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Conserved domains on  [gi|16765359|ref|NP_460974|]
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synthesis of vitamin B12 adenosyl cobalamide precursor [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

Protein Classification

cobalt-precorrin-4/precorrin-4 C(11)-methyltransferase( domain architecture ID 10794173)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
1-257 0e+00

cobalt-precorrin-4 methyltransferase;


:

Pssm-ID: 185370  Cd Length: 257  Bit Score: 537.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    1 MSETFDPRCVWFVGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAERYDSAELHLEQIIELMAAGVKAG 80
Cdd:PRK15473   1 MSETFDPRCVWFVGAGPGDKELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAECHDSAELHLEQIIDLMEAGVKAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   81 KTVVRLQTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLIITRLEGRTPVPAREQLEAF 160
Cdd:PRK15473  81 KTVVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIITRMEGRTPVPAREQLESF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  161 ASHQTSMAIYLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGNFLGKEY 240
Cdd:PRK15473 161 ASHQTSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVGNFLGEEY 240
                        250
                 ....*....|....*..
gi 16765359  241 HYSRLYAADFSHEYRKA 257
Cdd:PRK15473 241 HYSKLYDADFSHEYRKA 257
 
Name Accession Description Interval E-value
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
1-257 0e+00

cobalt-precorrin-4 methyltransferase;


Pssm-ID: 185370  Cd Length: 257  Bit Score: 537.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    1 MSETFDPRCVWFVGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAERYDSAELHLEQIIELMAAGVKAG 80
Cdd:PRK15473   1 MSETFDPRCVWFVGAGPGDKELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAECHDSAELHLEQIIDLMEAGVKAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   81 KTVVRLQTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLIITRLEGRTPVPAREQLEAF 160
Cdd:PRK15473  81 KTVVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIITRMEGRTPVPAREQLESF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  161 ASHQTSMAIYLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGNFLGKEY 240
Cdd:PRK15473 161 ASHQTSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVGNFLGEEY 240
                        250
                 ....*....|....*..
gi 16765359  241 HYSRLYAADFSHEYRKA 257
Cdd:PRK15473 241 HYSKLYDADFSHEYRKA 257
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
10-257 4.87e-153

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: 426.40  E-value: 4.87e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  10 VWFVGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAERYDSAELHLEQIIELMAAGVKAGKTVVRLQTG 89
Cdd:COG2875   5 VYFVGAGPGDPDLITVKGRRLLEEADVVLYAGSLVPPELLAYCKPGAEIVDSASMTLEEIIALMKEAAAEGKDVVRLHSG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  90 DVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLIITRLEGRTPVPAREQLEAFASHQTSMAI 169
Cdd:COG2875  85 DPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAEGRTPMPEGESLASLAAHGATLAI 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359 170 YLSVQRIHRVAERLIAgGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGNFLGKE-YHYSRLYAA 248
Cdd:COG2875 165 YLSAHRIDEVVEELLE-GYPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGPALGAEdFARSKLYDP 243

                ....*....
gi 16765359 249 DFSHEYRKA 257
Cdd:COG2875 244 GFSHGFRPA 252
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
13-237 1.70e-139

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: 390.60  E-value: 1.70e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  13 VGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAERYDSAELHLEQIIELMAAGVKAGKTVVRLQTGDVS 92
Cdd:cd11641   1 VGAGPGDPELITVKGARLLEEADVVIYAGSLVPPELLAYAKPGAEIVDSAGMTLEEIIEVMREAAREGKDVVRLHTGDPS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  93 LYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLIITRLEGRTPVPAREQLEAFASHQTSMAIYLS 172
Cdd:cd11641  81 LYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRLEGRTPVPEGESLRELAKHGATLAIFLS 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16765359 173 VQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGNFLG 237
Cdd:cd11641 161 AALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPALG 225
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
10-255 5.78e-119

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: 339.69  E-value: 5.78e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    10 VWFVGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAERYDSAELHLEQIIELMAAGVKAGKTVVRLQTG 89
Cdd:TIGR01465   1 VYFIGAGPGDPDLITVKGRKLIESADVILYAGSLVPPELLAHCRPGAEVVNSAGMSLEEIVDIMSDAHREGKDVARLHSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    90 DVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLIITRLEGRTPVPAREQLEAFASHQTSMAI 169
Cdd:TIGR01465  81 DPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGRTPMPEGEKLADLAKHGATMAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   170 YLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGNFLGKEYH-YSRLYAA 248
Cdd:TIGR01465 161 FLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPALDPRIGkRSKLYDP 240

