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Conserved domains on  [gi|1008885855|gb|AMR17529|]
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precorrin-3B C(17)-methyltransferase [Klebsiella quasipneumoniae]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 148)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; belongs to the tetrapyrrole methylase family

CATH:  3.40.1010.10|3.30.950.10
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168
PubMed:  16225687
SCOP:  4000056

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TP_methylase super family cl00304
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 1-241 4.35e-170

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.


The actual alignment was detected with superfamily member PRK15478:

Pssm-ID: 444820 [Multi-domain]  Cd Length: 241  Bit Score: 468.21  E-value: 4.35e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   1 MLSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGD 80
Cdd:PRK15478    1 MLSVIGIGPGSQAMMTMEAIEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  81 AGIYGMAGLVLELVNKQRLDIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWSVIEKRIVAAGEADFVICFYN 160
Cdd:PRK15478   81 AGIYGMAGLVLELVSKQKLDVEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWPVIEKRIVAAGEADFVICFYN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855 161 PRSRGREGHLARAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMDFAPVDMTSLVIVGNKATYIDKGLMITPRGYA 240
Cdd:PRK15478  161 PRSRGREGHLARAFDLLAASKSAQTPVGVVKSAGRKKEEKWLTTLGDMDFEPVDMTSLVIVGNKTTYVQDGLMITPRGYT 240


                  .
gi 1008885855 241 L 241
Cdd:PRK15478  241 L 241
 
Name Accession Description Interval E-value
cbiH PRK15478
precorrin-3B C(17)-methyltransferase;
1-241 4.35e-170

precorrin-3B C(17)-methyltransferase;


Pssm-ID: 185375 [Multi-domain]  Cd Length: 241  Bit Score: 468.21  E-value: 4.35e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   1 MLSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGD 80
Cdd:PRK15478    1 MLSVIGIGPGSQAMMTMEAIEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  81 AGIYGMAGLVLELVNKQRLDIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWSVIEKRIVAAGEADFVICFYN 160
Cdd:PRK15478   81 AGIYGMAGLVLELVSKQKLDVEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWPVIEKRIVAAGEADFVICFYN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855 161 PRSRGREGHLARAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMDFAPVDMTSLVIVGNKATYIDKGLMITPRGYA 240
Cdd:PRK15478  161 PRSRGREGHLARAFDLLAASKSAQTPVGVVKSAGRKKEEKWLTTLGDMDFEPVDMTSLVIVGNKTTYVQDGLMITPRGYT 240


                  .
gi 1008885855 241 L 241
Cdd:PRK15478  241 L 241
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
 2-239 3.75e-138

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: 387.16  E-value: 3.75e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   2 LSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGDA 81
Cdd:cd11646     1 LYVVGIGPGSADLMTPRAREALEEADVIVGYKTYLDLIEDLLPGKEVISSGMGEEVERAREALELALEGKRVALVSSGDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  82 GIYGMAGLVLELVNKQRLDIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWSVIEKRIVAAGEADFVICFYNP 161
Cdd:cd11646    81 GIYGMAGLVLELLDERWDDIEVEVVPGITAALAAAALLGAPLGHDFAVISLSDLLTPWEVIEKRLRAAAEADFVIALYNP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008885855 162 RSRGREGHLARAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMDFAPVDMTSLVIVGNKATYIDKGLMITPRGY 239
Cdd:cd11646   161 RSKKRPWQLEKALEILLEHRPPDTPVGIVRNAGREGEEVTITTLGELDPEDVDMFTTVIIGNSQTYIIGGKMITPRGY 238
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
 2-240 1.18e-135

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: 381.34  E-value: 1.18e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   2 LSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGDA 81
Cdd:COG1010     6 LYVVGLGPGSAELMTPRARAALAEADVVVGYGTYLDLIPPLLPGKEVHASGMREEVERAREALELAAEGKTVAVVSSGDP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  82 GIYGMAGLVLELV--NKQRLDIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWSVIEKRIVAAGEADFVICFY 159
Cdd:COG1010    86 GVYGMAGLVLEVLeeGGAWRDVEVEVVPGITAAQAAAARLGAPLGHDFCVISLSDLLTPWEVIEKRLRAAAEADFVIALY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855 160 NPRSRGREGHLARAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMDFAPVDMTSLVIVGNKATYIDKGLMITPRGY 239
Cdd:COG1010   166 NPRSRKRPWQLERALEILLEHRPPDTPVGIVRNAGRPDESVTVTTLGELDPEEVDMLTTVIIGNSQTRVIGGWMITPRGY 245


                  .
gi 1008885855 240 A 240
Cdd:COG1010   246 P 246
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
 2-240 2.13e-132

