CBID_GEOMG
ID CBID_GEOMG Reviewed; 369 AA.
AC Q39YF3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
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}; OrderedLocusNames=Gmet_0478;
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15;
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., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-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}.
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DR EMBL; CP000148; ABB30721.1; -; Genomic_DNA.
DR RefSeq; WP_004513847.1; NC_007517.1.
DR AlphaFoldDB; Q39YF3; -.
DR SMR; Q39YF3; -.
DR STRING; 269799.Gmet_0478; -.
DR PRIDE; Q39YF3; -.
DR EnsemblBacteria; ABB30721; ABB30721; Gmet_0478.
DR KEGG; gme:Gmet_0478; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_0_0_7; -.
DR OMA; YHGKLIK; -.
DR OrthoDB; 1282567at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000007073; 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; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..369
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000257763"
SQ SEQUENCE 369 AA; 39351 MW; 02AC6B693C6E1397 CRC64;
MNTKPLRHGY TTGACAAAAA KGAARMLREQ RPVEEVELVL PKGERVAFRL HGQEFDDSAA
SCFVVKDAGD DPDVTNGAEI HARVRREPLN RSGARTMVFV DGGKGVGTVT KPGLGVGVGN
PAINPVPMRM ITEGVKEEFS VVCLPQVLHV TISIPNGEEL AKKTLNARLG IVGGLSILGT
TGIVRPISAK AWTDTLDAAL DVARACGCET IVLSTGRTSE LVAIHAGIGD RGPGTGKTLP
EEAYVMMGDH VGYALRACAR KGVRHVILVG QFAKLLKIAC GHEQTHVSSS ELDLQMLAEW
LHELGSRSPV PGPWSRYNTA RQVLEESGND SLFMELVCTR ARDAARRLAP SLDIKVLLAG
YDSTVLYFG
