|
Name |
Accession |
Description |
Interval |
E-value |
| CobM |
COG2875 |
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ... |
1-252 |
3.22e-147 |
|
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: 411.38 E-value: 3.22e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 1 MTVHFIGAGPGAADLITVRGRDLIARCPVCLYAGSIVSPELLQYCPAGARIVDTAPMSLDEIEAEYLRAAAAGQDVARLH 80
Cdd:COG2875 3 GTVYFVGAGPGDPDLITVKGRRLLEEADVVLYAGSLVPPELLAYCKPGAEIVDSASMTLEEIIALMKEAAAEGKDVVRLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 81 SGDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLTRVSGRaSPMPNDETLAKFGATGAT 160
Cdd:COG2875 83 SGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAEGR-TPMPEGESLASLAAHGAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 161 LAIHLAIHALKQVVEELTPLYGVDCPVAIVVKASWPDERILRGTLADIEAKVAAEPIERTAIIFVGPSLAAEDFRESSLY 240
Cdd:COG2875 162 LAIYLSAHRIDEVVEELLEGYPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGPALGAEDFARSKLY 241
|
250
....*....|..
gi 517057394 241 DPAYQRRFRGRE 252
Cdd:COG2875 242 DPGFSHGFRPAK 253
|
|
| Precorrin-4_C11-MT |
cd11641 |
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ... |
6-230 |
4.23e-113 |
|
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. In the aerobic pathway, CobM catalyzes the methylation of precorrin-4 at C-11 to yield precorrin-5. In the anaerobic pathway, CibF catalyzes the methylation of cobalt-precorrin-4 to cobalt-precorrin-5. Both CibF and CobM, which are homologous, are included in this model. There are about 30 enzymes involved in vitamin B12 synthetic pathway. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared in both pathways and several of these enzymes are pathway-specific.
Pssm-ID: 381168 [Multi-domain] Cd Length: 225 Bit Score: 323.96 E-value: 4.23e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 6 IGAGPGAADLITVRGRDLIARCPVCLYAGSIVSPELLQYCPAGARIVDTAPMSLDEIEAEYLRAAAAGQDVARLHSGDLS 85
Cdd:cd11641 1 VGAGPGDPELITVKGARLLEEADVVIYAGSLVPPELLAYAKPGAEIVDSAGMTLEEIIEVMREAAREGKDVVRLHTGDPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 86 VWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLTRVSGRaSPMPNDETLAKFGATGATLAIHL 165
Cdd:cd11641 81 LYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRLEGR-TPVPEGESLRELAKHGATLAIFL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057394 166 AIHALKQVVEEL-TPLYGVDCPVAIVVKASWPDERILRGTLADIEAKVAAEPIERTAIIFVGPSLA 230
Cdd:cd11641 160 SAALIEEVVEELlAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPALG 225
|
|
| cobM_cbiF |
TIGR01465 |
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ... |
3-249 |
1.39e-110 |
|
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: 318.50 E-value: 1.39e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 3 VHFIGAGPGAADLITVRGRDLIARCPVCLYAGSIVSPELLQYCPAGARIVDTAPMSLDEIEAEYLRAAAAGQDVARLHSG 82
Cdd:TIGR01465 1 VYFIGAGPGDPDLITVKGRKLIESADVILYAGSLVPPELLAHCRPGAEVVNSAGMSLEEIVDIMSDAHREGKDVARLHSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 83 DLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLTRVSGRaSPMPNDETLAKFGATGATLA 162
Cdd:TIGR01465 81 DPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGR-TPMPEGEKLADLAKHGATMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 163 IHLAIHALKQVVEELTP-LYGVDCPVAIVVKASWPDERILRGTLADIEAKVAAEPIERTAIIFVGPSLAAEDFRESSLYD 241
Cdd:TIGR01465 160 IFLSAHILDKVVKELIEhGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPALDPRIGKRSKLYD 239
|
....*...
