ID   CBID_RHORT              Reviewed;         357 AA.
AC   Q8GDE1; Q2RQ04;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=Rru_A2996;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Roth E., Sommer H., Abou-Aisha K., Saegesser R., Ghosh R.;
RT   "The carotenoid gene cluster of Rhodospirillum rubrum S1 contains genes for
RT   cobalamin biosynthesis.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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; AY150801; AAN75025.1; -; Genomic_DNA.
DR   EMBL; CP000230; ABC23791.1; -; Genomic_DNA.
DR   RefSeq; WP_011390744.1; NC_007643.1.
DR   RefSeq; YP_428078.1; NC_007643.1.
DR   AlphaFoldDB; Q8GDE1; -.
DR   SMR; Q8GDE1; -.
DR   STRING; 269796.Rru_A2996; -.
DR   EnsemblBacteria; ABC23791; ABC23791; Rru_A2996.
DR   KEGG; rru:Rru_A2996; -.
DR   PATRIC; fig|269796.9.peg.3104; -.
DR   eggNOG; COG1903; Bacteria.
DR   HOGENOM; CLU_041273_0_0_5; -.
DR   OMA; YHGKLIK; -.
DR   OrthoDB; 1282567at2; -.
DR   PhylomeDB; Q8GDE1; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000001929; 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.
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_0000141682"
SQ   SEQUENCE   357 AA;  36399 MW;  9F79B2FABBB18112 CRC64;
     MDEADEGRSL RRGWTTGACA TAALKAALEA LVDRPFPDPV ALTLPRGERP AFALATRETG
     PGWARAGVIK DAGDDPDVTH GALIEATARL LPKGSGLIFR AGSGVGTVTK PGLPLAVGEP
     AINPVPRAMM TEVATAAGLA DLEISIAVAQ GASIALRTWN PRLGILGGLS ILGTTGVVVP
     YSCSAWIHSI RRGVDVARAT GRAHVVGTTG ATSERAALDH LGLDAEAVID MGDFVGGLLK
     YLRDHPIPHL TIAGGFAKLS KLADGALDLH SKRAQVDIPA LARRLAALGA TQAVVSEAER
     ANTALEVLTL AQAAGLPLAT AIAFEAATVA RAVLGEAPVR VSVLVVDRGG RVVGEGG