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Conserved domains on  [gi|499659424|ref|WP_011340158|]
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precorrin-6y C5,15-methyltransferase (decarboxylating) subunit CbiE [Syntrophotalea carbinolica]

Protein Classification

cobalt-precorrin-7 (C(5))-methyltransferase( domain architecture ID 10184509)

cobalt-precorrin-7 (C(5))-methyltransferase CbiE, together with CbiT, catalyzes two methylations (at C-5 and C-15) in cobalt-precorrin-6B and its decarboxylation, via cobalt-precorrin-7, to produce cobalt-precorrin-8X as part of the anaerobic-route biosynthesis of cobalamin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
 11-206 8.21e-61

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: 188.47  E-value: 8.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  11 VGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPEAKGKRVVVGA-DIAAALEFMDTHIGHTpmVVLVTGDPGMHSLA 89
Cdd:cd11644    1 IGIGPGGPEYLTPEAREAIEEADVVIGAKRLLELFPDLGAEKIPLPSeDIAELLEEIAEAGKRV--VVLASGDPGFYGIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  90 RPVVRHFGRKLCRIIPGISSVQAAFAAAGLDWMDARILSAHGALPDIDHSELDTVDKIAVLAGSPAALRWIAA--LAEHL 167
Cdd:cd11644   79 KTLLRRLGGEEVEVIPGISSVQLAAARLGLPWEDARLVSLHGRDLENLRRALRRGRKVFVLTDGKNTPAEIARllLERGL 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 499659424 168 APRWVLVCEELTLPGETVTQVTASDLVTMQASSRTVVLL 206
Cdd:cd11644  159 GDSRVTVGENLGYPDERITEGTAEELAEEEFSDLNVVLI 197
 
Name Accession Description Interval E-value
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
 11-206 8.21e-61

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: 188.47  E-value: 8.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  11 VGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPEAKGKRVVVGA-DIAAALEFMDTHIGHTpmVVLVTGDPGMHSLA 89
Cdd:cd11644    1 IGIGPGGPEYLTPEAREAIEEADVVIGAKRLLELFPDLGAEKIPLPSeDIAELLEEIAEAGKRV--VVLASGDPGFYGIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  90 RPVVRHFGRKLCRIIPGISSVQAAFAAAGLDWMDARILSAHGALPDIDHSELDTVDKIAVLAGSPAALRWIAA--LAEHL 167
Cdd:cd11644   79 KTLLRRLGGEEVEVIPGISSVQLAAARLGLPWEDARLVSLHGRDLENLRRALRRGRKVFVLTDGKNTPAEIARllLERGL 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 499659424 168 APRWVLVCEELTLPGETVTQVTASDLVTMQASSRTVVLL 206
Cdd:cd11644  159 GDSRVTVGENLGYPDERITEGTAEELAEEEFSDLNVVLI 197
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
 5-206 1.23e-57

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: 180.73  E-value: 1.23e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   5 DQPITIVGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPEAKGKRVVVGADIAAALEFMDTHIGHTPMVVLVTGDPG 84
Cdd:COG2241    1 MPWLTVVGIGPGGPDGLTPAAREAIAEADVVVGGKRHLELFPDLGAERIVWPSPLSELLEELLALLRGRRVVVLASGDPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  85 MHSLARPVVRHFGRKLCRIIPGISSVQAAFAAAGLDWMDARILSAHGALPDIDHSELDTVDKIAVLAGSPAALRWIAA-L 163
Cdd:COG2241   81 FYGIGATLARHLPAEEVRVIPGISSLQLAAARLGWPWQDAAVVSLHGRPLERLLPALAPGRRVLVLTDDGNTPAAIARlL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 499659424 164 AEH-LAPRWVLVCEELTLPGETVTQVTASDLVTMQASSRTVVLL 206
Cdd:COG2241  161 LERgFGDSRLTVLENLGGPDERITRGTAEELADADFSDLNVVAI 204
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
7-208 3.68e-41

