CBID_PROM9
ID CBID_PROM9 Reviewed; 370 AA.
AC Q31DE8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Cobalt-precorrin-5B C(1)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00787};
DE EC=2.1.1.195 {ECO:0000255|HAMAP-Rule:MF_00787};
DE AltName: Full=Cobalt-precorrin-6A synthase {ECO:0000255|HAMAP-Rule:MF_00787};
GN Name=cbiD {ECO:0000255|HAMAP-Rule:MF_00787};
GN OrderedLocusNames=PMT9312_0036;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to
CC form cobalt-precorrin-6A. {ECO:0000255|HAMAP-Rule:MF_00787}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:26285, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:60063, ChEBI:CHEBI:60064;
CC EC=2.1.1.195; Evidence={ECO:0000255|HAMAP-Rule:MF_00787};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC step 6/10. {ECO:0000255|HAMAP-Rule:MF_00787}.
CC -!- SIMILARITY: Belongs to the CbiD family. {ECO:0000255|HAMAP-
CC Rule:MF_00787}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB49097.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000111; ABB49097.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_036924448.1; NC_007577.1.
DR AlphaFoldDB; Q31DE8; -.
DR SMR; Q31DE8; -.
DR STRING; 74546.PMT9312_0036; -.
DR EnsemblBacteria; ABB49097; ABB49097; PMT9312_0036.
DR KEGG; pmi:PMT9312_0036; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_1_2_3; -.
DR OMA; YHGKLIK; -.
DR OrthoDB; 1282567at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000002715; Chromosome.
DR GO; GO:0043780; F:cobalt-precorrin-5B C1-methyltransferase activity; IEA:RHEA.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046140; P:corrin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2110.10; -; 1.
DR HAMAP; MF_00787; CbiD; 1.
DR InterPro; IPR002748; CbiD.
DR InterPro; IPR036074; CbiD_sf.
DR PANTHER; PTHR35863; PTHR35863; 1.
DR Pfam; PF01888; CbiD; 1.
DR PIRSF; PIRSF026782; CbiD; 1.
DR SUPFAM; SSF111342; SSF111342; 1.
DR TIGRFAMs; TIGR00312; cbiD; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..370
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000257770"
SQ SEQUENCE 370 AA; 41294 MW; 5856A44643133150 CRC64;
MKKGFSLPLW VAGAARSALK KLVGLPFDNY ELIKIPNEKK EIKIEIHSVG LLKDDSHALG
ISFAKSGLYL DITQNLEIWT IASLERNSFN NPLQTNPINI IAGSGVGIKE DTSEICISDF
AKEVLYENLL DIIPEGFNLK LEIIFPNGVF LAERTSNKSF GIVDGLSIIG TSAETYSSAS
PDQLEEAKTN LAKLVQNDFK GKVVFVIGEN GLNLAKNCNL KFPILKVGNW IGPLIVDAAI
KKVKTVILFG YHGKLIKLAG GIFHTHNHLA DGRIEILVYL AVQEKVPTEI IVQLSHLKNL
EEALLLLERF DKSIAEKLFL NLSNTIEKRS FTYVNRYVKT DMEIASIIFD RKREIRWAGT
YGNKYISDFQ