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: 372.79  E-value: 2.13e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   2 LSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGDA 81
Cdd:TIGR01466   1 LYVVGIGPGAEELMTPEAKEALAEADVIVGYKTYLDLIEDLIPGKEVVTSGMREEIARAELAIELAAEGRTVALVSSGDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  82 GIYGMAGLVLELVNKQRLDIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWSVIEKRIVAAGEADFVICFYNP 161
Cdd:TIGR01466  81 GIYGMAALVFEALEKKGAEVDIEVIPGITAASAAASLLGAPLGHDFCVISLSDLLTPWPEIEKRLRAAAEADFVIAIYNP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008885855 162 RSRGREGHLARAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMDFAPVDMTSLVIVGNKATYIDKGLMITPRGYA 240
Cdd:TIGR01466 161 RSKRRPEQFRRAMEILLEHRKPDTPVGIVRNAGREGEEVEITTLAELDEELIDMLTTVIIGNSETYVIDGWMITPRGYA 239
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 1-209 8.99e-35

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


Pssm-ID: 425769 [Multi-domain]  Cd Length: 209  Bit Score: 123.22  E-value: 8.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   1 MLSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKT-YTHLVKAFTGDKQVIKTGMCKEI------ERCQAAIELAQAGHNV 73
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSrALEILLDLLPEDLYFPMTEDKEPleeayeEIAEALAAALRAGKDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  74 ALISSGDAGIYGMAGLVLELVnkQRLDIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSdLLTPWSVIEKRIVAAGEA- 152
Cdd:pfam00590  81 ARLVSGDPLVYGTGSYLVEAL--RAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVL-FLPGLARIELRLLEALLAn 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1008885855 153 -DFVICFYNPRSRGREghlaraFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMD 209
Cdd:pfam00590 158 gDTVVLLYGPRRLAEL------AELLLELYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
 
Name Accession Description Interval E-value
cbiH PRK15478
precorrin-3B C(17)-methyltransferase;
1-241 4.35e-170

precorrin-3B C(17)-methyltransferase;


Pssm-ID: 185375 [Multi-domain]  Cd Length: 241  Bit Score: 468.21  E-value: 4.35e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   1 MLSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGD 80
Cdd:PRK15478    1 MLSVIGIGPGSQAMMTMEAIEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  81 AGIYGMAGLVLELVNKQRLDIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWSVIEKRIVAAGEADFVICFYN 160
Cdd:PRK15478   81 AGIYGMAGLVLELVSKQKLDVEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWPVIEKRIVAAGEADFVICFYN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855 161 PRSRGREGHLARAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMDFAPVDMTSLVIVGNKATYIDKGLMITPRGYA 240
Cdd:PRK15478  161 PRSRGREGHLARAFDLLAASKSAQTPVGVVKSAGRKKEEKWLTTLGDMDFEPVDMTSLVIVGNKTTYVQDGLMITPRGYT 240


                  .
gi 1008885855 241 L 241
Cdd:PRK15478  241 L 241
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
 2-239 3.75e-138

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: 387.16  E-value: 3.75e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   2 LSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGDA 81
Cdd:cd11646     1 LYVVGIGPGSADLMTPRAREALEEADVIVGYKTYLDLIEDLLPGKEVISSGMGEEVERAREALELALEGKRVALVSSGDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  82 GIYGMAGLVLELVNKQRLDIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWSVIEKRIVAAGEADFVICFYNP 161
Cdd:cd11646    81 GIYGMAGLVLELLDERWDDIEVEVVPGITAALAAAALLGAPLGHDFAVISLSDLLTPWEVIEKRLRAAAEADFVIALYNP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008885855 162 RSRGREGHLARAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMDFAPVDMTSLVIVGNKATYIDKGLMITPRGY 239
Cdd:cd11646   161 RSKKRPWQLEKALEILLEHRPPDTPVGIVRNAGREGEEVTITTLGELDPEDVDMFTTVIIGNSQTYIIGGKMITPRGY 238
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
 2-240 1.18e-135

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: 381.34  E-value: 1.18e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   2 LSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGDA 81
Cdd:COG1010     6 LYVVGLGPGSAELMTPRARAALAEADVVVGYGTYLDLIPPLLPGKEVHASGMREEVERAREALELAAEGKTVAVVSSGDP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  82 GIYGMAGLVLELV--NKQRLDIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWSVIEKRIVAAGEADFVICFY 159
Cdd:COG1010    86 GVYGMAGLVLEVLeeGGAWRDVEVEVVPGITAAQAAAARLGAPLGHDFCVISLSDLLTPWEVIEKRLRAAAEADFVIALY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855 160 NPRSRGREGHLARAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMDFAPVDMTSLVIVGNKATYIDKGLMITPRGY 239
Cdd:COG1010   166 NPRSRKRPWQLERALEILLEHRPPDTPVGIVRNAGRPDESVTVTTLGELDPEEVDMLTTVIIGNSQTRVIGGWMITPRGY 245


                  .
gi 1008885855 240 A 240
Cdd:COG1010   246 P 246
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
 2-240 2.13e-132