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


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 138.85  E-value: 3.68e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   7 PITIVGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPE-AKGKRVVVGADIAAALEFMDTHIGHTPMVVLVTGDPgM 85
Cdd:PRK05787   1 MIYIVGIGPGDPEYLTLKALEAIRKADVVVGSKRVLELFPElIDGEAFVLTAGLRDLLEWLELAAKGKNVVVLSTGDP-L 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  86 HS--LARPVVRHFGRKLCRIIPGISSVQAAFAAAGLDWMDARILSAHGALPDIDHSE--LDTVDKIAVLAGSPAALRWIA 161
Cdd:PRK05787  80 FSglGKLLKVRRAVAEDVEVIPGISSVQYAAARLGIDMNDVVFTTSHGRGPNFEELEdlLKNGRKVIMLPDPRFGPKEIA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 499659424 162 A-LAEHLAP-RWVLVCEELTLPGETVTQVTASDLVTMQASSRTVVLLVR 208
Cdd:PRK05787 160 AeLLERGKLeRRIVVGENLSYPDERIHKLTLSEIEPLEFSDMSVVVILD 208
CbiE TIGR02467
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ...
 10-206 1.93e-39

precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes the CbiE methylase which is responsible, in part (along with CbiT), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiT subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL.


Pssm-ID: 274146 [Multi-domain]  Cd Length: 204  Bit Score: 134.37  E-value: 1.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   10 IVGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPEAKGKRVVVG---ADIAAALEFMDTHIGHTPMVVLVTGDPGMH 86
Cdd:TIGR02467   1 VVGIGPGGPELLTPAAIEAIRKADLVVGGERHLELLAELIGEKREIIltyKDLDELLEFIAATRKEKRVVVLASGDPLFY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   87 SLARPVVRHFGRKLCRIIPGISSVQAAFAAAGLDWMDARILSAHGAlpDIDHSELD---TVDKIAVL---AGSPAALRWI 160
Cdd:TIGR02467  81 GIGRTLAERLGKERLEIIPGISSVQYAFARLGLPWQDAVVISLHGR--ELDELLLAllrGHRKVAVLtdpRNGPAEIARE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 499659424  161 aALAEHLAPRWVL-VCEELTLPGETVTQVTASDLVTMQASSRTVVLL 206
Cdd:TIGR02467 159 -LIELGIGGSYELtVGENLGYEDERITEGTLEEIAAAQFDFSPLLVV 204
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 8-193 9.88e-21

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: 85.86  E-value: 9.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424    8 ITIVGCGPGGSAYLTDAARQAVNRADILIGAN-----RLLALFPEA--------KGKRVVVGADIAAALeFMDTHIGHTP 74
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDsraleILLDLLPEDlyfpmtedKEPLEEAYEEIAEAL-AAALRAGKDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   75 mVVLVTGDPGMHSLARPVVRHFGRK--LCRIIPGISSVQAAFAAAGLDWMDARILSAHGALPDIDHSELDTVDKIA---- 148
Cdd:pfam00590  81 -ARLVSGDPLVYGTGSYLVEALRAAgiDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRLLEALLangd 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 499659424  149 --VLAGSPAALRWIA-ALAEHLAPRW-VLVCEELTLPGETVTQVTASDL 193
Cdd:pfam00590 160 tvVLLYGPRRLAELAeLLLELYPDTTpVAVVERAGTPDEKVVRGTLGEL 208
 
Name Accession Description Interval E-value
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
 11-206 8.21e-61

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: 188.47  E-value: 8.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  11 VGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPEAKGKRVVVGA-DIAAALEFMDTHIGHTpmVVLVTGDPGMHSLA 89
Cdd:cd11644    1 IGIGPGGPEYLTPEAREAIEEADVVIGAKRLLELFPDLGAEKIPLPSeDIAELLEEIAEAGKRV--VVLASGDPGFYGIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  90 RPVVRHFGRKLCRIIPGISSVQAAFAAAGLDWMDARILSAHGALPDIDHSELDTVDKIAVLAGSPAALRWIAA--LAEHL 167
Cdd:cd11644   79 KTLLRRLGGEEVEVIPGISSVQLAAARLGLPWEDARLVSLHGRDLENLRRALRRGRKVFVLTDGKNTPAEIARllLERGL 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 499659424 168 APRWVLVCEELTLPGETVTQVTASDLVTMQASSRTVVLL 206
Cdd:cd11644  159 GDSRVTVGENLGYPDERITEGTAEELAEEEFSDLNVVLI 197
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
 5-206 1.23e-57