                  ....*..
gi 16765359   249 DFSHEYR 255
Cdd:TIGR01465 241 DFSHSFR 247
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
10-215 2.35e-55

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: 176.76  E-value: 2.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    10 VWFVGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQ-----AERYDSAELHLEQIIELMAAGVKAGKTVV 84
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDlyfpmTEDKEPLEEAYEEIAEALAAALRAGKDVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    85 RLQTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLIITRlegRTPVPAREQLEAFASHQ 164
Cdd:pfam00590  82 RLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLP---GLARIELRLLEALLANG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16765359   165 TSMAIYLSVQRIHRVAERLIAgGYPATTPVAVIYKATWPESQTVRGTLADI 215
Cdd:pfam00590 159 DTVVLLYGPRRLAELAELLLE-LYPDTTPVAVVERAGTPDEKVVRGTLGEL 208
 
Name Accession Description Interval E-value
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
1-257 0e+00

cobalt-precorrin-4 methyltransferase;


Pssm-ID: 185370  Cd Length: 257  Bit Score: 537.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    1 MSETFDPRCVWFVGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAERYDSAELHLEQIIELMAAGVKAG 80
Cdd:PRK15473   1 MSETFDPRCVWFVGAGPGDKELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAECHDSAELHLEQIIDLMEAGVKAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   81 KTVVRLQTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLIITRLEGRTPVPAREQLEAF 160
Cdd:PRK15473  81 KTVVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIITRMEGRTPVPAREQLESF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  161 ASHQTSMAIYLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGNFLGKEY 240
Cdd:PRK15473 161 ASHQTSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVGNFLGEEY 240
                        250
                 ....*....|....*..
gi 16765359  241 HYSRLYAADFSHEYRKA 257
Cdd:PRK15473 241 HYSKLYDADFSHEYRKA 257
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
10-257 4.87e-153

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: 426.40  E-value: 4.87e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  10 VWFVGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAERYDSAELHLEQIIELMAAGVKAGKTVVRLQTG 89
Cdd:COG2875   5 VYFVGAGPGDPDLITVKGRRLLEEADVVLYAGSLVPPELLAYCKPGAEIVDSASMTLEEIIALMKEAAAEGKDVVRLHSG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  90 DVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLIITRLEGRTPVPAREQLEAFASHQTSMAI 169
Cdd:COG2875  85 DPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAEGRTPMPEGESLASLAAHGATLAI 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359 170 YLSVQRIHRVAERLIAgGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGNFLGKE-YHYSRLYAA 248
Cdd:COG2875 165 YLSAHRIDEVVEELLE-GYPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGPALGAEdFARSKLYDP 243

                ....*....
gi 16765359 249 DFSHEYRKA 257
Cdd:COG2875 244 GFSHGFRPA 252
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
13-237 1.70e-139

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: 390.60  E-value: 1.70e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  13 VGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAERYDSAELHLEQIIELMAAGVKAGKTVVRLQTGDVS 92
Cdd:cd11641   1 VGAGPGDPELITVKGARLLEEADVVIYAGSLVPPELLAYAKPGAEIVDSAGMTLEEIIEVMREAAREGKDVVRLHTGDPS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  93 LYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLIITRLEGRTPVPAREQLEAFASHQTSMAIYLS 172
Cdd:cd11641  81 LYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRLEGRTPVPEGESLRELAKHGATLAIFLS 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16765359 173 VQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGNFLG 237
Cdd:cd11641 161 AALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPALG 225
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
10-255 5.78e-119

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: 339.69  E-value: 5.78e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    10 VWFVGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAERYDSAELHLEQIIELMAAGVKAGKTVVRLQTG 89
Cdd:TIGR01465   1 VYFIGAGPGDPDLITVKGRKLIESADVILYAGSLVPPELLAHCRPGAEVVNSAGMSLEEIVDIMSDAHREGKDVARLHSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    90 DVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLIITRLEGRTPVPAREQLEAFASHQTSMAI 169
Cdd:TIGR01465  81 DPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGRTPMPEGEKLADLAKHGATMAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   170 YLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGNFLGKEYH-YSRLYAA 248
Cdd:TIGR01465 161 FLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPALDPRIGkRSKLYDP 240

