ID   CBID_MAGSA              Reviewed;         357 AA.
AC   Q2W3X9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=amb2642;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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; AP007255; BAE51446.1; -; Genomic_DNA.
DR   RefSeq; WP_011385022.1; NC_007626.1.
DR   AlphaFoldDB; Q2W3X9; -.
DR   SMR; Q2W3X9; -.
DR   STRING; 342108.amb2642; -.
DR   EnsemblBacteria; BAE51446; BAE51446; amb2642.
DR   KEGG; mag:amb2642; -.
DR   HOGENOM; CLU_041273_0_0_5; -.
DR   OMA; YHGKLIK; -.
DR   OrthoDB; 1282567at2; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000007058; 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   PIRSF; PIRSF026782; CbiD; 1.
DR   SUPFAM; SSF111342; SSF111342; 1.
DR   TIGRFAMs; TIGR00312; cbiD; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..357
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_0000257765"
SQ   SEQUENCE   357 AA;  36765 MW;  0460DF8373DD1764 CRC64;
     MADEQALRQG WTTGACATAA AKAACCALLG DGFPDPVGID LPGGRTPAFA LALAEMGEGW
     ARAGIVKDAG DDPDVTHGAT IIATLRHGIA GAGLVFRAGR GVGIVTRPGL PLAVGEPAIN
     PVPRRLMAEA VAAIAARHGM ACDLEIEISV PGGEDIALRT WNPRLGILGG ISILGTTGVV
     IPYSCSAWIH SIQRGIDVAR ACGLIHVAGC VGSTSEKAVR KVRGLGEEAI IDMGDFAGGM
     LKYLRRHPIP RVTIAGGFAK MCKLAAGQMD LHSSRSQVDM VWLAAQLRSL GADAALVAAS
     AQANTALEVL ELAEGFPLGQ AIARQARAAA REVLDNPEVS LDVLVVDRQG RVIGDAH