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: 180.73  E-value: 1.23e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   5 DQPITIVGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPEAKGKRVVVGADIAAALEFMDTHIGHTPMVVLVTGDPG 84
Cdd:COG2241    1 MPWLTVVGIGPGGPDGLTPAAREAIAEADVVVGGKRHLELFPDLGAERIVWPSPLSELLEELLALLRGRRVVVLASGDPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  85 MHSLARPVVRHFGRKLCRIIPGISSVQAAFAAAGLDWMDARILSAHGALPDIDHSELDTVDKIAVLAGSPAALRWIAA-L 163
Cdd:COG2241   81 FYGIGATLARHLPAEEVRVIPGISSLQLAAARLGWPWQDAAVVSLHGRPLERLLPALAPGRRVLVLTDDGNTPAAIARlL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 499659424 164 AEH-LAPRWVLVCEELTLPGETVTQVTASDLVTMQASSRTVVLL 206
Cdd:COG2241  161 LERgFGDSRLTVLENLGGPDERITRGTAEELADADFSDLNVVAI 204
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
7-208 3.68e-41

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


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 138.85  E-value: 3.68e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   7 PITIVGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPE-AKGKRVVVGADIAAALEFMDTHIGHTPMVVLVTGDPgM 85
Cdd:PRK05787   1 MIYIVGIGPGDPEYLTLKALEAIRKADVVVGSKRVLELFPElIDGEAFVLTAGLRDLLEWLELAAKGKNVVVLSTGDP-L 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  86 HS--LARPVVRHFGRKLCRIIPGISSVQAAFAAAGLDWMDARILSAHGALPDIDHSE--LDTVDKIAVLAGSPAALRWIA 161
Cdd:PRK05787  80 FSglGKLLKVRRAVAEDVEVIPGISSVQYAAARLGIDMNDVVFTTSHGRGPNFEELEdlLKNGRKVIMLPDPRFGPKEIA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 499659424 162 A-LAEHLAP-RWVLVCEELTLPGETVTQVTASDLVTMQASSRTVVLLVR 208
Cdd:PRK05787 160 AeLLERGKLeRRIVVGENLSYPDERIHKLTLSEIEPLEFSDMSVVVILD 208
CbiE TIGR02467
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ...
 10-206 1.93e-39

precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes the CbiE methylase which is responsible, in part (along with CbiT), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiT subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL.


Pssm-ID: 274146 [Multi-domain]  Cd Length: 204  Bit Score: 134.37  E-value: 1.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   10 IVGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPEAKGKRVVVG---ADIAAALEFMDTHIGHTPMVVLVTGDPGMH 86
Cdd:TIGR02467   1 VVGIGPGGPELLTPAAIEAIRKADLVVGGERHLELLAELIGEKREIIltyKDLDELLEFIAATRKEKRVVVLASGDPLFY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   87 SLARPVVRHFGRKLCRIIPGISSVQAAFAAAGLDWMDARILSAHGAlpDIDHSELD---TVDKIAVL---AGSPAALRWI 160
Cdd:TIGR02467  81 GIGRTLAERLGKERLEIIPGISSVQYAFARLGLPWQDAVVISLHGR--ELDELLLAllrGHRKVAVLtdpRNGPAEIARE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 499659424  161 aALAEHLAPRWVL-VCEELTLPGETVTQVTASDLVTMQASSRTVVLL 206
Cdd:TIGR02467 159 -LIELGIGGSYELtVGENLGYEDERITEGTLEEIAAAQFDFSPLLVV 204
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 8-193 9.88e-21

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: 85.86  E-value: 9.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424    8 ITIVGCGPGGSAYLTDAARQAVNRADILIGAN-----RLLALFPEA--------KGKRVVVGADIAAALeFMDTHIGHTP 74
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDsraleILLDLLPEDlyfpmtedKEPLEEAYEEIAEAL-AAALRAGKDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   75 mVVLVTGDPGMHSLARPVVRHFGRK--LCRIIPGISSVQAAFAAAGLDWMDARILSAHGALPDIDHSELDTVDKIA---- 148
Cdd:pfam00590  81 -ARLVSGDPLVYGTGSYLVEALRAAgiDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRLLEALLangd 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 499659424  149 --VLAGSPAALRWIA-ALAEHLAPRW-VLVCEELTLPGETVTQVTASDL 193
Cdd:pfam00590 160 tvVLLYGPRRLAELAeLLLELYPDTTpVAVVERAGTPDEKVVRGTLGEL 208
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
 8-118 1.35e-12