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: 372.79  E-value: 2.13e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   2 LSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGDA 81
Cdd:TIGR01466   1 LYVVGIGPGAEELMTPEAKEALAEADVIVGYKTYLDLIEDLIPGKEVVTSGMREEIARAELAIELAAEGRTVALVSSGDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  82 GIYGMAGLVLELVNKQRLDIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWSVIEKRIVAAGEADFVICFYNP 161
Cdd:TIGR01466  81 GIYGMAALVFEALEKKGAEVDIEVIPGITAASAAASLLGAPLGHDFCVISLSDLLTPWPEIEKRLRAAAEADFVIAIYNP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008885855 162 RSRGREGHLARAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMDFAPVDMTSLVIVGNKATYIDKGLMITPRGYA 240
Cdd:TIGR01466 161 RSKRRPEQFRRAMEILLEHRKPDTPVGIVRNAGREGEEVEITTLAELDEELIDMLTTVIIGNSETYVIDGWMITPRGYA 239
PRK05765 PRK05765
precorrin-3B C17-methyltransferase; Provisional
 2-239 2.57e-80

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 235597  Cd Length: 246  Bit Score: 241.23  E-value: 2.57e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   2 LSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGDA 81
Cdd:PRK05765    4 LYIVGIGPGSKEQRTIKAQEAIEKSNVIIGYNTYLRLISDLLDGKEVIGARMKEEIFRANTAIEKALEGNIVALVSSGDP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  82 GIYGMAGLVLELVNKQRLDIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWSVIEKRIVAAGEADFVICFYNP 161
Cdd:PRK05765   84 QVYGMAGLVFELISRRKLDVDVEVIPGVTAALAAAARLGSPLSLDFVVISLSDLLIPREEILHRVTKAAEADFVIVFYNP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855 162 RSRGReghLARAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGE--MDFAPVDMTSLVIVGNKATYIDKGLMITPRGY 239
Cdd:PRK05765  164 INENL---LIEVMDIVSKHRKPNTPVGLVKSAYRNNENVVITTLSSwkEHMDEIGMTTTMIIGNSLTYSWKNYMITPRGY 240
PRK05991 PRK05991
precorrin-3B C17-methyltransferase; Provisional
 2-237 1.23e-54

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 180342 [Multi-domain]  Cd Length: 250  Bit Score: 175.71  E-value: 1.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   2 LSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAfTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGDA 81
Cdd:PRK05991    5 LFVIGTGPGNPEQMTPEALAAVEAATDFFGYGPYLDRLPL-RADQLRHASDNREELDRAGAALAMAAAGANVCVVSGGDP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  82 GIYGMAGLVLELVNKQRL---DIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWSVIEKRIVAAGEADFVICF 158
Cdd:PRK05991   84 GVFAMAAAVCEAIENGPAawrAVDLTIVPGVTAMLAVAARIGAPLGHDFCAISLSDNLKPWELIEKRLRLAAEAGFVIAL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855 159 YNPRSRGREGHLARAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMDFAPVDMTSLVIVGNKATYI-----DKGLM 233
Cdd:PRK05991  164 YNPISRARPWQLGEAFDLLREHLPATVPVIFGRAAGRPDERIAVAPLAEADASMADMATCVIIGSAETRIvarpgKPDLV 243


                  ....
gi 1008885855 234 ITPR 237
Cdd:PRK05991  244 YTPR 247
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 1-209 8.99e-35

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


Pssm-ID: 425769 [Multi-domain]  Cd Length: 209  Bit Score: 123.22  E-value: 8.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   1 MLSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKT-YTHLVKAFTGDKQVIKTGMCKEI------ERCQAAIELAQAGHNV 73
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSrALEILLDLLPEDLYFPMTEDKEPleeayeEIAEALAAALRAGKDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  74 ALISSGDAGIYGMAGLVLELVnkQRLDIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSdLLTPWSVIEKRIVAAGEA- 152
Cdd:pfam00590  81 ARLVSGDPLVYGTGSYLVEAL--RAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVL-FLPGLARIELRLLEALLAn 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1008885855 153 -DFVICFYNPRSRGREghlaraFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMD 209
Cdd:pfam00590 158 gDTVVLLYGPRRLAEL------AELLLELYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 5-222 1.02e-24

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: 97.46  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   5 IGIGPGSQAMMTMEAVEALQAAEIVVGYKTY-----THLVKAFTGDKQVI-KTGMCKEIERCQAAIELAQAGHNVALISS 78
Cdd:cd09815     1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDskllsLVLRAILKDGKRIYdLHDPNVEEEMAELLLEEARQGKDVAFLSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  79 GDAGIYGMAGLVLELvnKQRLDIEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWSVieKRIVAAGEADFVICF 158
Cdd:cd09815    81 GDPGVAGTGAELVER--AEREGVEVKVIPGVSAADAAAAALGIDLGESFLFVTASDLLENPRL--LVLKALAKERRHLVL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008885855 159 YNPRSRgregHLARAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMDFA---PVDMTSLVIVG 222
Cdd:cd09815   157 FLDGHR----FLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKELRAErteRGKPLTTILVG 219
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
1-132 9.44e-20