gi 517057394 242 PAYQRRFR 249
Cdd:TIGR01465 240 PDFSHSFR 247
|
|
| cbiF |
PRK15473 |
cobalt-precorrin-4 methyltransferase; |
3-250 |
3.77e-77 |
|
cobalt-precorrin-4 methyltransferase;
Pssm-ID: 185370 Cd Length: 257 Bit Score: 233.88 E-value: 3.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 3 VHFIGAGPGAADLITVRGRDLIARCPVCLYAGSIVSPELLQYCPAGARIVDTAPMSLDEIEAEYLRAAAAGQDVARLHSG 82
Cdd:PRK15473 10 VWFVGAGPGDKELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAECHDSAELHLEQIIDLMEAGVKAGKTVVRLQTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 83 DLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLTRVSGRaSPMPNDETLAKFGATGATLA 162
Cdd:PRK15473 90 DVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIITRMEGR-TPVPAREQLESFASHQTSMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 163 IHLAIHALKQVVEELTP-LYGVDCPVAIVVKASWPDERILRGTLADIEAKVAAEPIERTAIIFVGPSLaAEDFRESSLYD 241
Cdd:PRK15473 169 IFLSVQRIHRVAERLIAgGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVGNFL-GEEYHYSKLYD 247
|
....*....
gi 517057394 242 PAYQRRFRG 250
Cdd:PRK15473 248 ADFSHEYRK 256
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
2-209 |
4.43e-41 |
|
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: 140.17 E-value: 4.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 2 TVHFIGAGPGAADLITVRGRDLIARCPVCLYAGSIVSPELLQYCPAG-----ARIVDTAPMSLDEIEAEYLRAAAAGQDV 76
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDlyfpmTEDKEPLEEAYEEIAEALAAALRAGKDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 77 ARLHSGDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLTrvsgRASPMPNDETLAKFGA 156
Cdd:pfam00590 81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFL----PGLARIELRLLEALLA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057394 157 TGATLAIHLAIHALKQVVEELTPLYGVDCPVAIVVKASWPDERILRGTLADIE 209
Cdd:pfam00590 157 NGDTVVLLYGPRRLAELAELLLELYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CobM |
COG2875 |
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ... |
1-252 |
3.22e-147 |
|
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: 411.38 E-value: 3.22e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 1 MTVHFIGAGPGAADLITVRGRDLIARCPVCLYAGSIVSPELLQYCPAGARIVDTAPMSLDEIEAEYLRAAAAGQDVARLH 80
Cdd:COG2875 3 GTVYFVGAGPGDPDLITVKGRRLLEEADVVLYAGSLVPPELLAYCKPGAEIVDSASMTLEEIIALMKEAAAEGKDVVRLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 81 SGDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLTRVSGRaSPMPNDETLAKFGATGAT 160
Cdd:COG2875 83 SGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAEGR-TPMPEGESLASLAAHGAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 161 LAIHLAIHALKQVVEELTPLYGVDCPVAIVVKASWPDERILRGTLADIEAKVAAEPIERTAIIFVGPSLAAEDFRESSLY 240
Cdd:COG2875 162 LAIYLSAHRIDEVVEELLEGYPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGPALGAEDFARSKLY 241
|
250
....*....|..
gi 517057394 241 DPAYQRRFRGRE 252
Cdd:COG2875 242 DPGFSHGFRPAK 253
|
|
| Precorrin-4_C11-MT |
cd11641 |
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ... |
6-230 |
4.23e-113 |
|
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. In the aerobic pathway, CobM catalyzes the methylation of precorrin-4 at C-11 to yield precorrin-5. In the anaerobic pathway, CibF catalyzes the methylation of cobalt-precorrin-4 to cobalt-precorrin-5. Both CibF and CobM, which are homologous, are included in this model. There are about 30 enzymes involved in vitamin B12 synthetic pathway. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared in both pathways and several of these enzymes are pathway-specific.
