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Conserved domains on  [gi|1437643405|emb|STD44174|]
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Cobalt-precorrin-2 C(20)-methyltransferase [Edwardsiella tarda]

Protein Classification

cobalt-factor II C(20)-methyltransferase( domain architecture ID 10792556)

cobalt-factor II C(20)-methyltransferase catalyzes the methylation of cobalt-precorrin-2 at the C-20 position of its cyclic tetrapyrrole ring using S-adenosylmethionine as a methyl group source to produce cobalt-precorrin-3A in the anaerobic cobalamin biosynthesis pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
3-234 2.71e-113

cobalt-factor II C(20)-methyltransferase;


:

Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 324.18  E-value: 2.71e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   3 GRLYALSTGPGAADLVTVRAARLLATLDVLYAPAGRRGGDSLALSIVREYLTPQTEIRCRHFPMSGDSAEKEAAWDGIAT 82
Cdd:PRK05576    2 GKLYGIGLGPGDPELLTVKAARILEEADVVYAPASRKGGGSLALNIVRPYLKEETEIVELHFPMSKDEEEKEAVWKENAE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  83 ELIQAVEAGQRVGFITLGDAMLFSTWVFLLQRIGS-PAWLEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTApEAEII 161
Cdd:PRK05576   82 EIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKChDIEVETVPGISSFTAIASRAGVPLAMGDESLAIIPATR-EALIE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437643405 162 QALQQHDSLVLMKVYGRFARIKALLAQAGLleCALMMAEATLPGERCWRHLDEVDEEQPlaYFSTILVNKRWR 234
Cdd:PRK05576  161 QALTDFDSVVLMKVYKNFALIEELLEEGYL--DALYVRRAYMEGEQILRRLEEILDDLD--YFSTIIANRQWE 229
 
Name Accession Description Interval E-value
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
3-234 2.71e-113

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 324.18  E-value: 2.71e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   3 GRLYALSTGPGAADLVTVRAARLLATLDVLYAPAGRRGGDSLALSIVREYLTPQTEIRCRHFPMSGDSAEKEAAWDGIAT 82
Cdd:PRK05576    2 GKLYGIGLGPGDPELLTVKAARILEEADVVYAPASRKGGGSLALNIVRPYLKEETEIVELHFPMSKDEEEKEAVWKENAE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  83 ELIQAVEAGQRVGFITLGDAMLFSTWVFLLQRIGS-PAWLEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTApEAEII 161
Cdd:PRK05576   82 EIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKChDIEVETVPGISSFTAIASRAGVPLAMGDESLAIIPATR-EALIE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437643405 162 QALQQHDSLVLMKVYGRFARIKALLAQAGLleCALMMAEATLPGERCWRHLDEVDEEQPlaYFSTILVNKRWR 234
Cdd:PRK05576  161 QALTDFDSVVLMKVYKNFALIEELLEEGYL--DALYVRRAYMEGEQILRRLEEILDDLD--YFSTIIANRQWE 229
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
3-231 3.66e-89

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: 263.02  E-value: 3.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   3 GRLYALSTGPGAADLVTVRAARLLATLDVLYAPAGRRGGDSLALSIVREYLTP-QTEIRCRHFPMSGDSAEKEAAWDGIA 81
Cdd:TIGR01467   1 GKLYGVGVGPGDPELITVKALEALRSADVIAVPASKKGRESLARKIVEDYLKPnDTRILELVFPMTKDRDELEKAWDEAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  82 TELIQAVEAGQRVGFITLGDAMLFSTWVFLLQRIGSP-AWLEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTAPEAEI 160
Cdd:TIGR01467  81 EAVAAELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMgIEVEVVPGITSFAACASAAGLPLVEGDESLAILPATAGEAEL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437643405 161 IQALQQHDSLVLMKVYGRFARIKALLAQAGLLECALMMAEATLPGERCWRHLDEVDEEQpLAYFSTILVNK 231
Cdd:TIGR01467 161 EKALAEFDTVVLMKVGRNLPQIKEALAKLGRLDAAVVVERATMPDEKIVDLVREAIDDA-LPYFSTILVRR 230
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
1-229 6.26e-89