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


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 84.15  E-value: 9.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   1 MLSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAF-TGDKQVIKTGMCKEIERcqaaIELAQAGHNVALISSG 79
Cdd:PRK05787    1 MIYIVGIGPGDPEYLTLKALEAIRKADVVVGSKRVLELFPELiDGEAFVLTAGLRDLLEW----LELAAKGKNVVVLSTG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1008885855  80 DAGIYGMaGLVLELVNKQRLDIEVrlIPGMTASIAAASLLGAPlMHDFCHISL 132
Cdd:PRK05787   77 DPLFSGL-GKLLKVRRAVAEDVEV--IPGISSVQYAAARLGID-MNDVVFTTS 125
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
 1-132 9.78e-20

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: 83.66  E-value: 9.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   1 MLSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERcqaaIELAQAGHNVALISSGD 80
Cdd:COG2241     3 WLTVVGIGPGGPDGLTPAAREAIAEADVVVGGKRHLELFPDLGAERIVWPSPLSELLEE----LLALLRGRRVVVLASGD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1008885855  81 AGIYGMAGLVLELVNKQrldiEVRLIPGMTASIAAASLLGAPlMHDFCHISL 132
Cdd:COG2241    79 PLFYGIGATLARHLPAE----EVRVIPGISSLQLAAARLGWP-WQDAAVVSL 125
CbiE TIGR02467
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ...
 4-132 8.78e-19

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


Pssm-ID: 274146 [Multi-domain]  Cd Length: 204  Bit Score: 81.21  E-value: 8.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   4 VIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAF-TGDKQVIKTGmcKEIERCQAAIELAQAGHNVALISSGDAG 82
Cdd:TIGR02467   1 VVGIGPGGPELLTPAAIEAIRKADLVVGGERHLELLAELiGEKREIILTY--KDLDELLEFIAATRKEKRVVVLASGDPL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1008885855  83 IYGMAGLVLELVNKQRLDIevrlIPGMTASIAAASLLGAPlMHDFCHISL 132
Cdd:TIGR02467  79 FYGIGRTLAERLGKERLEI----IPGISSVQYAFARLGLP-WQDAVVISL 123
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
 5-132 2.35e-18

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: 79.85  E-value: 2.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   5 IGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTgmcKEIErcqAAIE-LAQAGHNVALISSGDAGI 83
Cdd:cd11644     1 IGIGPGGPEYLTPEAREAIEEADVVIGAKRLLELFPDLGAEKIPLPS---EDIA---ELLEeIAEAGKRVVVLASGDPGF 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1008885855  84 YGMAGLVLELVNkqrlDIEVRLIPGMTASIAAASLLGAPlMHDFCHISL 132
Cdd:cd11644    75 YGIGKTLLRRLG----GEEVEVIPGISSVQLAAARLGLP-WEDARLVSL 118
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
 2-208 8.59e-18

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: 79.52  E-value: 8.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   2 LSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGM-------------------CKEIERCQA 62
Cdd:cd11724     2 LYLVGVGPGDPDLITLRALKAIKKADVVFAPPDLRKRFAEYLAGKEVLDDPHglftyygkkcspleeaekeCEELEKQRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  63 AI-----ELAQAGHNVALISSGDAGIYG-MAGLVLELVnkqrlDIEVRLIPGMTASIAAASLLGAPLMHDFCH----ISL 132
Cdd:cd11724    82 EIvqkirEALAQGKNVALLDSGDPTIYGpWIWYLEEFA-----DLNPEVIPGVSSFNAANAALKRSLTGGGDSrsviLTA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855 133 SDLLTPWSVIEKRIVAAGEadfVICFYNPRS-------RGREGHlarafallaaskSADTPVGVVKSAGRKKQEK-WLTT 204
Cdd:cd11724   157 PFALKENEDLLEDLAATGD---TLVIFMMRLdldelveKLKKHY------------PPDTPVAIVYHAGYSEKEKvIRGT 221


                  ....
gi 1008885855 205 LGEM 208
Cdd:cd11724   222 LDDI 225
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
 5-223 8.01e-16

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: 73.63  E-value: 8.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   5 IGIGPGSQAMMTMEAVEALQAAEIVVgyktYTHLV-----KAFTGDKQVIKTGmcK----------EIerCQAAIELAQA 69
Cdd:cd11642     1 VGAGPGDPDLLTLKALRALQQADVVL----YDRLVspeilALAPPGAELIYVG--KrpgrhsvpqeEI--NELLVELARE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  70 GHNVALISSGDAGIYGMAG-LVLELVNKQrldIEVRLIPGMTASIAAASLLGAPLMH-DFCHiSLSdLLT-------PWS 140
Cdd:cd11642    73 GKRVVRLKGGDPFVFGRGGeEIEALREAG---IPFEVVPGITSAIAAAAYAGIPLTHrGVAS-SVT-FVTgheadgkLPD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855 141 VIEKRIVAAGeadfVICFYNPRSRGREghlaRAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEM----DFAPVDMT 216
Cdd:cd11642   148 DDAALARPGG----TLVIYMGVSNLEE----IAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELaekaAEAGIRSP 219