Pssm-ID: 381168 [Multi-domain] Cd Length: 225 Bit Score: 323.96 E-value: 4.23e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 6 IGAGPGAADLITVRGRDLIARCPVCLYAGSIVSPELLQYCPAGARIVDTAPMSLDEIEAEYLRAAAAGQDVARLHSGDLS 85
Cdd:cd11641 1 VGAGPGDPELITVKGARLLEEADVVIYAGSLVPPELLAYAKPGAEIVDSAGMTLEEIIEVMREAAREGKDVVRLHTGDPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 86 VWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLTRVSGRaSPMPNDETLAKFGATGATLAIHL 165
Cdd:cd11641 81 LYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRLEGR-TPVPEGESLRELAKHGATLAIFL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057394 166 AIHALKQVVEEL-TPLYGVDCPVAIVVKASWPDERILRGTLADIEAKVAAEPIERTAIIFVGPSLA 230
Cdd:cd11641 160 SAALIEEVVEELlAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPALG 225
|
|
| cobM_cbiF |
TIGR01465 |
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ... |
3-249 |
1.39e-110 |
|
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: 318.50 E-value: 1.39e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 3 VHFIGAGPGAADLITVRGRDLIARCPVCLYAGSIVSPELLQYCPAGARIVDTAPMSLDEIEAEYLRAAAAGQDVARLHSG 82
Cdd:TIGR01465 1 VYFIGAGPGDPDLITVKGRKLIESADVILYAGSLVPPELLAHCRPGAEVVNSAGMSLEEIVDIMSDAHREGKDVARLHSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 83 DLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLTRVSGRaSPMPNDETLAKFGATGATLA 162
Cdd:TIGR01465 81 DPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGR-TPMPEGEKLADLAKHGATMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 163 IHLAIHALKQVVEELTP-LYGVDCPVAIVVKASWPDERILRGTLADIEAKVAAEPIERTAIIFVGPSLAAEDFRESSLYD 241
Cdd:TIGR01465 160 IFLSAHILDKVVKELIEhGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPALDPRIGKRSKLYD 239
|
....*...
gi 517057394 242 PAYQRRFR 249
Cdd:TIGR01465 240 PDFSHSFR 247
|
|
| cbiF |
PRK15473 |
cobalt-precorrin-4 methyltransferase; |
3-250 |
3.77e-77 |
|
cobalt-precorrin-4 methyltransferase;
Pssm-ID: 185370 Cd Length: 257 Bit Score: 233.88 E-value: 3.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 3 VHFIGAGPGAADLITVRGRDLIARCPVCLYAGSIVSPELLQYCPAGARIVDTAPMSLDEIEAEYLRAAAAGQDVARLHSG 82
Cdd:PRK15473 10 VWFVGAGPGDKELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAECHDSAELHLEQIIDLMEAGVKAGKTVVRLQTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 83 DLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLTRVSGRaSPMPNDETLAKFGATGATLA 162
Cdd:PRK15473 90 DVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIITRMEGR-TPVPAREQLESFASHQTSMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 163 IHLAIHALKQVVEELTP-LYGVDCPVAIVVKASWPDERILRGTLADIEAKVAAEPIERTAIIFVGPSLaAEDFRESSLYD 241
Cdd:PRK15473 169 IFLSVQRIHRVAERLIAgGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVGNFL-GEEYHYSKLYD 247
|
....*....