                  ....*..
gi 16765359   249 DFSHEYR 255
Cdd:TIGR01465 241 DFSHSFR 247
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
13-234 5.67e-69

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: 212.30  E-value: 5.67e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  13 VGAGPGDRELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAERYD------SAELHLEQIIELMAAGVKAGKTVVRL 86
Cdd:cd11642   1 VGAGPGDPDLLTLKALRALQQADVVLY-DRLVSPEILALAPPGAELIYvgkrpgRHSVPQEEINELLVELAREGKRVVRL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  87 QTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLII---TRLEGRTPvparEQLEAFASH 163
Cdd:cd11642  80 KGGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFvtgHEADGKLP----DDDAALARP 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16765359 164 QTSMAIYLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGN 234
Cdd:cd11642 156 GGTLVIYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGE 226
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
10-233 1.99e-65

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: 203.77  E-value: 1.99e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  10 VWFVGAGPGDRELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAERYD------SAELHLEQIIELMAAGVKAGKTV 83
Cdd:COG0007   4 VYLVGAGPGDPDLLTLKALRALQQADVVLY-DRLVSPEILALARPDAELIYvgkrggRHSLPQEEINALLVELARAGKRV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  84 VRLQTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSL-IITrleGRTPVPAREQ-LEAFA 161
Cdd:COG0007  83 VRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVtFVT---GHEKDGKLDLdWAALA 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16765359 162 SHQTSMAIYLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVG 233
Cdd:COG0007 160 RPGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVG 231
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
10-215 2.35e-55

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: 176.76  E-value: 2.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    10 VWFVGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQ-----AERYDSAELHLEQIIELMAAGVKAGKTVV 84
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDlyfpmTEDKEPLEEAYEEIAEALAAALRAGKDVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    85 RLQTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLIITRlegRTPVPAREQLEAFASHQ 164
Cdd:pfam00590  82 RLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLP---GLARIELRLLEALLANG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16765359   165 TSMAIYLSVQRIHRVAERLIAgGYPATTPVAVIYKATWPESQTVRGTLADI 215
Cdd:pfam00590 159 DTVVLLYGPRRLAELAELLLE-LYPDTTPVAVVERAGTPDEKVVRGTLGEL 208
cobA_cysG_Cterm TIGR01469
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ...
10-234 1.49e-54

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


Pssm-ID: 273643  Cd Length: 236  Bit Score: 175.49  E-value: 1.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    10 VWFVGAGPGDRELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAERYDSAELHL------EQIIELMAAGVKAGKTV 83
Cdd:TIGR01469   2 VYLVGAGPGDPELLTLKALRLLQEADVVLY-DALVSPEILAYAPPQAELIDVGKRPGchskkqEEINRLLVELAREGKKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    84 VRLQTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSL-IITrleGRTPVPAREQL--EAF 160
Cdd:TIGR01469  81 VRLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVtFVT---GHEADDKALEVdwEAL 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16765359   161 ASHQTSMAIYLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGN 234
Cdd:TIGR01469 158 AKGAGTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGE 231
PRK06136 PRK06136
uroporphyrinogen-III C-methyltransferase;
10-234 6.72e-54

uroporphyrinogen-III C-methyltransferase;


Pssm-ID: 235711  Cd Length: 249  Bit Score: 174.25  E-value: 6.72e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   10 VWFVGAGPGDRELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAE------RYDSAELHLEQIIELMAAGVKAGKTV 83
Cdd:PRK06136   5 VYLVGAGPGDPDLITLKGVRLLEQADVVLY-DDLVSPEILAYAKPDAEliyvgkRAGRHSTKQEEINRLLVDYARKGKVV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   84 VRLQTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLI-ITRLEGRTPVPAREQLEAFAS 162
Cdd:PRK06136  84 VRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTfVTGHEAAGKLEPEVNWSALAD 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16765359  163 HQTSMAIYLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGN 234
Cdd:PRK06136 164 GADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIQSPAIIVIGE 235
PLN02625 PLN02625
uroporphyrin-III C-methyltransferase
10-234 3.80e-53