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: 64.36  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   8 ITIVGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPE-AKGKRVVV---GADIA---AALEFMDThiGHTpmVVLV- 79
Cdd:cd11646    1 LYVVGIGPGSADLMTPRAREALEEADVIVGYKTYLDLIEDlLPGKEVISsgmGEEVErarEALELALE--GKR--VALVs 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499659424  80 TGDPG---MHSLARPVVRHFGRKLC-RIIPGISSVQAAFAAAG 118
Cdd:cd11646   77 SGDPGiygMAGLVLELLDERWDDIEvEVVPGITAALAAAALLG 119
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
 8-118 1.17e-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: 59.31  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   8 ITIVGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPE-AKGKRVV-----VGAD-----IAAALEfmdthiGHTpmV 76
Cdd:COG1010    6 LYVVGLGPGSAELMTPRARAALAEADVVVGYGTYLDLIPPlLPGKEVHasgmrEEVErareaLELAAE------GKT--V 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 499659424  77 VLV-TGDPG---MHSLARPVVRHFGRKL---CRIIPGISSVQAAFAAAG 118
Cdd:COG1010   78 AVVsSGDPGvygMAGLVLEVLEEGGAWRdveVEVVPGITAAQAAAARLG 126
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
 8-206 2.65e-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: 58.08  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424    8 ITIVGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPEAKGKRVVVGADIAAALEFMDTHI-----GHTpmVVLVT-G 81
Cdd:TIGR01466   1 LYVVGIGPGAEELMTPEAKEALAEADVIVGYKTYLDLIEDLIPGKEVVTSGMREEIARAELAIelaaeGRT--VALVSsG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   82 DPGMHSLARPV----VRHFGRKLCRIIPGISSVQAAFAAAG------------------LDWMDARILSAHGAlpdidhs 139
Cdd:TIGR01466  79 DPGIYGMAALVfealEKKGAEVDIEVIPGITAASAAASLLGaplghdfcvislsdlltpWPEIEKRLRAAAEA------- 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499659424  140 elDTVdkIAVLAGSPAALRW--IAA---LAEHLAP-RWVLVCEELTLPGETVTQVTASDLVTMQASSRTVVLL 206
Cdd:TIGR01466 152 --DFV--IAIYNPRSKRRPEqfRRAmeiLLEHRKPdTPVGIVRNAGREGEEVEITTLAELDEELIDMLTTVII 220
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 11-193 2.59e-08

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: 52.40  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  11 VGCGPGGSAYLTDAARQAVNRADILIGANRLLAL------FPEAKGKRVVVGADIAAALEFMDTHI----GHTPMVVLVT 80
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLlslvlrAILKDGKRIYDLHDPNVEEEMAELLLeearQGKDVAFLSP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  81 GDPGMHSLARPVVRHFGRK--LCRIIPGISSVQAAFAAAGLDWMDA-RILSAHGALPDIDHSELDTVDKI----AVLAGS 153
Cdd:cd09815   81 GDPGVAGTGAELVERAEREgvEVKVIPGVSAADAAAAALGIDLGESfLFVTASDLLENPRLLVLKALAKErrhlVLFLDG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 499659424 154 PAALRWIAALAEHLAPRWVLVC--EELTLPGETVTQVTASDL 193
Cdd:cd09815  161 HRFLKALERLLKELGEDDTPVVlvANAGSEGEVIRTGTVKEL 202
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
 11-186 4.17e-08

