ID   CBID_METB6              Reviewed;         334 AA.
AC   A7I7N1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Mboo_1224;
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX   PubMed=25998264; DOI=10.1099/mic.0.000117;
RA   Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA   Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT   "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT   peatland environments.";
RL   Microbiology 161:1572-1581(2015).
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; CP000780; ABS55742.1; -; Genomic_DNA.
DR   RefSeq; WP_012106773.1; NC_009712.1.
DR   AlphaFoldDB; A7I7N1; -.
DR   SMR; A7I7N1; -.
DR   STRING; 456442.Mboo_1224; -.
DR   EnsemblBacteria; ABS55742; ABS55742; Mboo_1224.
DR   GeneID; 5411903; -.
DR   KEGG; mbn:Mboo_1224; -.
DR   eggNOG; arCOG04383; Archaea.
DR   HOGENOM; CLU_820433_0_0_2; -.
DR   OMA; NDHESDI; -.
DR   OrthoDB; 57676at2157; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000002408; 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; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..334
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_1000046863"
SQ   SEQUENCE   334 AA;  34634 MW;  6BB93078449C8B1D CRC64;
     MRDPVTGFVY PAAWVEKVSD PAGLEKVRGG SAVLTSSGTV LLRGYTTGTT AAAACKAAIL
     SLAGDISRVT IQLPCGLSAD LPVKARAGHA SCRKYAGDYP SDVTAGIEFI ADAAVAQKGI
     LLVPGPGIGH FVRDTPRYKK REPAISTAPL ACILSSMEEA LGATGLSGAT VTLSIPEGRT
     IADQTLNPRI GIEGGISVLG STGLVEPWDD HLEDSVIARV AGATDPVITT GRVGLRYARL
     LFPDREVVLA GGKIKGALAA AKGEVTLCGL PALILKYIEP HILDKTGYAT VEELAASPSF
     PSVALPILVA YKKKHPRVRV VLVNREGTVI AESP