uroporphyrin-III C-methyltransferase


Pssm-ID: 178232 [Multi-domain]  Cd Length: 263  Bit Score: 172.89  E-value: 3.80e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   10 VWFVGAGPGDRELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAE------RYDSAELHLEQIIELMAAGVKAGKTV 83
Cdd:PLN02625  17 VFLVGTGPGDPDLLTLKALRLLQTADVVLY-DRLVSPDILDLVPPGAEllyvgkRGGYHSRTQEEIHELLLSFAEAGKTV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   84 VRLQTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLIITRLEGRT-PVPAREQLEAFAS 162
Cdd:PLN02625  96 VRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRFLTGHDREgGTDPLDVAEAAAD 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16765359  163 HQTSMAIYLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGN 234
Cdd:PLN02625 176 PDTTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAGLVSPTVIVVGE 247
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
12-233 5.66e-39

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: 135.76  E-value: 5.66e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  12 FVGAGPGDRELITLKGYRLLQQAQVVI-------------------YAGSLINTELLDYCPAQAERYDSAELH---LEQI 69
Cdd:cd11724   4 LVGVGPGDPDLITLRALKAIKKADVVFappdlrkrfaeylagkevlDDPHGLFTYYGKKCSPLEEAEKECEELekqRAEI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  70 IELMAAGVKAGKTVVRLQTGDVSLYGSVREQGEELTRRGIdwQVVPGVSAFLGAAAELGVEYTVPEVSQSLIITrlEGRT 149
Cdd:cd11724  84 VQKIREALAQGKNVALLDSGDPTIYGPWIWYLEEFADLNP--EVIPGVSSFNAANAALKRSLTGGGDSRSVILT--APFA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359 150 PVPAREQLEAFASHQTSMAIYLSVQRIHRVAERLiAGGYPATTPVAVIYKATWPESQTV-RGTLADISDKVRDAGIRKTA 228
Cdd:cd11724 160 LKENEDLLEDLAATGDTLVIFMMRLDLDELVEKL-KKHYPPDTPVAIVYHAGYSEKEKViRGTLDDILEKLGGEKEPFLG 238

                ....*
gi 16765359 229 LILVG 233
Cdd:cd11724 239 LIYVG 243
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
13-233 6.36e-32

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: 116.72  E-value: 6.36e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  13 VGAGPGDRELITLKGYRLLQQAQVVIYAGS---LINTELLDYCPAQAERYD-SAELHLEQIIELMAAGVKAGKTVVRLQT 88
Cdd:cd09815   1 VGVGPGDPDLLTLRALEILRAADVVVAEDKdskLLSLVLRAILKDGKRIYDlHDPNVEEEMAELLLEEARQGKDVAFLSP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  89 GDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVeytvpEVSQSLIITRLEGRTPVPAREQLEAFASHQTSMA 168
Cdd:cd09815  81 GDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGI-----DLGESFLFVTASDLLENPRLLVLKALAKERRHLV 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16765359 169 IYLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIsDKVRDAGIRKTALILVG 233
Cdd:cd09815 156 LFLDGHRFLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKEL-RAERTERGKPLTTILVG 219
PRK07168 PRK07168
uroporphyrin-III C-methyltransferase;
10-234 2.37e-31

uroporphyrin-III C-methyltransferase;


Pssm-ID: 180864 [Multi-domain]  Cd Length: 474  Bit Score: 120.48  E-value: 2.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   10 VWFVGAGPGDRELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAERYDSAELHLEQII--ELMAAGV----KAGKTV 83
Cdd:PRK07168   5 VYLVGAGPGDEGLITKKAIECLKRADIVLY-DRLLNPFFLSYTKQTCELMYCGKMPKNHIMrqEMINAHLlqfaKEGKIV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   84 VRLQTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSliITRLEGRTPVPAREQLEAFASH 163
Cdd:PRK07168  84 VRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNS--VTLLTGHAKGPLTDHGKYNSSH 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16765359  164 QT-SMAIYLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGIRKTALILVGN 234
Cdd:PRK07168 162 NSdTIAYYMGIKNLPTICENLRQAGKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSIVKNENISNPSMTIVGD 233
cysG PRK10637
siroheme synthase CysG;
1-237 1.71e-27

siroheme synthase CysG;


Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 109.46  E-value: 1.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    1 MSETFDPRC-VWFVGAGPGDRELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAERY---DSAELHL---EQIIELM 73
Cdd:PRK10637 208 FSEPLDHRGeVVLVGAGPGDAGLLTLKGLQQIQQADVVVY-DRLVSDDIMNLVRRDADRVfvgKRAGYHCvpqEEINQIL 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   74 AAGVKAGKTVVRLQTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSL-IITrleGRTPVP 152
Cdd:PRK10637 287 LREAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVrLVT---GHLKTG 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  153 AREQLEAFASHQTSMAIYLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAGirKTALILV 232
Cdd:PRK10637 364 GELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMPADMPVALVENGTSVTQRVVSGTLTQLGELAQQVN--SPSLIIV 441

                 ....*
gi 16765359  233 GNFLG 237
Cdd:PRK10637 442 GRVVG 446
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
13-219 2.26e-21

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: 89.10  E-value: 2.26e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  13 VGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAERYDSAEL----------------HLEQIIELMAAG 76
Cdd:cd11645   1 VGVGPGDPELLTLKAVRILKEADVIFVPVSKGGEGSAALIIAAALLIPDKEIiplefpmtkdreeleeAWDEAAEEIAEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  77 VKAGKTVVRLQTGDVSLYGS---VReqgEELTRRGIDWQVVPGVSAFLGAAAELGVEYTvpEVSQSLIItrlegrtpVPA 153
Cdd:cd11645  81 LKEGKDVAFLTLGDPSLYSTfsyLL---ERLRAPGVEVEIIPGITSFSAAAARLGIPLA--EGDESLAI--------LPA 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16765359 154 ---REQLEAFASHQTSMAIYLSVQRIHRVAERLIAGGYPATtpVAVIYKATWPESQTVRGTLADISDKV 219
Cdd:cd11645 148 tydEEELEKALENFDTVVLMKVGRNLEEIKELLEELGLLDK--AVYVERCGMEGERIYTDLEELKEEKL 214
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
10-218 2.77e-20

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: 86.31  E-value: 2.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  10 VWFVGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTE------LLDYCPAQAER---------YDSAELHLEQIIELMA 74
Cdd:COG2243   5 LYGVGVGPGDPELLTLKAVRALREADVIAYPAKGAGKAslareiVAPYLPPARIVelvfpmttdYEALVAAWDEAAARIA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  75 AGVKAGKTVVRLQTGDVSLYGS---VReqgEELTRRGIDWQVVPGVSAFLGAAAELGveytVP--EVSQSLIITrlegrt 149
Cdd:COG2243  85 EELEAGRDVAFLTEGDPSLYSTfmyLL---ERLRERGFEVEVIPGITSFSAAAAALG----IPlaEGDEPLTVL------ 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16765359 150 pvPAR---EQLEAFASHQTSMAIYLSVQRIHRVAERLIAGGYPATtpVAVIYKATWPESQTVRGtLADISDK 218
Cdd:COG2243 152 --PGTlleEELERALDDFDTVVIMKVGRNFPKVREALEEAGLLDR--AWYVERAGMPDERIVPG-LAEVDIE 218
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
13-218 1.20e-16

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: 75.61  E-value: 1.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  13 VGAGPGDRELITLKGYRLLQQAQVVIYAGSLIntELLDycPAQAERYdsaELHLEQIIELMAAGVKAGKTVVRLQTGDVS 92
Cdd:cd11644   1 IGIGPGGPEYLTPEAREAIEEADVVIGAKRLL--ELFP--DLGAEKI---PLPSEDIAELLEEIAEAGKRVVVLASGDPG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  93 LYGSvreqGEELTRR--GIDWQVVPGVSAFLGAAAELGVEYtvpevsQSLIITRLEGRTPVPAREQLEAFAshqtSMAIY 170
Cdd:cd11644  74 FYGI----GKTLLRRlgGEEVEVIPGISSVQLAAARLGLPW------EDARLVSLHGRDLENLRRALRRGR----KVFVL 139
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16765359 171 LS-VQRIHRVAERLIAGGYPATTpVAVIYKATWPESQTVRGTLADISDK 218
Cdd:cd11644 140 TDgKNTPAEIARLLLERGLGDSR-VTVGENLGYPDERITEGTAEELAEE 187
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
13-141 1.50e-15