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: 262.34  E-value: 6.26e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   1 MTGRLYALSTGPGAADLVTVRAARLLATLDVLYAPAGRRGGDSLALSIVREYLTPQTEIRCrHFPMSGDSAEKEAAWDGI 80
Cdd:COG2243     1 MMGKLYGVGVGPGDPELLTLKAVRALREADVIAYPAKGAGKASLAREIVAPYLPPARIVEL-VFPMTTDYEALVAAWDEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  81 ATELIQAVEAGQRVGFITLGDAMLFSTWVFLLQRI-GSPAWLEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTAPEAE 159
Cdd:COG2243    80 AARIAEELEAGRDVAFLTEGDPSLYSTFMYLLERLrERGFEVEVIPGITSFSAAAAALGIPLAEGDEPLTVLPGTLLEEE 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405 160 IIQALQQHDSLVLMKVYGRFARIKALLAQAGLLECALMMAEATLPGERCWRHLDEVDEEqPLAYFSTILV 229
Cdd:COG2243   160 LERALDDFDTVVIMKVGRNFPKVREALEEAGLLDRAWYVERAGMPDERIVPGLAEVDIE-EAPYFSLILV 228
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
9-229 1.68e-80

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: 240.87  E-value: 1.68e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   9 STGPGAADLVTVRAARLLATLDVLYAPAGRRGGDSLALSIVREYLTPQTEIRCRHFPMSGDSAEKEAAWDGIATELIQAV 88
Cdd:cd11645     2 GVGPGDPELLTLKAVRILKEADVIFVPVSKGGEGSAALIIAAALLIPDKEIIPLEFPMTKDREELEEAWDEAAEEIAEEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  89 EAGQRVGFITLGDAMLFSTWVFLLQRIGSP-AWLEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTAPEAEIIQALQQH 167
Cdd:cd11645    82 KEGKDVAFLTLGDPSLYSTFSYLLERLRAPgVEVEIIPGITSFSAAAARLGIPLAEGDESLAILPATYDEEELEKALENF 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437643405 168 DSLVLMKVYGRFARIKALLAQAGLLECALMMAEATLPGERCWRHLDEVDEEqPLAYFSTILV 229
Cdd:cd11645   162 DTVVLMKVGRNLEEIKELLEELGLLDKAVYVERCGMEGERIYTDLEELKEE-KLPYFSLIIV 222
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
4-210 3.60e-35

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: 124.38  E-value: 3.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   4 RLYALSTGPGAADLVTVRAARLLATLDVLYAPagrrggDSLALSIVREYLTPQteircRHFPMSGDSAEKEAAWDGIATE 83
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGD------DSRALEILLDLLPED-----LYFPMTEDKEPLEEAYEEIAEA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  84 LIQAVEAGQRVGFITLGDAMLFSTWVFLLQRIGSPAW-LEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTAPE----A 158
Cdd:pfam00590  70 LAAALRAGKDVARLVSGDPLVYGTGSYLVEALRAAGIdVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLArielR 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1437643405 159 EIIQALQQHDSLVLMKVYGRFARIKALLAQA-GLLECALMMAEATLPGERCWR 210
Cdd:pfam00590 150 LLEALLANGDTVVLLYGPRRLAELAELLLELyPDTTPVAVVERAGTPDEKVVR 202
 
Name Accession Description Interval E-value
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
3-234 2.71e-113

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 324.18  E-value: 2.71e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   3 GRLYALSTGPGAADLVTVRAARLLATLDVLYAPAGRRGGDSLALSIVREYLTPQTEIRCRHFPMSGDSAEKEAAWDGIAT 82
Cdd:PRK05576    2 GKLYGIGLGPGDPELLTVKAARILEEADVVYAPASRKGGGSLALNIVRPYLKEETEIVELHFPMSKDEEEKEAVWKENAE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  83 ELIQAVEAGQRVGFITLGDAMLFSTWVFLLQRIGS-PAWLEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTApEAEII 161
Cdd:PRK05576   82 EIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKChDIEVETVPGISSFTAIASRAGVPLAMGDESLAIIPATR-EALIE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437643405 162 QALQQHDSLVLMKVYGRFARIKALLAQAGLleCALMMAEATLPGERCWRHLDEVDEEQPlaYFSTILVNKRWR 234
Cdd:PRK05576  161 QALTDFDSVVLMKVYKNFALIEELLEEGYL--DALYVRRAYMEGEQILRRLEEILDDLD--YFSTIIANRQWE 229
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
3-231 3.66e-89

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: 263.02  E-value: 3.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   3 GRLYALSTGPGAADLVTVRAARLLATLDVLYAPAGRRGGDSLALSIVREYLTP-QTEIRCRHFPMSGDSAEKEAAWDGIA 81
Cdd:TIGR01467   1 GKLYGVGVGPGDPELITVKALEALRSADVIAVPASKKGRESLARKIVEDYLKPnDTRILELVFPMTKDRDELEKAWDEAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  82 TELIQAVEAGQRVGFITLGDAMLFSTWVFLLQRIGSP-AWLEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTAPEAEI 160
Cdd:TIGR01467  81 EAVAAELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMgIEVEVVPGITSFAACASAAGLPLVEGDESLAILPATAGEAEL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437643405 161 IQALQQHDSLVLMKVYGRFARIKALLAQAGLLECALMMAEATLPGERCWRHLDEVDEEQpLAYFSTILVNK 231
Cdd:TIGR01467 161 EKALAEFDTVVLMKVGRNLPQIKEALAKLGRLDAAVVVERATMPDEKIVDLVREAIDDA-LPYFSTILVRR 230
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
1-229 6.26e-89

