ID   CBIC_METJA              Reviewed;         210 AA.
AC   Q58340;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Cobalt-precorrin-8 methylmutase;
DE            EC=5.4.99.60;
DE   AltName: Full=Cobalt-precorrin isomerase;
GN   Name=cbiC; Synonyms=cobH; OrderedLocusNames=MJ0930;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate.
CC       {ECO:0000250}.
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   -!- 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; L77117; AAB98932.1; -; Genomic_DNA.
DR   PIR; B64416; B64416.
DR   RefSeq; WP_010870444.1; NC_000909.1.
DR   AlphaFoldDB; Q58340; -.
DR   SMR; Q58340; -.
DR   STRING; 243232.MJ_0930; -.
DR   EnsemblBacteria; AAB98932; AAB98932; MJ_0930.
DR   GeneID; 1451819; -.
DR   KEGG; mja:MJ_0930; -.
DR   eggNOG; arCOG02247; Archaea.
DR   HOGENOM; CLU_084703_1_1_2; -.
DR   InParanoid; Q58340; -.
DR   OMA; GAPIFCD; -.
DR   OrthoDB; 71138at2157; -.
DR   PhylomeDB; Q58340; -.
DR   UniPathway; UPA00148; UER00230.
DR   Proteomes; UP000000805; Chromosome.
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   3: Inferred from homology;
KW   Cobalamin biosynthesis; Isomerase; Reference proteome.
FT   CHAIN           1..210
FT                   /note="Cobalt-precorrin-8 methylmutase"
FT                   /id="PRO_0000135928"
FT   ACT_SITE        47
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   210 AA;  22974 MW;  2B5773E46E3105E6 CRC64;
     MGAISKDGLN IANKSREIVR NKIKEVLGDR INEFNEKEMG IIERVVHATA DPEYAKLLVF
     KNNPIEEGIK AIKEEKPIIV DVNMIKAGIR YNKVHCFINH PDVYEVAKKE GITRAVASMR
     LAKDLIDDGI VVIGNSPTAL FEVIRLVKEE NIKPKLIVGV PVGFVQASES KEALREVNVP
     SISTIGPKGG TPVAVAIING IIAYAKNEKA