gi 517057394 242 PAYQRRFRG 250
Cdd:PRK15473 248 ADFSHEYRK 256
|
|
| SUMT |
cd11642 |
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
6-226 |
5.78e-45 |
|
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: 150.67 E-value: 5.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 6 IGAGPGAADLITVRGRDLIARCPVCLYaGSIVSPELLQYCPAGARIVDT------APMSLDEIEAEYLRAAAAGQDVARL 79
Cdd:cd11642 1 VGAGPGDPDLLTLKALRALQQADVVLY-DRLVSPEILALAPPGAELIYVgkrpgrHSVPQEEINELLVELAREGKRVVRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 80 HSGDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLtrVSGRASPMPNDETLAKFGATGA 159
Cdd:cd11642 80 KGGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTF--VTGHEADGKLPDDDAALARPGG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517057394 160 TLAIHLAIHALKQVVEELTpLYGV--DCPVAIVVKASWPDERILRGTLADIEAKVAAEPIERTAIIFVG 226
Cdd:cd11642 158 TLVIYMGVSNLEEIAERLI-AAGLppDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVG 225
|
|
| PRK06136 |
PRK06136 |
uroporphyrinogen-III C-methyltransferase; |
1-233 |
1.13e-41 |
|
uroporphyrinogen-III C-methyltransferase;
Pssm-ID: 235711 Cd Length: 249 Bit Score: 142.66 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 1 MTVHFIGAGPGAADLITVRGRDLIARCPVCLYaGSIVSPELLQYCPAGARIVDT------APMSLDEIEAEYLRAAAAGQ 74
Cdd:PRK06136 3 GKVYLVGAGPGDPDLITLKGVRLLEQADVVLY-DDLVSPEILAYAKPDAELIYVgkragrHSTKQEEINRLLVDYARKGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 75 DVARLHSGDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLT---RVSGRASPMPNDETL 151
Cdd:PRK06136 82 VVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVtghEAAGKLEPEVNWSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 152 AKfgaTGATLAIHLAIHALKQVVEELTpLYG--VDCPVAIVVKASWPDERILRGTLADIEAKVAAEPIERTAIIFVGPSL 229
Cdd:PRK06136 162 AD---GADTLVIYMGVRNLPYIAAQLL-AAGraPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIQSPAIIVIGEVV 237
|
....
gi 517057394 230 AAED 233
Cdd:PRK06136 238 ALRA 241
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
2-209 |
4.43e-41 |
|
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: 140.17 E-value: 4.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 2 TVHFIGAGPGAADLITVRGRDLIARCPVCLYAGSIVSPELLQYCPAG-----ARIVDTAPMSLDEIEAEYLRAAAAGQDV 76
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDlyfpmTEDKEPLEEAYEEIAEALAAALRAGKDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 77 ARLHSGDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLTrvsgRASPMPNDETLAKFGA 156
Cdd:pfam00590 81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFL----PGLARIELRLLEALLA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057394 157 TGATLAIHLAIHALKQVVEELTPLYGVDCPVAIVVKASWPDERILRGTLADIE 209
Cdd:pfam00590 157 NGDTVVLLYGPRRLAELAELLLELYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
|
|
| CysG |
COG0007 |
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
2-226 |
1.55e-40 |
|
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: 139.44 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 2 TVHFIGAGPGAADLITVRGRDLIARCPVCLYaGSIVSPELLQYCPAGARIVDT------APMSLDEIEAEYLRAAAAGQD 75
Cdd:COG0007 3 KVYLVGAGPGDPDLLTLKALRALQQADVVLY-DRLVSPEILALARPDAELIYVgkrggrHSLPQEEINALLVELARAGKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 76 VARLHSGDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLtrVSGRASPMPNDETLAKFG 155
Cdd:COG0007 82 VVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTF--VTGHEKDGKLDLDWAALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057394 156 ATGATLAIHLAIHALKQVVEELTpLYGV--DCPVAIVVKASWPDERILRGTLADIEAKVAAEPIERTAIIFVG 226
Cdd:COG0007 160 RPGGTLVIYMGVKNLPEIAAALI-AAGRspDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVG 231
|
|
| PLN02625 |
PLN02625 |
uroporphyrin-III C-methyltransferase |
2-234 |
8.92e-34 |
|
uroporphyrin-III C-methyltransferase
Pssm-ID: 178232 [Multi-domain] Cd Length: 263 Bit Score: 122.82 E-value: 8.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 2 TVHFIGAGPGAADLITVRGRDLIARCPVCLYaGSIVSPELLQYCPAGARIV------DTAPMSLDEIEAEYLRAAAAGQD 75
Cdd:PLN02625 16 NVFLVGTGPGDPDLLTLKALRLLQTADVVLY-DRLVSPDILDLVPPGAELLyvgkrgGYHSRTQEEIHELLLSFAEAGKT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 76 VARLHSGDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLTrvSGRASPMPNDETLAKFG 155
Cdd:PLN02625 95 VVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRFL--TGHDREGGTDPLDVAEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 156 ATGA--TLAIHLAIHALKQVVEELTPL-YGVDCPVAIVVKASWPDERILRGTLADIEAKVAAEPIERTAIIFVGPSLAAE 232
Cdd:PLN02625 173 AADPdtTLVVYMGLGTLPSLAEKLIAAgLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAGLVSPTVIVVGEVVALS 252
|
..