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: 262.34  E-value: 6.26e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   1 MTGRLYALSTGPGAADLVTVRAARLLATLDVLYAPAGRRGGDSLALSIVREYLTPQTEIRCrHFPMSGDSAEKEAAWDGI 80
Cdd:COG2243     1 MMGKLYGVGVGPGDPELLTLKAVRALREADVIAYPAKGAGKASLAREIVAPYLPPARIVEL-VFPMTTDYEALVAAWDEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  81 ATELIQAVEAGQRVGFITLGDAMLFSTWVFLLQRI-GSPAWLEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTAPEAE 159
Cdd:COG2243    80 AARIAEELEAGRDVAFLTEGDPSLYSTFMYLLERLrERGFEVEVIPGITSFSAAAAALGIPLAEGDEPLTVLPGTLLEEE 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405 160 IIQALQQHDSLVLMKVYGRFARIKALLAQAGLLECALMMAEATLPGERCWRHLDEVDEEqPLAYFSTILV 229
Cdd:COG2243   160 LERALDDFDTVVIMKVGRNFPKVREALEEAGLLDRAWYVERAGMPDERIVPGLAEVDIE-EAPYFSLILV 228
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
9-229 1.68e-80

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: 240.87  E-value: 1.68e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   9 STGPGAADLVTVRAARLLATLDVLYAPAGRRGGDSLALSIVREYLTPQTEIRCRHFPMSGDSAEKEAAWDGIATELIQAV 88
Cdd:cd11645     2 GVGPGDPELLTLKAVRILKEADVIFVPVSKGGEGSAALIIAAALLIPDKEIIPLEFPMTKDREELEEAWDEAAEEIAEEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  89 EAGQRVGFITLGDAMLFSTWVFLLQRIGSP-AWLEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTAPEAEIIQALQQH 167
Cdd:cd11645    82 KEGKDVAFLTLGDPSLYSTFSYLLERLRAPgVEVEIIPGITSFSAAAARLGIPLAEGDESLAILPATYDEEELEKALENF 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437643405 168 DSLVLMKVYGRFARIKALLAQAGLLECALMMAEATLPGERCWRHLDEVDEEqPLAYFSTILV 229
Cdd:cd11645   162 DTVVLMKVGRNLEEIKELLEELGLLDKAVYVERCGMEGERIYTDLEELKEE-KLPYFSLIIV 222
PRK05948 PRK05948
precorrin-2 C(20)-methyltransferase;
1-232 2.26e-37

precorrin-2 C(20)-methyltransferase;


Pssm-ID: 180320  Cd Length: 238  Bit Score: 130.92  E-value: 2.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   1 MTGRLYALSTGPGAADLVTVRAARLLATLDVLYAPAGRRGGDSLALSIVREYLTPQTEIRCRHFPMSGDSAEKEAAWDGI 80
Cdd:PRK05948    2 TLGTLYGISVGPGDPELITLKGLRLLQSAPVVAFPAGLAGQPGLAEQIIAPWLSPQQIKLPLYFPYVQDEEQLEQAWQAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  81 ATELIQAVEAGQRVGFITLGDAMLFSTWVFL---LQRIGSPAWLEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTAPE 157
Cdd:PRK05948   82 ADQVWHYLEQGEDVAFACEGDVSFYSTFTYLaqtLQELYPQVAIQTIPGVCSPLAAAAALGIPLTLGSQRLAILPALYHL 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437643405 158 AEIIQALQQHDSLVLMKVYGRFARIKALLAQAGLLECALMMAEATLPGERCWRHLDEVdEEQPLAYFSTILVNKR 232
Cdd:PRK05948  162 EELEQALTWADVVVLMKVSSVYPQVWQWLKARNLLEQASLVERATTPEQVIYRNLEDY-PDLRLPYFSLLIIQKR 235
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
4-210 3.60e-35