                  ....*..
gi 1008885855 217 SLVIVGN 223
Cdd:cd11642   220 ALIVVGE 226
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
 5-222 6.61e-15

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: 71.64  E-value: 6.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   5 IGIGPGSQAMMTMEAVEALQAAEIVVgyktYTHLV-----KAFTGDKQVI---KTGMCKEI---ERCQAAIELAQAGHNV 73
Cdd:COG0007     7 VGAGPGDPDLLTLKALRALQQADVVL----YDRLVspeilALARPDAELIyvgKRGGRHSLpqeEINALLVELARAGKRV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  74 ALISSGDAGIYGMAGLVLELVnkQRLDIEVRLIPGMTASIAAASLLGAPLMH-DFC--------HISLSDLLTPWSviek 144
Cdd:COG0007    83 VRLKGGDPFVFGRGGEEAEAL--AAAGIPFEVVPGITAAIAAPAYAGIPLTHrGVAssvtfvtgHEKDGKLDLDWA---- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855 145 rivAAGEADFVICFYNPRSRGRE--------GhlarafallaasKSADTPVGVVKSAGRKKQEKWLTTLGEM----DFAP 212
Cdd:COG0007   157 ---ALARPGGTLVIYMGVKNLPEiaaaliaaG------------RSPDTPVAVIENGTTPDQRVVTGTLATLaelaAEAG 221

                         250
                  ....*....|
gi 1008885855 213 VDMTSLVIVG 222
Cdd:COG0007   222 LKSPALIVVG 231
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
1-127 2.10e-14

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 69.95  E-value: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   1 MLSVIGIGPGSQAMMTMEAVEALQAAEIVV---GYKTYTHL----VKAFTGDKQVIKT---GMCKEIERCQAAIE----- 65
Cdd:PRK05576    3 KLYGIGLGPGDPELLTVKAARILEEADVVYapaSRKGGGSLalniVRPYLKEETEIVElhfPMSKDEEEKEAVWKenaee 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008885855  66 ---LAQAGHNVALISSGDAGIYGMAGLVLELVNkqRLDIEVRLIPGMTASIAAASLLGAPLMHDF 127
Cdd:PRK05576   83 iaaEAEEGKNVAFITLGDPNLYSTFSHLLEYLK--CHDIEVETVPGISSFTAIASRAGVPLAMGD 145
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
 2-123 3.04e-14

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: 69.36  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   2 LSVIGIGPGSQAMMTMEAVEALQAAEIVVGYKTYTH-------LVKAFTGDKQVI---------KTGMCKEIERCQAAI- 64
Cdd:COG2243     5 LYGVGVGPGDPELLTLKAVRALREADVIAYPAKGAGkaslareIVAPYLPPARIVelvfpmttdYEALVAAWDEAAARIa 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1008885855  65 ELAQAGHNVALISSGDAGIYGMAGLVLELVnkQRLDIEVRLIPGMTASIAAASLLGAPL 123
Cdd:COG2243    85 EELEAGRDVAFLTEGDPSLYSTFMYLLERL--RERGFEVEVIPGITSFSAAAAALGIPL 141
PLN02625 PLN02625
uroporphyrin-III C-methyltransferase
 5-223 4.59e-13

uroporphyrin-III C-methyltransferase


Pssm-ID: 178232 [Multi-domain]  Cd Length: 263  Bit Score: 66.58  E-value: 4.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   5 IGIGPGSQAMMTMEAVEALQAAEIVV----GYKTYTHLVKAFTGDKQVIKTGMC---KEIERCQAAIELAQAGHNVALIS 77
Cdd:PLN02625   20 VGTGPGDPDLLTLKALRLLQTADVVLydrlVSPDILDLVPPGAELLYVGKRGGYhsrTQEEIHELLLSFAEAGKTVVRLK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  78 SGDAGIYGMAGLvlELVNKQRLDIEVRLIPGMTASIAAASLLGAPLMH-------DFCHISLSDLLTPwSVIEKRIVAAG 150
Cdd:PLN02625  100 GGDPLVFGRGGE--EMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHrgvatsvRFLTGHDREGGTD-PLDVAEAAADP 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008885855 151 EADFVicFYNPRSRGReghlARAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEM--DFAPVDMTS--LVIVGN 223
Cdd:PLN02625  177 DTTLV--VYMGLGTLP----SLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIaeDVAAAGLVSptVIVVGE 247
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
 5-123 4.91e-13