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: 51.74  E-value: 4.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  11 VGCGPGGSAYLTDAARQAVNRADILIganrllalFPEAKGKRVVVGADIAAALEFMDTHIG--HTPM------------- 75
Cdd:cd11645    1 VGVGPGDPELLTLKAVRILKEADVIF--------VPVSKGGEGSAALIIAAALLIPDKEIIplEFPMtkdreeleeawde 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  76 --------------VVLVT-GDPGMHS----LARpVVRHFGRKlCRIIPGISSVQAAFAAAG--LDWMDAR--ILSAHGA 132
Cdd:cd11645   73 aaeeiaeelkegkdVAFLTlGDPSLYStfsyLLE-RLRAPGVE-VEIIPGITSFSAAAARLGipLAEGDESlaILPATYD 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499659424 133 LPDIDHsELDTVDKIAVLAGSPAALRWIAALAEH-LAPRWVLVcEELTLPGETVT 186
Cdd:cd11645  151 EEELEK-ALENFDTVVLMKVGRNLEEIKELLEELgLLDKAVYV-ERCGMEGERIY 203
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
 8-186 8.32e-08

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: 50.87  E-value: 8.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   8 ITIVGCGPGGSAYLTDAARQAVNRADIL--------------------IGANRLLAL-FPEAKGKRVVVG------ADIA 60
Cdd:COG2243    5 LYGVGVGPGDPELLTLKAVRALREADVIaypakgagkaslareivapyLPPARIVELvFPMTTDYEALVAawdeaaARIA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  61 AALEfmdthIGHTpmVVLVT-GDPG-----MHSLARPVVRHFGrklCRIIPGISSVQAAFAAAG--LDWMDAR--ILSAH 130
Cdd:COG2243   85 EELE-----AGRD--VAFLTeGDPSlystfMYLLERLRERGFE---VEVIPGITSFSAAAAALGipLAEGDEPltVLPGT 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499659424 131 GALPDIDHsELDTVDKIAVLAGSPAALRWIAALAEHLAPRWVLVCEELTLPGETVT 186
Cdd:COG2243  155 LLEEELER-ALDDFDTVVIMKVGRNFPKVREALEEAGLLDRAWYVERAGMPDERIV 209
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
 10-116 9.96e-08

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: 50.63  E-value: 9.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  10 IVGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPEA-KGKRVVVG------------------ADIAAALEFMDTHI 70
Cdd:cd11724    4 LVGVGPGDPDLITLRALKAIKKADVVFAPPDLRKRFAEYlAGKEVLDDphglftyygkkcspleeaEKECEELEKQRAEI 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499659424  71 ----------GHTpMVVLVTGDPGMHSLARPVVRHFGRKLCRIIPGISSVQAAFAA 116
Cdd:cd11724   84 vqkirealaqGKN-VALLDSGDPTIYGPWIWYLEEFADLNPEVIPGVSSFNAANAA 138
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
 11-194 4.11e-06

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: 45.89  E-value: 4.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  11 VGCGPGGSAYLTDAARQAVNRADILI----GANRLLALFPeAKGKRVVVG----------ADI-----AAALEfmdthiG 71
Cdd:cd11642    1 VGAGPGDPDLLTLKALRALQQADVVLydrlVSPEILALAP-PGAELIYVGkrpgrhsvpqEEInellvELARE------G 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  72 HTpmVV-LVTGDPGMhslarpvvrhFGR------KL------CRIIPGISSVQAAFAAAGL-----DWMDA-RILSAH-- 130
Cdd:cd11642   74 KR--VVrLKGGDPFV----------FGRggeeieALreagipFEVVPGITSAIAAAAYAGIplthrGVASSvTFVTGHea 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499659424 131 -GALPDIDHSELDTVDKIAVLAGSPAALRWIAALAEH-LAPRW-VLVCEELTLPGETVTQVTASDLV 194
Cdd:cd11642  142 dGKLPDDDAALARPGGTLVIYMGVSNLEEIAERLIAAgLPPDTpVAIVENATTPDQRVVVGTLAELA 208
PRK05765 PRK05765
precorrin-3B C17-methyltransferase; Provisional
 8-117 1.27e-05

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 235597  Cd Length: 246  Bit Score: 44.77  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   8 ITIVGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPEAKGKRVVVGAD-----------IAAALEfmdthiGHTpmV 76
Cdd:PRK05765   4 LYIVGIGPGSKEQRTIKAQEAIEKSNVIIGYNTYLRLISDLLDGKEVIGARmkeeifrantaIEKALE------GNI--V 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499659424  77 VLVT-GDPGMHSLARPVVRHFGRKLC----RIIPGissVQAAFAAA 117
Cdd:PRK05765  76 ALVSsGDPQVYGMAGLVFELISRRKLdvdvEVIPG---VTAALAAA 118
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
 8-118 9.80e-05