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: 124.38  E-value: 3.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   4 RLYALSTGPGAADLVTVRAARLLATLDVLYAPagrrggDSLALSIVREYLTPQteircRHFPMSGDSAEKEAAWDGIATE 83
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGD------DSRALEILLDLLPED-----LYFPMTEDKEPLEEAYEEIAEA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  84 LIQAVEAGQRVGFITLGDAMLFSTWVFLLQRIGSPAW-LEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTAPE----A 158
Cdd:pfam00590  70 LAAALRAGKDVARLVSGDPLVYGTGSYLVEALRAAGIdVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLArielR 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1437643405 159 EIIQALQQHDSLVLMKVYGRFARIKALLAQA-GLLECALMMAEATLPGERCWR 210
Cdd:pfam00590 150 LLEALLANGDTVVLLYGPRRLAELAELLLELyPDTTPVAVVERAGTPDEKVVR 202
PRK05990 PRK05990
precorrin-2 C(20)-methyltransferase; Reviewed
1-235 1.02e-34

precorrin-2 C(20)-methyltransferase; Reviewed


Pssm-ID: 180341  Cd Length: 241  Bit Score: 124.33  E-value: 1.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   1 MTGRLYALSTGPGAADLVTVRAARLLATLDVL--YAPAGRRGGdslALSIVREYLTPQTEIRCRHFPMSGDSAEKEAAW- 77
Cdd:PRK05990    1 AKGRLIGLGVGPGDPELLTLKALRLLQAAPVVayFVAKGKKGN---AFGIVEAHLSPGQTLLPLVYPVTTEILPPPLCYe 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  78 -------DGIATELIQAVEAGQRVGFITLGDAMLFSTWVFLLQRIGSPAWLEIVPGVTSFAAIAARAQTPLAMEQQSLAV 150
Cdd:PRK05990   78 tviadfyDTSAEAVAAHLDAGRDVAVICEGDPFFYGSYMYLHDRLAPRYETEVIPGVCSMLGCWSVLGAPLVYRNQSLSV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405 151 IACTAPEAEIIQALQQHDSLVLMKVYGRFARIKALLAQAGLLECALMMAEATLPGERCWRhLDEVDEEqPLAYFSTILV- 229
Cdd:PRK05990  158 LSGVLPEEELRRRLADADAAVIMKLGRNLDKVRRVLAALGLLDRALYVERATMANQRIVP-LAEVDPM-ASPYFSLILVp 235

                  ....*.
gi 1437643405 230 NKRWRQ 235
Cdd:PRK05990  236 GEKWQG 241
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
4-172 1.90e-15

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: 72.97  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   4 RLYALSTGPGAADLVTVRAARLLATLDVLYAPAGRRGGdslalsiVREYLTPQtEI-------------RCRHFPMSGDS 70
Cdd:cd11724     1 KLYLVGVGPGDPDLITLRALKAIKKADVVFAPPDLRKR-------FAEYLAGK-EVlddphglftyygkKCSPLEEAEKE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  71 A-EKEAAWDGIATELIQAVEAGQRVGFITLGDAMLFSTWVFLLQRiGSPAWLEIVPGVTSFAAIAARAQTPLAMEQQSLA 149
Cdd:cd11724    73 CeELEKQRAEIVQKIREALAQGKNVALLDSGDPTIYGPWIWYLEE-FADLNPEVIPGVSSFNAANAALKRSLTGGGDSRS 151
                         170       180
                  ....*....|....*....|....*....
gi 1437643405 150 VIAcTAPEAE-----IIQALQQH-DSLVL 172
Cdd:cd11724   152 VIL-TAPFALkenedLLEDLAATgDTLVI 179
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
5-218 4.07e-14

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: 69.28  E-value: 4.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   5 LYALSTGPGAADLVTVRAARLLATLDV-LYApagrrggDSLALSIVREYLTPQTEIRcrhfpmsgDSAEKeaAWDGIATE 83
Cdd:TIGR01465   1 VYFIGAGPGDPDLITVKGRKLIESADViLYA-------GSLVPPELLAHCRPGAEVV--------NSAGM--SLEEIVDI 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  84 LIQAVEAGQRVGFITLGDAMLFST---WVFLLQRIGSPawLEIVPGVTSFAAIAARAQTPLAMEQQSLAVI------ACT 154
Cdd:TIGR01465  64 MSDAHREGKDVARLHSGDPSIYGAiaeQMRLLEALGIP--YEVVPGVSSFFAAAAALGAELTVPEVSQTVIltrasgRTP 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437643405 155 APEAEIIQALQQHDSlvLMKVYGRFARIKALlaQAGLLE--------CALMMaEATLPGERCWR-HLDEVDEE 218
Cdd:TIGR01465 142 MPEGEKLADLAKHGA--TMAIFLSAHILDKV--VKELIEhgysedtpVAVVY-RATWPDEKIVRgTLADLADL 209
PRK06136 PRK06136
uroporphyrinogen-III C-methyltransferase;
1-210 4.95e-14

uroporphyrinogen-III C-methyltransferase;