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 73.41  E-value: 1.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   13 VGAGPGDRELITLKGYRLLQQAQVViYA-------GSLINTELLDYCPAQAER----------YDSAELHLEQIIELMAA 75
Cdd:PRK05576   7 IGLGPGDPELLTVKAARILEEADVV-YApasrkggGSLALNIVRPYLKEETEIvelhfpmskdEEEKEAVWKENAEEIAA 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16765359   76 GVKAGKTVVRLQTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELGVEYTVPEVSQSLI 141
Cdd:PRK05576  86 EAEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSFTAIASRAGVPLAMGDESLAII 151
PRK05990 PRK05990
precorrin-2 C(20)-methyltransferase; Reviewed
13-129 2.02e-14

precorrin-2 C(20)-methyltransferase; Reviewed


Pssm-ID: 180341  Cd Length: 241  Bit Score: 70.40  E-value: 2.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   13 VGAGPGDRELITLKGYRLLQQAQVVIY---AGSLIN-------------TELLDYCPAQAERyDSAELHLEQII------ 70
Cdd:PRK05990   8 LGVGPGDPELLTLKALRLLQAAPVVAYfvaKGKKGNafgiveahlspgqTLLPLVYPVTTEI-LPPPLCYETVIadfydt 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16765359   71 --ELMAAGVKAGKTVVRLQTGDVSLYGSVREQGEELTRRgIDWQVVPGVSAFLGAAAELGV 129
Cdd:PRK05990  87 saEAVAAHLDAGRDVAVICEGDPFFYGSYMYLHDRLAPR-YETEVIPGVCSMLGCWSVLGA 146
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
13-128 3.82e-13

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: 66.56  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    13 VGAGPGDRELITLKGYRLLQQAQVVIY------AGSLINTELLDYCPAQAER---------YDSAEL--HLEQIIELMAA 75
Cdd:TIGR01467   6 VGVGPGDPELITVKALEALRSADVIAVpaskkgRESLARKIVEDYLKPNDTRilelvfpmtKDRDELekAWDEAAEAVAA 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 16765359    76 GVKAGKTVVRLQTGDVSLYGSVREQGEELTRRGIDWQVVPGVSAFLGAAAELG 128
Cdd:TIGR01467  86 ELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAG 138
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
13-218 2.51e-12

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: 64.01  E-value: 2.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  13 VGAGPGDRELITLKGYRLLQQAQVVIyaGSLINTELLDYCPAQAERYDSAelhLEQIIELMAAGVkAGKTVVRLQTGDVS 92
Cdd:COG2241   7 VGIGPGGPDGLTPAAREAIAEADVVV--GGKRHLELFPDLGAERIVWPSP---LSELLEELLALL-RGRRVVVLASGDPL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  93 LYGSVREQGEELTRRgiDWQVVPGVSAFLGAAAELGVEYtvpevsQSLIITRLEGRTPvparEQLEAFASHQTSMAIYLS 172
Cdd:COG2241  81 FYGIGATLARHLPAE--EVRVIPGISSLQLAAARLGWPW------QDAAVVSLHGRPL----ERLLPALAPGRRVLVLTD 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 16765359 173 -VQRIHRVAERLIAGGYPATTpVAVIYKATWPESQTVRGTLADISDK 218
Cdd:COG2241 149 dGNTPAAIARLLLERGFGDSR-LTVLENLGGPDERITRGTAEELADA 194
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
13-234 3.52e-12