gi 517057394 233 DF 234
Cdd:PLN02625 253 PL 254
|
|
| TP_methylase |
cd11724 |
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
3-226 |
1.41e-27 |
|
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: 105.72 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 3 VHFIGAGPGAADLITVRGRDLIARCPVCLYAGSIVS--PELLQ--------------YCPAGARIVDT--APMSLDEIEA 64
Cdd:cd11724 2 LYLVGVGPGDPDLITLRALKAIKKADVVFAPPDLRKrfAEYLAgkevlddphglftyYGKKCSPLEEAekECEELEKQRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 65 EYLR----AAAAGQDVARLHSGDLSV---WSAVAEQVRRLQKHGIdytmtPGVPAFAAAASALGRELTIPAVAQSLVLTr 137
Cdd:cd11724 82 EIVQkireALAQGKNVALLDSGDPTIygpWIWYLEEFADLNPEVI-----PGVSSFNAANAALKRSLTGGGDSRSVILT- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 138 vsGRASPMPNDETLAKFGATGATLAIHLAIHALKQVVEELTPLYGVDCPVAIVVKASWPD-ERILRGTLADIEAKVAAEP 216
Cdd:cd11724 156 --APFALKENEDLLEDLAATGDTLVIFMMRLDLDELVEKLKKHYPPDTPVAIVYHAGYSEkEKVIRGTLDDILEKLGGEK 233
|
250
....*....|
gi 517057394 217 IERTAIIFVG 226
Cdd:cd11724 234 EPFLGLIYVG 243
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
6-226 |
1.72e-22 |
|
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.
Pssm-ID: 381167 [Multi-domain] Cd Length: 219 Bit Score: 91.69 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 6 IGAGPGAADLITVRGRDLIARCPVCLYAGSIV---SPELLQYCPAGARIVDTA-PMSLDEIEAEYLRAAAAGQDVARLHS 81
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSkllSLVLRAILKDGKRIYDLHdPNVEEEMAELLLEEARQGKDVAFLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 82 GDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELtipavAQSLVLTRVSGRaSPMPNDETLAKFGATGATL 161
Cdd:cd09815 81 GDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDL-----GESFLFVTASDL-LENPRLLVLKALAKERRHL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057394 162 AIHLAIHALKQVVEELTPLYGV-DCPVAIVVKASWPDERILRGTLADIEAKVaAEPIERTAIIFVG 226
Cdd:cd09815 155 VLFLDGHRFLKALERLLKELGEdDTPVVLVANAGSEGEVIRTGTVKELRAER-TERGKPLTTILVG 219
|
|
| PRK07168 |
PRK07168 |
uroporphyrin-III C-methyltransferase; |
3-226 |
7.85e-17 |
|
uroporphyrin-III C-methyltransferase;
Pssm-ID: 180864 [Multi-domain] Cd Length: 474 Bit Score: 79.27 E-value: 7.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 3 VHFIGAGPGAADLITVRGRDLIARCPVCLYaGSIVSPELLQYCPAGARIVDTAPMSLDE------IEAEYLRAAAAGQDV 76
Cdd:PRK07168 5 VYLVGAGPGDEGLITKKAIECLKRADIVLY-DRLLNPFFLSYTKQTCELMYCGKMPKNHimrqemINAHLLQFAKEGKIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 77 ARLHSGDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLtrVSGRASPMPNDETLAKFGA 156
Cdd:PRK07168 84 VRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNSVTL--LTGHAKGPLTDHGKYNSSH 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057394 157 TGATLAIHLAIHALKQVVEELTPL-YGVDCPVAIVVKASWPDERILRGTLADIEAKVAAEPIERTAIIFVG 226
Cdd:PRK07168 162 NSDTIAYYMGIKNLPTICENLRQAgKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSIVKNENISNPSMTIVG 232
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
1-126 |
2.64e-11 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 61.47 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 1 MTVHFIGAGPGAADLITVRGRDLIARCPVcLY-----------AGSIVSPellqYCPAGARIVDTA-PMSLD--EIEAEY 66
Cdd:PRK05576 2 GKLYGIGLGPGDPELLTVKAARILEEADV-VYapasrkgggslALNIVRP----YLKEETEIVELHfPMSKDeeEKEAVW 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517057394 67 LRAAAA-------GQDVARLHSGDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTI 126