Pssm-ID: 235711  Cd Length: 249  Bit Score: 69.09  E-value: 4.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   1 MTGRLYALSTGPGAADLVTVRAARLLATLDV-LYapagrrggDSLALSIVREYLTPQTEI-----RC-RHFPmsgdsaek 73
Cdd:PRK06136    1 MMGKVYLVGAGPGDPDLITLKGVRLLEQADVvLY--------DDLVSPEILAYAKPDAELiyvgkRAgRHST-------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  74 eaAWDGIATELIQAVEAGQRVGFITLGDAMLFStwvfllqRIGSPA-WL-------EIVPGVTSFAAIAARAQTPLAMEQ 145
Cdd:PRK06136   65 --KQEEINRLLVDYARKGKVVVRLKGGDPFVFG-------RGGEELeALeaagipyEVVPGITAAIAAAAYAGIPLTHRG 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437643405 146 QSLAVIACTAPEAE-------IIQAL-QQHDSLV-LMKVyGRFARIKALLAQAGLLE---CALMMAeATLPGERCWR 210
Cdd:PRK06136  136 VARSVTFVTGHEAAgklepevNWSALaDGADTLViYMGV-RNLPYIAAQLLAAGRAPdtpVAIIEN-GTTPEQRVVR 210
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
1-187 6.25e-14

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: 68.93  E-value: 6.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   1 MTGRLYALSTGPGAADLVTVRAARLLATLDV-LYApagrrggDSLALSIVREYLTPQTEIRcrhfpmsgDSAEKeaAWDG 79
Cdd:COG2875     1 MKGTVYFVGAGPGDPDLITVKGRRLLEEADVvLYA-------GSLVPPELLAYCKPGAEIV--------DSASM--TLEE 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  80 IATELIQAVEAGQRVGFITLGDAMLFSTwVF----LLQRIGSPawLEIVPGVTSFAAIAARAQTPLameqqslaviacTA 155
Cdd:COG2875    64 IIALMKEAAAEGKDVVRLHSGDPSLYGA-IAeqmrRLDALGIP--YEVVPGVSAFAAAAAALGREL------------TL 128
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1437643405 156 PeaEIIQalqqhdSLVLMKVYGR-----------FARIKALLA 187
Cdd:COG2875   129 P--EVSQ------TVILTRAEGRtpmpegeslasLAAHGATLA 163
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
2-210 4.49e-13

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: 66.64  E-value: 4.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   2 TGRLYALSTGPGAADLVTVRAARLLATLDV-LYapagrrggDSLALSIVREYLTPQTEI-----RCRHFPMSGDSaekea 75
Cdd:COG0007     1 KGKVYLVGAGPGDPDLLTLKALRALQQADVvLY--------DRLVSPEILALARPDAELiyvgkRGGRHSLPQEE----- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  76 awdgIATELIQAVEAGQRV----GfitlGDAMLFStwvfllqRIGSPA-WL-------EIVPGVTSFAAIAARAQTPLAM 143
Cdd:COG0007    68 ----INALLVELARAGKRVvrlkG----GDPFVFG-------RGGEEAeALaaagipfEVVPGITAAIAAPAYAGIPLTH 132
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437643405 144 --EQQSLAVI-ACTAPEAEII--QAL-QQHDSLV-LMKVyGRFARIKALLAQAGL---LECALMMAeATLPGERCWR 210
Cdd:COG0007   133 rgVASSVTFVtGHEKDGKLDLdwAALaRPGGTLViYMGV-KNLPEIAAALIAAGRspdTPVAVIEN-GTTPDQRVVT 207
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
11-210 1.34e-12

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: 64.77  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  11 GPGAADLVTVRAARLLATLDV-LYapagrrggDSLALSIVREYLTPQTEI-----RCRHFPMSGDSaekeaawdgIATEL 84
Cdd:cd11642     4 GPGDPDLLTLKALRALQQADVvLY--------DRLVSPEILALAPPGAELiyvgkRPGRHSVPQEE---------INELL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  85 IQAVEAGQRV----GfitlGDAMLFStwvfllqRIGSPA-WL-------EIVPGVTSFAAIAARAQTPLAMEQQSLAVIA 152
Cdd:cd11642    67 VELAREGKRVvrlkG----GDPFVFG-------RGGEEIeALreagipfEVVPGITSAIAAAAYAGIPLTHRGVASSVTF 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437643405 153 CTA------PEAEIIQALQQHDSLVLMKVYGRFARIKALLAQAGLLEC--ALMMAEATLPGERCWR 210
Cdd:cd11642   136 VTGheadgkLPDDDAALARPGGTLVIYMGVSNLEEIAERLIAAGLPPDtpVAIVENATTPDQRVVV 201
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
11-141 6.33e-12