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


Pssm-ID: 381172 [Multi-domain]  Cd Length: 223  Bit Score: 65.99  E-value: 4.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   5 IGIGPGSQAMMTMEAVEALQAAEIVV--------GYKTYTHLVKAFTGDKQVIKTG--MCKEIERCQAA--------IEL 66
Cdd:cd11645     1 VGVGPGDPELLTLKAVRILKEADVIFvpvskggeGSAALIIAAALLIPDKEIIPLEfpMTKDREELEEAwdeaaeeiAEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1008885855  67 AQAGHNVALISSGDAGIYGMAGLVLELVnkQRLDIEVRLIPGMTASIAAASLLGAPL 123
Cdd:cd11645    81 LKEGKDVAFLTLGDPSLYSTFSYLLERL--RAPGVEVEIIPGITSFSAAAARLGIPL 135
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
 1-123 2.65e-11

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: 61.17  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   1 MLSVIGIGPGSQAMMTMEAVEALQAAEIV-----------VGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAA------ 63
Cdd:TIGR01467   2 KLYGVGVGPGDPELITVKALEALRSADVIavpaskkgresLARKIVEDYLKPNDTRILELVFPMTKDRDELEKAwdeaae 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1008885855  64 --IELAQAGHNVALISSGDAGIYGMAGLVLELVnkQRLDIEVRLIPGMTASIAAASLLGAPL 123
Cdd:TIGR01467  82 avAAELEEGRDVAFLTLGDPSLYSTFSYLLQRL--QGMGIEVEVVPGITSFAACASAAGLPL 141
PRK06136 PRK06136
uroporphyrinogen-III C-methyltransferase;
5-208 2.79e-11

uroporphyrinogen-III C-methyltransferase;


Pssm-ID: 235711  Cd Length: 249  Bit Score: 61.38  E-value: 2.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   5 IGIGPGSQAMMTMEAVEALQAAEIVVgyktYTHLVK----AFTGDK----QVIKTGMC---KEIERCQAAIELAQAGHNV 73
Cdd:PRK06136    8 VGAGPGDPDLITLKGVRLLEQADVVL----YDDLVSpeilAYAKPDaeliYVGKRAGRhstKQEEINRLLVDYARKGKVV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  74 ALISSGDAGIYGMAGLvlELVNKQRLDIEVRLIPGMTASIAAASLLGAPLMHDfcHISLS----------DLLTP---WS 140
Cdd:PRK06136   84 VRLKGGDPFVFGRGGE--ELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHR--GVARSvtfvtgheaaGKLEPevnWS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008885855 141 VIekrivAAGEADFVIcfYNPRSRGREghlaRAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEM 208
Cdd:PRK06136  160 AL-----ADGADTLVI--YMGVRNLPY----IAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTI 216
PRK07168 PRK07168
uroporphyrin-III C-methyltransferase;
4-125 4.33e-11

uroporphyrin-III C-methyltransferase;


Pssm-ID: 180864 [Multi-domain]  Cd Length: 474  Bit Score: 61.93  E-value: 4.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   4 VIGIGPGSQAMMTMEAVEALQAAEIVVgyktYTHLVKAF--TGDKQVIKTGMCKEIERCQAA---------IELAQAGHN 72
Cdd:PRK07168    7 LVGAGPGDEGLITKKAIECLKRADIVL----YDRLLNPFflSYTKQTCELMYCGKMPKNHIMrqeminahlLQFAKEGKI 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1008885855  73 VALISSGDAGIYGMAGLVLELVNKQrlDIEVRLIPGMTASIAAASLLGAPLMH 125
Cdd:PRK07168   83 VVRLKGGDPSIFGRVGEEAETLAAA--NIPYEIVPGITSSIAASSYAGIPLTH 133
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
 5-222 1.04e-08

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: 54.30  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   5 IGIGPGSQAMMTMEAVEALQAAEIVVgyktYT------HLVKAFTGDKQVIKT-GMCKE--IERCQAAielAQAGHNVAL 75
Cdd:COG2875     8 VGAGPGDPDLITVKGRRLLEEADVVL----YAgslvppELLAYCKPGAEIVDSaSMTLEeiIALMKEA---AAEGKDVVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  76 ISSGDAGIYG-----MAGLvlelvnkQRLDIEVRLIPGMTASIAAASLLGAPLmhdfchiSLSDLltPWSVIEKRI---- 146
Cdd:COG2875    81 LHSGDPSLYGaiaeqMRRL-------DALGIPYEVVPGVSAFAAAAAALGREL-------TLPEV--SQTVILTRAegrt 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855 147 -VAAGE--ADFV-----ICFY-------NPRSRGREGHlarafallaaskSADTPVGVVKSAGRKKQEKWLTTLGEMDF- 210
Cdd:COG2875   145 pMPEGEslASLAahgatLAIYlsahridEVVEELLEGY------------PPDTPVAVVYRASWPDEKIVRGTLADIAEk 212

                         250
                  ....*....|....*
gi 1008885855 211 ---APVDMTSLVIVG 222
Cdd:COG2875   213 vkeAGITRTALILVG 227
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
 5-123 1.42e-08