Cdd:PRK05576 77 KENAEEiaaeaeeGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSFTAIASRAGVPLAM 143
|
|
| cysG |
PRK10637 |
siroheme synthase CysG; |
3-226 |
7.25e-10 |
|
siroheme synthase CysG;
Pssm-ID: 182606 [Multi-domain] Cd Length: 457 Bit Score: 58.62 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 3 VHFIGAGPGAADLITVRGRDLIARCPVCLYaGSIVSPELLQYCPAGARIVDTAPMS------LDEIEAEYLRAAAAGQDV 76
Cdd:PRK10637 218 VVLVGAGPGDAGLLTLKGLQQIQQADVVVY-DRLVSDDIMNLVRRDADRVFVGKRAgyhcvpQEEINQILLREAQKGKRV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 77 ARLHSGDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLVLtrVSGRASpmpNDETL--AKF 154
Cdd:PRK10637 297 VRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRL--VTGHLK---TGGELdwENL 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517057394 155 GATGATLAIHLAIHALKQVVEELTPlYGV--DCPVAIVVKASWPDERILRGTLADIEAkvAAEPIERTAIIFVG 226
Cdd:PRK10637 372 AAEKQTLVFYMGLNQAATIQQKLIE-HGMpaDMPVALVENGTSVTQRVVSGTLTQLGE--LAQQVNSPSLIIVG 442
|
|
| Precorrin_2_C20_MT |
cd11645 |
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
6-212 |
8.76e-09 |
|
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: 54.05 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 6 IGAGPGAADLITVRGRDLIARCPV----------CLYAGSIVSPELLQycpaGARIVD-TAPMSLDEIEAEYLRAAAAGQ 74
Cdd:cd11645 1 VGVGPGDPELLTLKAVRILKEADVifvpvskggeGSAALIIAAALLIP----DKEIIPlEFPMTKDREELEEAWDEAAEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 75 DVARLHS---------GDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPavAQSLVLTrvsgrasPM 145
Cdd:cd11645 77 IAEELKEgkdvafltlGDPSLYSTFSYLLERLRAPGVEVEIIPGITSFSAAAARLGIPLAEG--DESLAIL-------PA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057394 146 PND-ETLAKFGATGATLAI---HLAIHALKQVVEELtplyGVDCPVAIVVKASWPDERILRGTLADIEAKV 212
Cdd:cd11645 148 TYDeEELEKALENFDTVVLmkvGRNLEEIKELLEEL----GLLDKAVYVERCGMEGERIYTDLEELKEEKL 214
|
|
| CobF |
COG2243 |
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
1-213 |
1.18e-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: 53.95 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 1 MTVHFIGAGPGAADLITVRGRDLIARCPVCLY----------AGSIVSPELlqycpAGARIVDTA-PMSLD--EIEAEYL 67
Cdd:COG2243 3 GKLYGVGVGPGDPELLTLKAVRALREADVIAYpakgagkaslAREIVAPYL-----PPARIVELVfPMTTDyeALVAAWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 68 RAAA-------AGQDVARLHSGDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGreltIPAVAQSLVLTRVSG 140
Cdd:COG2243 78 EAAAriaeeleAGRDVAFLTEGDPSLYSTFMYLLERLRERGFEVEVIPGITSFSAAAAALG----IPLAEGDEPLTVLPG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057394 141 RASpmpnDETLAKFGATGATLAI---HLAIHALKQVVEELtplyGVDCPVAIVVKASWPDERILRGtLADIEAKVA 213
Cdd:COG2243 154 TLL----EEELERALDDFDTVVImkvGRNFPKVREALEEA----GLLDRAWYVERAGMPDERIVPG-LAEVDIEEA 220
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
1-139 |
2.43e-07 |
|
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: 50.00 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 1 MTVHFIGAGPGAADLITVRGRDLIARCPVCLY----------AGSIVSPELLqycPAGARIVDTA-PMS--LDEIEAEYL 67
Cdd:TIGR01467 1 GKLYGVGVGPGDPELITVKALEALRSADVIAVpaskkgreslARKIVEDYLK---PNDTRILELVfPMTkdRDELEKAWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 68 RAAAA-------GQDVARLHSGDLSVWSAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELT--------IPAVAQS 132
Cdd:TIGR01467 78 EAAEAvaaeleeGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAGLPLVegdeslaiLPATAGE 157
|
....*..