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: 62.80  E-value: 6.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  11 GPGAADLVTVRAARLLATLD-VLYApagrrggDSLALSIVREYLTPQTEIRcrhfpmsgDSAEKeaAWDGIATELIQAVE 89
Cdd:cd11641     4 GPGDPELITVKGARLLEEADvVIYA-------GSLVPPELLAYAKPGAEIV--------DSAGM--TLEEIIEVMREAAR 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1437643405  90 AGQRVGFITLGDAMLFST---WVFLLQRIGSPAwlEIVPGVTSFAAIAARAQTPL 141
Cdd:cd11641    67 EGKDVVRLHTGDPSLYGAireQIDALDKLGIPY--EVVPGVSSFFAAAAALGTEL 119
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
4-232 4.90e-11

Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441842 [Multi-domain]  Cd Length: 207  Bit Score: 60.16  E-value: 4.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   4 RLYALSTGPGAADLVTVRAARLLATLDVLYApaGRRggdslALSIVREYltpqteiRCRHFPMSGDSAEkeaawdgiATE 83
Cdd:COG2241     3 WLTVVGIGPGGPDGLTPAAREAIAEADVVVG--GKR-----HLELFPDL-------GAERIVWPSPLSE--------LLE 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  84 LIQAVEAGQRVGFITLGDAMLFSTWVFLLQRIGsPAWLEIVPGVTSFAAIAARAQTPLameqQSLAVI-ACTAPEAEIIQ 162
Cdd:COG2241    61 ELLALLRGRRVVVLASGDPLFYGIGATLARHLP-AEEVRVIPGISSLQLAAARLGWPW----QDAAVVsLHGRPLERLLP 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437643405 163 ALQQHDSL-VLMKVYGRFARIKALLAQAGLLECALMMAEA-TLPGERCWR-HLDEVDeEQPLAYFSTILVNKR 232
Cdd:COG2241   136 ALAPGRRVlVLTDDGNTPAAIARLLLERGFGDSRLTVLENlGGPDERITRgTAEELA-DADFSDLNVVAIECR 207
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
10-188 9.31e-11

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: 59.71  E-value: 9.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  10 TGPGAADLVTVRAARLLATLDVLYAPagrRGGDSLALSIVREYLTPQTEIRCRHFPMSgdsaekeaaWDGIATELIQAVE 89
Cdd:cd09815     3 VGPGDPDLLTLRALEILRAADVVVAE---DKDSKLLSLVLRAILKDGKRIYDLHDPNV---------EEEMAELLLEEAR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  90 AGQRVGFITLGDAMLFSTWVFLLQRIGSP-AWLEIVPGVTSFAAIAARAQTPLAmeqQSLAVIACTAPEAE-----IIQA 163
Cdd:cd09815    71 QGKDVAFLSPGDPGVAGTGAELVERAEREgVEVKVIPGVSAADAAAAALGIDLG---ESFLFVTASDLLENprllvLKAL 147
                         170       180
                  ....*....|....*....|....*
gi 1437643405 164 LQQHDSLVLMKVYGRFARIKALLAQ 188
Cdd:cd09815   148 AKERRHLVLFLDGHRFLKALERLLK 172
PLN02625 PLN02625
uroporphyrin-III C-methyltransferase
1-210 1.83e-10

uroporphyrin-III C-methyltransferase


Pssm-ID: 178232 [Multi-domain]  Cd Length: 263  Bit Score: 59.26  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   1 MTGRLYALSTGPGAADLVTVRAARLLATLD-VLYapagrrggDSLALSIVREYLTPQTEIRC-RHFPMSGDSAEKEaawd 78
Cdd:PLN02625   13 GPGNVFLVGTGPGDPDLLTLKALRLLQTADvVLY--------DRLVSPDILDLVPPGAELLYvGKRGGYHSRTQEE---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  79 gIATELIQAVEAGQRVGFITLGDAMLFS---TWVFLLQRIGSPAwlEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTA 155
Cdd:PLN02625   81 -IHELLLSFAEAGKTVVRLKGGDPLVFGrggEEMDALRKNGIPV--TVVPGITAAIGAPAELGIPLTHRGVATSVRFLTG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437643405 156 --------PEAEIIQALQQHDSLVLMKVYGRFARIKALLAQAGLL--ECALMMAEATLPGERCWR 210
Cdd:PLN02625  158 hdreggtdPLDVAEAAADPDTTLVVYMGLGTLPSLAEKLIAAGLPpdTPAAAVERGTTPEQRVVF 222
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
5-229 2.37e-10

