CBIC_METTH
ID CBIC_METTH Reviewed; 206 AA.
AC O26329;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=MTH_227;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB84733.1; -; Genomic_DNA.
DR PIR; B69128; B69128.
DR AlphaFoldDB; O26329; -.
DR SMR; O26329; -.
DR STRING; 187420.MTH_227; -.
DR EnsemblBacteria; AAB84733; AAB84733; MTH_227.
DR KEGG; mth:MTH_227; -.
DR PATRIC; fig|187420.15.peg.196; -.
DR HOGENOM; CLU_084703_1_1_2; -.
DR OMA; GAPIFCD; -.
DR UniPathway; UPA00148; UER00230.
DR Proteomes; UP000005223; 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..206
FT /note="Cobalt-precorrin-8 methylmutase"
FT /id="PRO_0000135929"
FT ACT_SITE 44
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 206 AA; 21904 MW; DC45675682D12FF6 CRC64;
MMGASTGQGY EIARKSREIV RELISEDISS LGPAEVAIVE RIVHSTADPE YARITEFSQG
FVDEALRSLR SSGGILTDIE MVRAGISHPS RCYIREPAVR ELAEKRDITR AAASMEYAAS
QGFRGIVVIG NAPTALMKVI ELTLEGLMDA RAVIGVPVGF VGAAESKEAL RGTEIPHMIT
RGPKGGTPVA VAAANALIAL SKDKEV