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: 53.55  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   5 IGIGPGSQAMMTMEAVEALQAAEIVVgyktYT------HLVKAFTGDKQVIKT-GMCKEiERCQAAIELAQAGHNVALIS 77
Cdd:cd11641     1 VGAGPGDPELITVKGARLLEEADVVI----YAgslvppELLAYAKPGAEIVDSaGMTLE-EIIEVMREAAREGKDVVRLH 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1008885855  78 SGDAGIYG-----MAGLvlelvnkQRLDIEVRLIPGMTASIAAASLLGAPL 123
Cdd:cd11641    76 TGDPSLYGaireqIDAL-------DKLGIPYEVVPGVSSFFAAAAALGTEL 119
DHP5_DphB cd11647
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ...
 1-120 2.14e-07

diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester synthase (DHP5) and archaeal diphthamide synthase (DphB) participate in the second step of the biosynthetic pathway of diphthamide. The eukaryotic enzyme catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester; the archaeal enzyme, catalyzes only 3 methylations, producing diphthine. Diphtheria toxin ADP-ribosylates diphthamide leading to inhibition of protein synthesis in the eukaryotic host cells.


Pssm-ID: 381174  Cd Length: 241  Bit Score: 50.11  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   1 MLSVIGIGPGSQAMMTMEAVEALQAAEIVVgYKTYTHLVKAFTGDKQVIKTGmcKEI---------ERCQAAIELAQAGh 71
Cdd:cd11647     1 MLYLIGLGLGDEKDITLEGLEALKKADKVY-LEAYTSILPGSKLEELEKLIG--KKIilldredleEESEEILEEAKKK- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1008885855  72 NVALISSGDAgiygMAG-----LVLELVnkqRLDIEVRLIPGmtASI--AAASLLG 120
Cdd:cd11647    77 DVALLVPGDP----LIAtthidLRLEAK---KRGIKVKVIHN--ASIlsAAGSTSG 123
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
 5-222 2.73e-07

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: 50.02  E-value: 2.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   5 IGIGPGSQAMMTMEAVEALQAAEIVVgyktY-------THLVKAFTGDKQVIKTGM-CKEIERCQaaIELAQAGHNVALI 76
Cdd:TIGR01465   4 IGAGPGDPDLITVKGRKLIESADVIL----YagslvppELLAHCRPGAEVVNSAGMsLEEIVDIM--SDAHREGKDVARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  77 SSGDAGIYGmaGLVLELVNKQRLDIEVRLIPGMTASIAAASLLGAPLMHDfcHISLSDLLTPwsvIEKRI-VAAGE--AD 153
Cdd:TIGR01465  78 HSGDPSIYG--AIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVP--EVSQTVILTR---ASGRTpMPEGEklAD 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008885855 154 FV-----ICFYNPRSRGREghlaRAFALLAASKSADTPVGVVKSAGRKKQEKWLTTLGEMDF----APVDMTSLVIVG 222
Cdd:TIGR01465 151 LAkhgatMAIFLSAHILDK----VVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADlvreEGIYRTTLILVG 224
PRK05990 PRK05990
precorrin-2 C(20)-methyltransferase; Reviewed
 5-123 7.16e-07

precorrin-2 C(20)-methyltransferase; Reviewed


Pssm-ID: 180341  Cd Length: 241  Bit Score: 48.83  E-value: 7.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   5 IGIGPGSQAMMTMEAVEALQAAEiVVGYKTYT-------HLVKAFTGDKQV-------IKTGMCKEIERCQAAI------ 64
Cdd:PRK05990    8 LGVGPGDPELLTLKALRLLQAAP-VVAYFVAKgkkgnafGIVEAHLSPGQTllplvypVTTEILPPPLCYETVIadfydt 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008885855  65 ---ELAQ---AGHNVALISSGDAGIYGmAGLVLELVNKQRLDIEVrlIPGMTASIAAASLLGAPL 123
Cdd:PRK05990   87 saeAVAAhldAGRDVAVICEGDPFFYG-SYMYLHDRLAPRYETEV--IPGVCSMLGCWSVLGAPL 148
PRK05948 PRK05948
precorrin-2 C(20)-methyltransferase;
2-123 2.96e-06

precorrin-2 C(20)-methyltransferase;


Pssm-ID: 180320  Cd Length: 238  Bit Score: 46.95  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   2 LSVIGIGPGSQAMMTMEAVEALQ-----------------AAEIVVGYK----TYTHLVKAFTGDKQVIKTGMCKEIerC 60
Cdd:PRK05948    6 LYGISVGPGDPELITLKGLRLLQsapvvafpaglagqpglAEQIIAPWLspqqIKLPLYFPYVQDEEQLEQAWQAAA--D 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1008885855  61 QAAIELAQaGHNVALISSGDAGIYGMAGLVLELVNKQRLDIEVRLIPGMTASIAAASLLGAPL 123
Cdd:PRK05948   84 QVWHYLEQ-GEDVAFACEGDVSFYSTFTYLAQTLQELYPQVAIQTIPGVCSPLAAAAALGIPL 145
cysG PRK10637
siroheme synthase CysG;
4-125 5.53e-06

siroheme synthase CysG;


Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 46.67  E-value: 5.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   4 VIGIGPGSQAMMTMEAVEALQAAEIVVgyktYTHLV-------------KAFTGDKQVIKTGMCKEIErcQAAIELAQAG 70
Cdd:PRK10637  220 LVGAGPGDAGLLTLKGLQQIQQADVVV----YDRLVsddimnlvrrdadRVFVGKRAGYHCVPQEEIN--QILLREAQKG 293

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1008885855  71 HNVALISSGDAGIYGMAGLVLELVnkQRLDIEVRLIPGMTASIAAASLLGAPLMH 125
Cdd:PRK10637  294 KRVVRLKGGDPFIFGRGGEELETL--CNAGIPFSVVPGITAASGCSAYSGIPLTH 346
RsmI_like cd19917
tetrapyrrole methylase family protein similar to ribosomal RNA small subunit methyltransferase ...
 10-130 9.33e-05

tetrapyrrole methylase family protein 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: 381180  Cd Length: 217  Bit Score: 42.33  E-value: 9.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  10 GSQAMMTMEAVEALQAAEIVVG--YKTYTHLVKAFTGDKQVIKT-GMCKEIERCQAAIELAQAGHNVALISsgDAGIYGM 86
Cdd:cd19917     8 GNTDDITLRALETLKAVDLIICedTRNASRLLKHVGIIGKTLEVlNEHNTPEDIQELLDKLAGGKNVALVS--DAGTPAF 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1008885855  87 AGLVLELVNK-QRLDIEVRLIPGMTASIAAASLLGAPLmHDFCHI 130
Cdd:cd19917    86 ADPGADLVKLcRDAGIPVVPLPGASSLMTALSASGLKS-DRFLFY 129
RsmI_like cd19918
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ...
 16-123 4.05e-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: 40.21  E-value: 4.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855  16 TMEAVEALQAAEIVVG--YKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISsgDAGIYGMAGLVLEL 93
Cdd:cd19918    14 TLRALEVLKEVDVIICeeFKEGSRLLKKLIIEKELLLLNEHNEKEDAAELLDLLAQGKSVALIS--DCGTPVFADPGALL 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1008885855  94 VnKQRLD--IEVRLIPGMTASIAAASLLGAPL 123
Cdd:cd19918    92 V-KLCIQkgIPVVPVPGASSLMAALSVSGFKI 122
RsmI cd11648
Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-) ...
 56-122 8.49e-04

Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-)-methyltransferase; RsmI 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: 381175  Cd Length: 216  Bit Score: 39.29  E-value: 8.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1008885855  56 EIERCQAAIELAQAGHNVALISsgDAgiyGMAG-------LVLELVNKqrlDIEVRLIPGMTASIAAASLLGAP 122
Cdd:cd11648    56 EKKRAEKIIELLKEGKSVALVS--DA---GTPGisdpgyrLVRAAIEA---GIEVVPIPGPSAVITALSASGLP 121
Precorrin-6A-synthase cd11643
Precorrin-6A synthase (also named CobF); Precorrin-6A synthase participates in the pathway ...
 4-30 9.91e-04

Precorrin-6A synthase (also named CobF); Precorrin-6A synthase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. This model represents CobF, the precorrin-6A synthase, an enzyme specific to the aerobic pathway. After precorrin-4 is methylated at C-11 by CobM to produce precorrin-5, CobF catalyzes the removal of the extruded acyl group in the subsequent step, and the addition of a methyl group at C-1. The product of this reaction is precorrin-6A, which gets reduced by an NADH-dependent reductase to yield precorrin-6B. This family includes enzymes in GC-rich Gram-positive bacteria, alpha proteobacteria and Pseudomonas-related species.


Pssm-ID: 381170  Cd Length: 244  Bit Score: 39.40  E-value: 9.91e-04
                          10        20
                  ....*....|....*....|....*..
gi 1008885855   4 VIGIGPGSQAMMTMEAVEALQAAEIVV 30
Cdd:cd11643     1 LIGIGPGDPDHLTLQAIEALNRVDVFF 27
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
5-121 2.81e-03

cobalt-precorrin-4 methyltransferase;


Pssm-ID: 185370  Cd Length: 257  Bit Score: 38.20  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008885855   5 IGIGPGSQAMMTMEAVEALQAAEIVV--GYKTYTHLVKaftgdkqviktgMCKEIERCQ--AAIELAQ----------AG 70
Cdd:PRK15473   13 VGAGPGDKELITLKGYRLLQQAQVVIyaGSLINTELLD------------YCPAQAECHdsAELHLEQiidlmeagvkAG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1008885855  71 HNVALISSGDAGIYGMAGLVLELVNKQrlDIEVRLIPGMTASIAAASLLGA 121
Cdd:PRK15473   81 KTVVRLQTGDVSLYGSIREQGEELTKR--GIDFQVVPGVSSFLGAAAELGV 129
 
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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