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


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 58.34  E-value: 2.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   5 LYALSTGPGAADLVTVRAARLLATLDVLYapAGRRggdslALSIVREYLTPQTEIRcrhfpmsGDSAEKEAAWDGIATel 84
Cdd:PRK05787    2 IYIVGIGPGDPEYLTLKALEAIRKADVVV--GSKR-----VLELFPELIDGEAFVL-------TAGLRDLLEWLELAA-- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  85 iqaveAGQRVGFITLGDAMlFSTWVFLLQRIGSPAW-LEIVPGVTSFAAIAARAQTPlaMEQqsLAVIAC---TAPEAEI 160
Cdd:PRK05787   66 -----KGKNVVVLSTGDPL-FSGLGKLLKVRRAVAEdVEVIPGISSVQYAAARLGID--MND--VVFTTShgrGPNFEEL 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437643405 161 IQALQQHDSlVLMKVYGRFA--RIKALLAQAGLLEC-ALMMAEATLPGERCWRHLDEVDEEQPLAYFSTILV 229
Cdd:PRK05787  136 EDLLKNGRK-VIMLPDPRFGpkEIAAELLERGKLERrIVVGENLSYPDERIHKLTLSEIEPLEFSDMSVVVI 206
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
1-141 8.35e-10

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: 57.39  E-value: 8.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   1 MTGRLYALSTGPGAADLVTVRAARLLATLDVLYapagrrgGDSLALSIVREYLTPQT--------EI-RCRHfpmsgdsa 71
Cdd:COG1010     2 MRGKLYVVGLGPGSAELMTPRARAALAEADVVV-------GYGTYLDLIPPLLPGKEvhasgmreEVeRARE-------- 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437643405  72 ekeaawdgiATELiqaVEAGQRVGFITLGDAMLF--STWVF-LLQRigSPAW----LEIVPGVTSFAAIAARAQTPL 141
Cdd:COG1010    67 ---------ALEL---AAEGKTVAVVSSGDPGVYgmAGLVLeVLEE--GGAWrdveVEVVPGITAAQAAAARLGAPL 129
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
11-229 1.92e-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: 55.58  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  11 GPGAADLVTVRAARLLATLDVLYApaGRRggdslALSIVREYLTPQTEIRcrhfpmsgdsaekeaaWDGIATELIQAVEA 90
Cdd:cd11644     4 GPGGPEYLTPEAREAIEEADVVIG--AKR-----LLELFPDLGAEKIPLP----------------SEDIAELLEEIAEA 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  91 GQRVGFITLGDAMLFSTWVFLLQRIGSPAwLEIVPGVTSFAAIAARAQTPLameqQSLAVI-ACTAPEAEIIQALQQHDS 169
Cdd:cd11644    61 GKRVVVLASGDPGFYGIGKTLLRRLGGEE-VEVIPGISSVQLAAARLGLPW----EDARLVsLHGRDLENLRRALRRGRK 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437643405 170 LVlmkVY--GRF--ARIKALLAQAGLLECALMMAEA-TLPGERCWRHLDEVDEEQPLAYFSTILV 229
Cdd:cd11644   136 VF---VLtdGKNtpAEIARLLLERGLGDSRVTVGENlGYPDERITEGTAEELAEEEFSDLNVVLI 197
Precorrin-6A-synthase cd11643
Precorrin-6A synthase (also named CobF); Precorrin-6A synthase participates in the pathway ...
11-141 2.58e-09

Precorrin-6A synthase (also named CobF); Precorrin-6A synthase 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. This model represents CobF, the precorrin-6A synthase, an enzyme specific to the aerobic pathway. After precorrin-4 is methylated at C-11 by CobM to produce precorrin-5, CobF catalyzes the removal of the extruded acyl group in the subsequent step, and the addition of a methyl group at C-1. The product of this reaction is precorrin-6A, which gets reduced by an NADH-dependent reductase to yield precorrin-6B. This family includes enzymes in GC-rich Gram-positive bacteria, alpha proteobacteria and Pseudomonas-related species.


Pssm-ID: 381170  Cd Length: 244  Bit Score: 55.97  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  11 GPGAADLVTVRAARLLATLDVLYAPA-GRRGGDSLAL--SIVREYLTPQTeIRCRHFPM------SGDSAEKEAAW-DGI 80
Cdd:cd11643     5 GPGDPDHLTLQAIEALNRVDVFFVLDkGEEKSDLAALrrEICERHLGDRP-YRVVEFPDperdrsPADYRAAVADWhDAR 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437643405  81 A---TELIQA-VEAGQRVGFITLGDAMLF-STwVFLLQRI---GSPAWLEIVPGVTSFAAIAARAQTPL 141
Cdd:cd11643    84 AalwEDAIAEeLPEGGTGAFLVWGDPSLYdST-LRILDRLragRVALEVEVIPGISSVQALAARHRIPL 151
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
5-142 6.54e-08

