ID   CBIC_PRIMG              Reviewed;         225 AA.
AC   O87692;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Cobalt-precorrin-8 methylmutase;
DE            EC=5.4.99.60;
DE   AltName: Full=Cobalt-precorrin isomerase;
GN   Name=cbiC;
OS   Priestia megaterium (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 509 / CCM 1464 / NBRC 12109;
RX   PubMed=9742225; DOI=10.1042/bj3350159;
RA   Raux E., Lanois A., Warren M.J., Rambach A., Thermes C.;
RT   "Cobalamin (vitamin B12) biosynthesis: identification and characterization
RT   of a Bacillus megaterium cobI operon.";
RL   Biochem. J. 335:159-166(1998).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=23922391; DOI=10.1073/pnas.1308098110;
RA   Moore S.J., Lawrence A.D., Biedendieck R., Deery E., Frank S., Howard M.J.,
RA   Rigby S.E., Warren M.J.;
RT   "Elucidation of the anaerobic pathway for the corrin component of cobalamin
RT   (vitamin B12).";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:14906-14911(2013).
CC   -!- FUNCTION: Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate.
CC       {ECO:0000269|PubMed:23922391}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-8X = cob(II)yrinate; Xref=Rhea:RHEA:16209,
CC         ChEBI:CHEBI:58894, ChEBI:CHEBI:70792; EC=5.4.99.60;
CC         Evidence={ECO:0000269|PubMed:23922391};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 9/10.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CobH/CbiC family. {ECO:0000305}.
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DR   EMBL; AJ000758; CAA04310.1; -; Genomic_DNA.
DR   PIR; T44686; T44686.
DR   AlphaFoldDB; O87692; -.
DR   SMR; O87692; -.
DR   BioCyc; MetaCyc:MON-18417; -.
DR   UniPathway; UPA00148; UER00230.
DR   GO; GO:0043778; F:cobalt-precorrin-8 methylmutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016993; F:precorrin-8X methylmutase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.10230; -; 1.
DR   InterPro; IPR003722; Cbl_synth_CobH/CbiC.
DR   InterPro; IPR036588; CobH/CbiC_sf.
DR   Pfam; PF02570; CbiC; 1.
DR   SUPFAM; SSF63965; SSF63965; 1.
PE   1: Evidence at protein level;
KW   Cobalamin biosynthesis; Isomerase.
FT   CHAIN           1..225
FT                   /note="Cobalt-precorrin-8 methylmutase"
FT                   /id="PRO_0000430344"
FT   ACT_SITE        47
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   225 AA;  24520 MW;  D91EA60ED8EB3BCB CRC64;
     MDFRTEFKPL TVQPQQIEGK SFEMITEELG PHPFTDEQYP IVQRVIHRSA DFELGRSMLF
     HPDAIQAGIK AIRSGKQVVA DVQMVQVGTN KQRIEKHGGE IKVYISDSDV MEEAKRLNTT
     RAIISMRKAI KEADGGIFAI GNAPTALLEL IRLIKEGEAK PGLVIGLPVG FVSAAESKEE
     LAKLYVPFIT NIGRKGGSTV TVAALNAISI LADSGVTYEG SAKRT