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: 64.32  E-value: 3.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  13 VGAGPGDRELITLKGYRLLQQAQVVI-YAGSLintELL-DYCPAQaERYDS--------AELHLEqiielMAAgvkAGKT 82
Cdd:COG1010   9 VGLGPGSAELMTPRARAALAEADVVVgYGTYL---DLIpPLLPGK-EVHASgmreeverAREALE-----LAA---EGKT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  83 VVRLQTGDVSLYG---SVREQGEELTR-RGIDWQVVPGVSAFLGAAAELGV----EYTVpeVSQS-------LIITRleg 147
Cdd:COG1010  77 VAVVSSGDPGVYGmagLVLEVLEEGGAwRDVEVEVVPGITAAQAAAARLGAplghDFCV--ISLSdlltpweVIEKR--- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359 148 rtpvpareqLEAFASHQTSMAIY--LSVQRIHRVAE--RLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKvrDAG 223
Cdd:COG1010 152 ---------LRAAAEADFVIALYnpRSRKRPWQLERalEILLEHRPPDTPVGIVRNAGRPDESVTVTTLGELDPE--EVD 220
                       250
                ....*....|.
gi 16765359 224 IRktALILVGN 234
Cdd:COG1010 221 ML--TTVIIGN 229
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
13-234 7.73e-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: 63.20  E-value: 7.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  13 VGAGPGDRELITLKGYRLLQQAQVVI-YAGSLintELLDYCPAQAERYDS--------AELHLEQiielmaagVKAGKTV 83
Cdd:cd11646   4 VGIGPGSADLMTPRAREALEEADVIVgYKTYL---DLIEDLLPGKEVISSgmgeeverAREALEL--------ALEGKRV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  84 VRLQTGDVSLYG---SVREQGEElTRRGIDWQVVPGVSAFLGAAAELGVEYT------------VPevsQSLIITRLEgr 148
Cdd:cd11646  73 ALVSSGDPGIYGmagLVLELLDE-RWDDIEVEVVPGITAALAAAALLGAPLGhdfavislsdllTP---WEVIEKRLR-- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359 149 tpvpareqleAFASHQTSMAIY--LSVQRIHRVAE--RLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKvrDAGI 224
Cdd:cd11646 147 ----------AAAEADFVIALYnpRSKKRPWQLEKalEILLEHRPPDTPVGIVRNAGREGEEVTITTLGELDPE--DVDM 214
                       250
                ....*....|
gi 16765359 225 RKTalILVGN 234
Cdd:cd11646 215 FTT--VIIGN 222
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
13-234 2.16e-11

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: 61.93  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    13 VGAGPGDRELITLKGYRLLQQAQVVI-YAG--SLINTELLDycpaqAERYDS--------AELHLEQiielmaagVKAGK 81
Cdd:TIGR01466   4 VGIGPGAEELMTPEAKEALAEADVIVgYKTylDLIEDLIPG-----KEVVTSgmreeiarAELAIEL--------AAEGR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359    82 TVVRLQTGDVSLYGSVREQGEELTRRGIDW--QVVPGVSAFLGAAAELGveytVPEVSQSLIITRLEGRTPVPAREQ-LE 158
Cdd:TIGR01466  71 TVALVSSGDPGIYGMAALVFEALEKKGAEVdiEVIPGITAASAAASLLG----APLGHDFCVISLSDLLTPWPEIEKrLR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   159 AFASHQTSMAIY--LSVQR---IHRVAERLIAgGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAgirkTALILVG 233
Cdd:TIGR01466 147 AAAEADFVIAIYnpRSKRRpeqFRRAMEILLE-HRKPDTPVGIVRNAGREGEEVEITTLAELDEELIDM----LTTVIIG 221

                  .
gi 16765359   234 N 234
Cdd:TIGR01466 222 N 222
PRK05948 PRK05948
precorrin-2 C(20)-methyltransferase;
11-142 2.82e-11

precorrin-2 C(20)-methyltransferase;


Pssm-ID: 180320  Cd Length: 238  Bit Score: 61.58  E-value: 2.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   11 WFVGAGPGDRELITLKGYRLLQQAQVVIYAGSLINTelldycPAQAERYDSAELHLEQII------------ELMAAGVK 78
Cdd:PRK05948   7 YGISVGPGDPELITLKGLRLLQSAPVVAFPAGLAGQ------PGLAEQIIAPWLSPQQIKlplyfpyvqdeeQLEQAWQA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16765359   79 A----------GKTVVRLQTGDVSLYGSVREQGEELTRR--GIDWQVVPGVSAFLGAAAELGVEYTVPevSQSLII 142
Cdd:PRK05948  81 AadqvwhyleqGEDVAFACEGDVSFYSTFTYLAQTLQELypQVAIQTIPGVCSPLAAAAALGIPLTLG--SQRLAI 154
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
10-217 3.38e-11