gi 517057394 133 LVLTRVS 139
Cdd:TIGR01467 158 AELEKAL 164
|
|
| cobJ_cbiH |
TIGR01466 |
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ... |
6-228 |
2.92e-06 |
|
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: 46.91 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 6 IGAGPGAADLITVRGRDLIARCPVCL-YAGSI--VSPELlqycpAGARIVDTaPMSlDEIE-AEY-LRAAAAGQDVARLH 80
Cdd:TIGR01466 4 VGIGPGAEELMTPEAKEALAEADVIVgYKTYLdlIEDLI-----PGKEVVTS-GMR-EEIArAELaIELAAEGRTVALVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 81 SGDLSVW--SAVAEQVRRLQKHGIDYTMTPGVPAFAAAASALGRELTIPAVAQSLvltrvSGRASPMPNDET-LAKFGAT 157
Cdd:TIGR01466 77 SGDPGIYgmAALVFEALEKKGAEVDIEVIPGITAASAAASLLGAPLGHDFCVISL-----SDLLTPWPEIEKrLRAAAEA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057394 158 GATLAIHLAIHA-----LKQVVEELTPLYGVDCPVAIVVKASWPDERILRGTLADieakVAAEPIERTAIIFVGPS 228
Cdd:TIGR01466 152 DFVIAIYNPRSKrrpeqFRRAMEILLEHRKPDTPVGIVRNAGREGEEVEITTLAE----LDEELIDMLTTVIIGNS 223
|
|
| PRK05787 |
PRK05787 |
cobalt-precorrin-7 (C(5))-methyltransferase; |
3-95 |
1.97e-05 |
|
cobalt-precorrin-7 (C(5))-methyltransferase;
Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 44.09 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 3 VHFIGAGPGAADLITVRGRDLIARCPVClyAGSIVSPELLQYCPAGARIVdtAPMSLDEIEaEYLRAAAAGQDVARLHSG 82
Cdd:PRK05787 2 IYIVGIGPGDPEYLTLKALEAIRKADVV--VGSKRVLELFPELIDGEAFV--LTAGLRDLL-EWLELAAKGKNVVVLSTG 76
|
90 100
....*....|....*....|..