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: 41.93  E-value: 9.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424    8 ITIVGCGPGGSAYLTDAARQAVNRADILIGANRLLA--LFPEAKGKRVVV---GADIAAALEFMDTHIGHTPMVV-LVTG 81
Cdd:TIGR01465   1 VYFIGAGPGDPDLITVKGRKLIESADVILYAGSLVPpeLLAHCRPGAEVVnsaGMSLEEIVDIMSDAHREGKDVArLHSG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 499659424   82 DPGMHSLARPVVRHFGRK--LCRIIPGISSVQAAFAAAG 118
Cdd:TIGR01465  81 DPSIYGAIAEQMRLLEALgiPYEVVPGVSSFFAAAAALG 119
cbiH PRK15478
precorrin-3B C(17)-methyltransferase;
8-119 5.69e-04

precorrin-3B C(17)-methyltransferase;


Pssm-ID: 185375 [Multi-domain]  Cd Length: 241  Bit Score: 39.87  E-value: 5.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   8 ITIVGCGPGGSAYLTDAARQAVNRADILIGANRLLALFPEAKGKRVVVGADIAAALEFMDTHI-----GHTpMVVLVTGD 82
Cdd:PRK15478   2 LSVIGIGPGSQAMMTMEAIEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIelaqaGHN-VALISSGD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499659424  83 PGMHSLARPVVRHFGRKLC----RIIPGISsvqAAFAAAGL 119
Cdd:PRK15478  81 AGIYGMAGLVLELVSKQKLdvevRLIPGMT---ASIAAASL 118
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
 11-118 9.97e-04

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: 38.91  E-value: 9.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  11 VGCGPGGSAYLTDAARQAVNRADILIGANRLL--ALFPEAKGKRVVV---GADIAAALEFMDTHIGHTPMVV-LVTGDPG 84
Cdd:cd11641    1 VGAGPGDPELITVKGARLLEEADVVIYAGSLVppELLAYAKPGAEIVdsaGMTLEEIIEVMREAAREGKDVVrLHTGDPS 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499659424  85 MHSLARPVVRHFgRKL---CRIIPGISSVQAAFAAAG 118
Cdd:cd11641   81 LYGAIREQIDAL-DKLgipYEVVPGVSSFFAAAAALG 116
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
11-186 1.98e-03

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 37.97  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  11 VGCGPGGSAYLTDAARQAVNRADILI-----GANRLLAL-----------------FPEAKGKRVVVGADIAAAlEFMDT 68
Cdd:PRK05576   7 IGLGPGDPELLTVKAARILEEADVVYapasrKGGGSLALnivrpylkeeteivelhFPMSKDEEEKEAVWKENA-EEIAA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424  69 HI--GHTpmVVLVT-GDPGMHS----LaRPVVRHFGRKlCRIIPGISSVQAAFAAAG--LDWMDARILSAHGALPDIDHS 139
Cdd:PRK05576  86 EAeeGKN--VAFITlGDPNLYStfshL-LEYLKCHDIE-VETVPGISSFTAIASRAGvpLAMGDESLAIIPATREALIEQ 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 499659424 140 ELDTVDKIAVL-AGSPAALrwIAALAEHLAPRWVLVcEELTLPGETVT 186
Cdd:PRK05576 162 ALTDFDSVVLMkVYKNFAL--IEELLEEGYLDALYV-RRAYMEGEQIL 206
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
 8-118 2.44e-03

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: 37.75  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499659424   8 ITIVGCGPGGSAYLTDAARQAVNRADILI----GANRLLALFPEAKgKRVVVG----------ADI-----AAALEfmdt 68
Cdd:COG0007    4 VYLVGAGPGDPDLLTLKALRALQQADVVLydrlVSPEILALARPDA-ELIYVGkrggrhslpqEEInallvELARA---- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499659424  69 hiGHTpmVV-LVTGDPGMhslarpvvrhFGRKL------------CRIIPGISSVQAAFAAAG 118
Cdd:COG0007   79 --GKR--VVrLKGGDPFV----------FGRGGeeaealaaagipFEVVPGITAAIAAPAYAG 127
 
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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