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


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 61.04  E-value: 3.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   10 VWFVGAGPGDRELITLKGYRLLQQAQVVIyaGSLINTELL-DYCPAQAERYDSAELHLEQIIELMAagvkAGKTVVRLQT 88
Cdd:PRK05787   2 IYIVGIGPGDPEYLTLKALEAIRKADVVV--GSKRVLELFpELIDGEAFVLTAGLRDLLEWLELAA----KGKNVVVLST 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   89 GDVSLYG-----SVREQGEEltrrgiDWQVVPGVSAFLGAAAELGVEYTvpevsqSLIITRLEGRTPVPaREQLEAFASH 163
Cdd:PRK05787  76 GDPLFSGlgkllKVRRAVAE------DVEVIPGISSVQYAAARLGIDMN------DVVFTTSHGRGPNF-EELEDLLKNG 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16765359  164 QTsmAIYLSVQRIH--RVAERLIAGGYPATTpVAVIYKATWPESQTVRGTLADISD 217
Cdd:PRK05787 143 RK--VIMLPDPRFGpkEIAAELLERGKLERR-IVVGENLSYPDERIHKLTLSEIEP 195
PRK05765 PRK05765
precorrin-3B C17-methyltransferase; Provisional
10-234 5.04e-08

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 235597  Cd Length: 246  Bit Score: 52.48  E-value: 5.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   10 VWFVGAGPGDRELITLKGYRLLQQAQVVI----YAGsLINtELLD---YCPAQA-ERYDSAELHLEQIIElmaagvkaGK 81
Cdd:PRK05765   4 LYIVGIGPGSKEQRTIKAQEAIEKSNVIIgyntYLR-LIS-DLLDgkeVIGARMkEEIFRANTAIEKALE--------GN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   82 TVVRLQTGDVSLYGSVREQGEELTRRGI--DWQVVPGVSAFLGAAAELG----VEYTVPEVSQSLiitrlegrtpVPARE 155
Cdd:PRK05765  74 IVALVSSGDPQVYGMAGLVFELISRRKLdvDVEVIPGVTAALAAAARLGsplsLDFVVISLSDLL----------IPREE 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359  156 QL---EAFASHQTSMAIYLSVQR-IHRVAERLIAGGYPATTPVAVIyKATWPESQTVRGTLADiSDKVRDAGIRKTALIL 231
Cdd:PRK05765 144 ILhrvTKAAEADFVIVFYNPINEnLLIEVMDIVSKHRKPNTPVGLV-KSAYRNNENVVITTLS-SWKEHMDEIGMTTTMI 221

                 ...
gi 16765359  232 VGN 234
Cdd:PRK05765 222 IGN 224
cbiH PRK15478
precorrin-3B C(17)-methyltransferase;
13-234 3.72e-04

precorrin-3B C(17)-methyltransferase;


Pssm-ID: 185375 [Multi-domain]  Cd Length: 241  Bit Score: 40.64  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   13 VGAGPGDRELITLKGYRLLQQAQVVIyaGSLINTELLDYCPAQAERYDSA---ELHLEQI-IELmaagVKAGKTVVRLQT 88
Cdd:PRK15478   5 IGIGPGSQAMMTMEAIEALQAAEIVV--GYKTYTHLVKAFTGDKQVIKTGmckEIERCQAaIEL----AQAGHNVALISS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765359   89 GDVSLYGSVREQGEELTRRGIDWQV--VPGVSAFLGAAAELGveytVPEVSQSLIITRLEGRTPVPAREQlEAFASHQTS 166
Cdd:PRK15478  79 GDAGIYGMAGLVLELVSKQKLDVEVrlIPGMTASIAAASLLG----APLMHDFCHISLSDLLTPWPVIEK-RIVAAGEAD 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16765359  167 MAIYL----SVQRIHRVAE--RLIAGGYPATTPVAVIYKATWPESQTVRGTLADISDKVRDAgirkTALILVGN 234
Cdd:PRK15478 154 FVICFynprSRGREGHLARafDLLAASKSAQTPVGVVKSAGRKKEEKWLTTLGDMDFEPVDM----TSLVIVGN 223
 
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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