ID   CBID_RALSO              Reviewed;         383 AA.
AC   Q8XS59;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=RSp0622;
GN   ORFNames=RS03745;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG   Plasmid megaplasmid Rsp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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; AL646053; CAD17773.1; -; Genomic_DNA.
DR   RefSeq; WP_011003920.1; NC_003296.1.
DR   AlphaFoldDB; Q8XS59; -.
DR   SMR; Q8XS59; -.
DR   STRING; 267608.RSp0622; -.
DR   EnsemblBacteria; CAD17773; CAD17773; RSp0622.
DR   GeneID; 60503538; -.
DR   KEGG; rso:RSp0622; -.
DR   PATRIC; fig|267608.8.peg.4092; -.
DR   eggNOG; COG1903; Bacteria.
DR   HOGENOM; CLU_041273_1_0_4; -.
DR   OMA; YHGKLIK; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000001436; Plasmid megaplasmid Rsp.
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; Plasmid; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..383
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_0000141681"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   383 AA;  40107 MW;  B9508D5FFC7100E5 CRC64;
     MQPSARRPFD LATPAPNGLR RGRTTGTCAT AAVKAALLRL VRGETVDAVE VSLPDPDYCL
     EVPIARIEPL ASGAVRADVL KYAGDDPDNT DGATIFAEVS VNHAGEVRFM AAPGVGTVTQ
     PGLRVPPGEP AINPVPRQMM RMAVDEVLAG GANPGFDLAI GCVDGERIAR RTFNPMLGIV
     GGISILGTSG IVEPMSLAAW MASIEVYVRV ALGDAPEAIA FTPGKIGRAY AAHPLALSKK
     QVVQIANFIG ASLDYAQTAL EEDRHRLGTL WVLGHPGKLA KVLDGVWDTH SSKSGMAMGS
     VAAVAAELGV AAALVEQIKT ANTVENVIQI LQHQPGAQAF WTEIEQRIAA RMQPRVPRAD
     RVAVRLFAMD GTPLGAAGQE AGA