ID   CBID_METMJ              Reviewed;         337 AA.
AC   A3CSU7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=Memar_0514;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
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; CP000562; ABN56447.1; -; Genomic_DNA.
DR   RefSeq; WP_011843357.1; NC_009051.1.
DR   AlphaFoldDB; A3CSU7; -.
DR   SMR; A3CSU7; -.
DR   STRING; 368407.Memar_0514; -.
DR   EnsemblBacteria; ABN56447; ABN56447; Memar_0514.
DR   GeneID; 4846013; -.
DR   KEGG; mem:Memar_0514; -.
DR   eggNOG; arCOG04383; Archaea.
DR   HOGENOM; CLU_820433_0_0_2; -.
DR   OMA; NDHESDI; -.
DR   OrthoDB; 57676at2157; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000002146; 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   SUPFAM; SSF111342; SSF111342; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..337
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_1000046866"
SQ   SEQUENCE   337 AA;  35742 MW;  2BE2EF86A7D5E1D6 CRC64;
     MRDPVTDFEY PAAWVAACRS PDLLDDVRRG LAVLTASGTV LRRGFSTGTT AAAACKAAIL
     SLACDTVREV DVTLPCGIAV RLAVDGYRGQ ASCRKDAGDY TADVTGGLEF VAMAAPSLSG
     GVQFVPGEGI GSFARDTPRH RRGTPAISAP ALDCIRRSID EAVEEADLSG TTVILTIPRG
     AEVAQKTLNP RVGVHGGISV LGTTGFVEPW DDHMTEGVID RIARAPGAVV LTTGRLGLRY
     SRLLFPEHEA ILVGNKLEEA LRAVEGDAVI CGLPGLILKF MNPDVLSGTG CVTVEELSAT
     PLWEETVRRE LAAFRARYPR VRVVIVDRDG RIIGEPP