVIL----YAGSLvpEAVLDGHQahtvVNTAELDLDAIVALLGAAHAR-GEHV 75
Cdd:PRK05765   2 GKLYIVGIGPGSKEQRTIKAQEAIEKSNVIIgyntYLRLI--SDLLDGKE----VIGARMKEEIFRANTAIEKALeGNIV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  76 ARVHSGDPSLYGAIGEQIRRLKALGIP--YEIVPGVTATAACAATLGVELTLPEVAQTV--ILTryagkttlPEGEALgg 151
Cdd:PRK05765  76 ALVSSGDPQVYGMAGLVFELISRRKLDvdVEVIPGVTAALAAAARLGSPLSLDFVVISLsdLLI--------PREEIL-- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956 152 laaHRATLA------------IHLGVrhLARIVEEVRPHYGDDCPVAVVYRASWPDETRVTGTLADivGKIAGTAIERTA 219
Cdd:PRK05765 146 ---HRVTKAaeadfvivfynpINENL--LIEVMDIVSKHRKPNTPVGLVKSAYRNNENVVITTLSS--WKEHMDEIGMTT 218

                 ....*
gi 640673956 220 LILIG 224
Cdd:PRK05765 219 TMIIG 223
PRK05990 PRK05990
precorrin-2 C(20)-methyltransferase; Reviewed
6-171 2.69e-07

precorrin-2 C(20)-methyltransferase; Reviewed


Pssm-ID: 180341  Cd Length: 241  Bit Score: 49.99  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   6 IGAGPGDPELITVKGQRLVRSCPVILY---------AGSLVpEAVLDGHQAH--------TVVNTAELDLDAIV------ 62
Cdd:PRK05990   8 LGVGPGDPELLTLKALRLLQAAPVVAYfvakgkkgnAFGIV-EAHLSPGQTLlplvypvtTEILPPPLCYETVIadfydt 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  63 -ALLGAAHA-RGEHVARVHSGDPSLYGAIGEQIRRLkALGIPYEIVPGVTATAACAATLGVeltlPEVAQTVILTRYAGk 140
Cdd:PRK05990  87 sAEAVAAHLdAGRDVAVICEGDPFFYGSYMYLHDRL-APRYETEVIPGVCSMLGCWSVLGA----PLVYRNQSLSVLSG- 160
                        170       180       190
                 ....*....|....*....|....*....|.
gi 640673956 141 tTLPEGEALGGLAAHRATLAIHLGvRHLARI 171
Cdd:PRK05990 161 -VLPEEELRRRLADADAAVIMKLG-RNLDKV 189
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
3-109 2.81e-07

Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440634  Cd Length: 250  Bit Score: 50.07  E-value: 2.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   3 VYFIGAGPGDPELITVKGQRLVRSCPVIL-YAG--SLVPEaVLDGHQAHTVVNTAELDldaivallGAAHA-----RGEH 74
Cdd:COG1010    6 LYVVGLGPGSAELMTPRARAALAEADVVVgYGTylDLIPP-LLPGKEVHASGMREEVE--------RAREAlelaaEGKT 76
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 640673956  75 VARVHSGDPSLYG---AIGEQIRRLKA-LGIPYEIVPGV 109
Cdd:COG1010   77 VAVVSSGDPGVYGmagLVLEVLEEGGAwRDVEVEVVPGI 115
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
3-206 4.76e-07

Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17)-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. This model includes CobJ of the aerobic pathway and CbiH of the anaerobic pathway, both as stand-alone enzymes and when CobJ or CbiH form part of bifunctional enzymes, such as in Mycobacterium tuberculosis CobIJ where CobJ fuses with a precorrin-2 C(20)-methyltransferase domain, or Bacillus megaterium CbiH60, where CbiH is fused to a nitrite and sulfite reductase-like domain. In the aerobic pathway, once CobG has generated precorrin-3b, CobJ catalyzes the methylation of precorrin-3b at C-17 to form precorrin-4 (the extruded methylated C-20 fragment is left attached as an acyl group at C-1). In the corresponding anaerobic pathway, CbiH carries out this ring contraction, using cobalt-precorrin-3b as a substrate to generate a tetramethylated delta-lactone.


Pssm-ID: 381173 [Multi-domain]  Cd Length: 238  Bit Score: 49.34  E-value: 4.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956   3 VYFIGAGPGDPELITVKGQRLVRSCPVIL-YAG--SLVPEaVLDGHQAHTVVNTAELDLdAIVALlgAAHARGEHVARVH 79
Cdd:cd11646    1 LYVVGIGPGSADLMTPRAREALEEADVIVgYKTylDLIED-LLPGKEVISSGMGEEVER-AREAL--ELALEGKRVALVS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640673956  80 SGDPSLYG---AIGEQIRRlKALGIPYEIVPGVTATAACAATLGVELT-----------LpeVAQTVILTRYAgkttlpe 145
Cdd:cd11646   77 SGDPGIYGmagLVLELLDE-RWDDIEVEVVPGITAALAAAALLGAPLGhdfavislsdlL--TPWEVIEKRLR------- 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640673956 146 gealgglAAHRATLAIHL-------GVRHLARIVEEVRPHYGDDCPVAVVYRASWPDETRVTGTLADI 206
Cdd:cd11646  147 -------AAAEADFVIALynprskkRPWQLEKALEILLEHRPPDTPVGIVRNAGREGEEVTITTLGEL 207
PTZ00175 PTZ00175
diphthine synthase; Provisional
1-30 4.06e-04

diphthine synthase; Provisional


Pssm-ID: 185500  Cd Length: 270  Bit Score: 40.71  E-value: 4.06e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 640673956   1 MTVYFIGAGPGDPELITVKGQRLVRSCPVI 30
Cdd:PTZ00175   1 MMLYIIGLGLGDEKDITVKGLEAVKSADVV 30
 
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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