gi 517057394 83 D---------LSVWSAVAEQVR 95
Cdd:PRK05787 77 DplfsglgklLKVRRAVAEDVE 98
|
|
| PRK05948 |
PRK05948 |
precorrin-2 C(20)-methyltransferase; |
2-202 |
2.31e-04 |
|
precorrin-2 C(20)-methyltransferase;
Pssm-ID: 180320 Cd Length: 238 Bit Score: 41.17 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 2 TVHFIGAGPGAADLITVRGRDLIARCPVCLY----------AGSIVSPELLqycPAGARIVDTAPMSLDE--IEAEYLRA 69
Cdd:PRK05948 5 TLYGISVGPGDPELITLKGLRLLQSAPVVAFpaglagqpglAEQIIAPWLS---PQQIKLPLYFPYVQDEeqLEQAWQAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 70 A-------AAGQDVARLHSGDLSVWSAVAEQVRRLQKhgidytmtpgvpafaaaasalgrelTIPAVAqslvLTRVSGRA 142
Cdd:PRK05948 82 AdqvwhylEQGEDVAFACEGDVSFYSTFTYLAQTLQE-------------------------LYPQVA----IQTIPGVC 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 143 SPMPNDETLAKFGATGA-TLAIHLAIHALKQVVEELTP-----LYGVDcPV-----------------AIVVKASWPDER 199
Cdd:PRK05948 133 SPLAAAAALGIPLTLGSqRLAILPALYHLEELEQALTWadvvvLMKVS-SVypqvwqwlkarnlleqaSLVERATTPEQV 211
|
...
gi 517057394 200 ILR 202
Cdd:PRK05948 212 IYR 214
|
|
| RsmI_like |
cd19918 |
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ... |
170-216 |
2.62e-04 |
|
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small subunit methyltransferase I (RsmI); RsmI, also known as rRNA (cytidine-2'-O-)-methyltransferase, is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress.
Pssm-ID: 381181 Cd Length: 217 Bit Score: 40.98 E-value: 2.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 517057394 170 LKQVVEELTPLYGVDCPVAIVVKASWPDERILRGTLADIEAKVAAEP 216
Cdd:cd19918 161 LKKLLEDLAKVFGPNRRIVLAYNLTLPDEKILRGTLAEILKKVEEKP 207
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| PRK05765 |
PRK05765 |
precorrin-3B C17-methyltransferase; Provisional |
1-229 |
3.34e-03 |
|
precorrin-3B C17-methyltransferase; Provisional
Pssm-ID: 235597 Cd Length: 246 Bit Score: 37.84 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 1 MTVHFIGAGPGAADLITVRGRDLIARCPVCL----YAGSIvsPELLqycpaGARIVDTAPMSLDEIEAEY-LRAAAAGQD 75
Cdd:PRK05765 2 GKLYIVGIGPGSKEQRTIKAQEAIEKSNVIIgyntYLRLI--SDLL-----DGKEVIGARMKEEIFRANTaIEKALEGNI 74
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 76 VARLHSGDLSVWSAVAEQVRRLQKHGI--DYTMTPGVPAFAAAASALGRELTIPAVAQSLvltrvsgraSPM--PNDETL 151
Cdd:PRK05765 75 VALVSSGDPQVYGMAGLVFELISRRKLdvDVEVIPGVTAALAAAARLGSPLSLDFVVISL---------SDLliPREEIL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 152 AKFGATGA---TLAIHLAIHA--LKQVVEELTPLYGVDCPVAIVVKASWPDERILRGTLAdiEAKVAAEPIERTAIIFVG 226
Cdd:PRK05765 146 HRVTKAAEadfVIVFYNPINEnlLIEVMDIVSKHRKPNTPVGLVKSAYRNNENVVITTLS--SWKEHMDEIGMTTTMIIG 223
|
...
gi 517057394 227 PSL 229
Cdd:PRK05765 224 NSL 226
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| Precorrin-6Y-MT |
cd11644 |
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
6-110 |
3.74e-03 |
|
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: 37.47 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057394 6 IGAGPGAADLITVRGRDLIARCPVClyagsIVSPELLQYCPAGARivDTAPMSLDEIEAEYLRAAAAGQDVARLHSGDLS 85
Cdd:cd11644 1 IGIGPGGPEYLTPEAREAIEEADVV-----IGAKRLLELFPDLGA--EKIPLPSEDIAELLEEIAEAGKRVVVLASGDPG 73
|
90 100
....*....|....*....|....*..
gi 517057394 86 VWSAvaeqVRRLQKHGIDYTMT--PGV 110
Cdd:cd11644 74 FYGI----GKTLLRRLGGEEVEviPGI 96
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