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: 51.65  E-value: 6.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   5 LYALSTGPGAADLVTVRAARLLATLDVLYapagrrgGDSLALSIVREYLTPQTEIRcrhfpmSGDSAEKEAawdgiATEL 84
Cdd:cd11646     1 LYVVGIGPGSADLMTPRAREALEEADVIV-------GYKTYLDLIEDLLPGKEVIS------SGMGEEVER-----AREA 62
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437643405  85 IQAVEAGQRVGFITLGDAMLF--STWVF-LLQRIGSPAWLEIVPGVTSFAAIAARAQTPLA 142
Cdd:cd11646    63 LELALEGKRVALVSSGDPGIYgmAGLVLeLLDERWDDIEVEVVPGITAALAAAALLGAPLG 123
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
5-141 1.53e-05

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: 44.60  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   5 LYALSTGPGAADLVTVRAARLLATLDVLYapagrrgGDSLALSIVREYLTPQTEIRCrhfPMSGDSAEKEAAwdgiatel 84
Cdd:TIGR01466   1 LYVVGIGPGAEELMTPEAKEALAEADVIV-------GYKTYLDLIEDLIPGKEVVTS---GMREEIARAELA-------- 62
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  85 IQAVEAGQRVGFITLGDAMLF--STWVF-LLQRIGSPAWLEIVPGVTSFAAIAARAQTPL 141
Cdd:TIGR01466  63 IELAAEGRTVALVSSGDPGIYgmAALVFeALEKKGAEVDIEVIPGITAASAAASLLGAPL 122
PRK07168 PRK07168
uroporphyrin-III C-methyltransferase;
1-154 1.87e-05

uroporphyrin-III C-methyltransferase;


Pssm-ID: 180864 [Multi-domain]  Cd Length: 474  Bit Score: 44.98  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   1 MTGRLYALSTGPGAADLVTVRAARLLATLD-VLYapagrrggDSLALSIVREYLTPQTE-IRCRHFPMSGDSAEkeaawD 78
Cdd:PRK07168    1 MNGYVYLVGAGPGDEGLITKKAIECLKRADiVLY--------DRLLNPFFLSYTKQTCElMYCGKMPKNHIMRQ-----E 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  79 GIATELIQAVEAGQRVGFITLGDAMLFStwvfllqRIGSPAW--------LEIVPGVTSFAAIAARAQTPLAMEQQSLAV 150
Cdd:PRK07168   68 MINAHLLQFAKEGKIVVRLKGGDPSIFG-------RVGEEAEtlaaanipYEIVPGITSSIAASSYAGIPLTHRNYSNSV 140

                  ....
gi 1437643405 151 IACT 154
Cdd:PRK07168  141 TLLT 144
PRK05765 PRK05765
precorrin-3B C17-methyltransferase; Provisional
3-161 3.51e-05

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 235597  Cd Length: 246  Bit Score: 43.62  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   3 GRLYALSTGPGAADLVTVRAARLLATLDVLYapagrrgGDSLALSIVREYLTPQTEIRCRhfpMSGDSAEKEAAwdgiat 82
Cdd:PRK05765    2 GKLYIVGIGPGSKEQRTIKAQEAIEKSNVII-------GYNTYLRLISDLLDGKEVIGAR---MKEEIFRANTA------ 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405  83 eLIQAVEaGQRVGFITLGDAMLF--STWVF-LLQRIGSPAWLEIVPGVTSFAAIAARAQTPLAMEQQSLAVIACTAPEAE 159
Cdd:PRK05765   66 -IEKALE-GNIVALVSSGDPQVYgmAGLVFeLISRRKLDVDVEVIPGVTAALAAAARLGSPLSLDFVVISLSDLLIPREE 143

                  ..
gi 1437643405 160 II 161
Cdd:PRK05765  144 IL 145
PRK05991 PRK05991
precorrin-3B C17-methyltransferase; Provisional
1-141 5.07e-05

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 180342 [Multi-domain]  Cd Length: 250  Bit Score: 43.20  E-value: 5.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437643405   1 MTGRLYALSTGPGAADLVTVRAARLLATLDVL--YAPagrrggdslalsivreYLTPQTEIRCRHFPMSGDSAEKEAAWD 78
Cdd:PRK05991    1 MSGRLFVIGTGPGNPEQMTPEALAAVEAATDFfgYGP----------------YLDRLPLRADQLRHASDNREELDRAGA 64
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437643405  79 GIAteliqAVEAGQRVGFITLGDAMLFSTWVFLLQRI--GSPAW----LEIVPGVTSFAAIAARAQTPL 141
Cdd:PRK05991   65 ALA-----MAAAGANVCVVSGGDPGVFAMAAAVCEAIenGPAAWravdLTIVPGVTAMLAVAARIGAPL 128
 
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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