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CBID_BURCJ
ID   CBID_BURCJ              Reviewed;         362 AA.
AC   B4E9C7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-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};
GN   OrderedLocusNames=BceJ2315_16910; ORFNames=BCAL1728;
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=216591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX   PubMed=18931103; DOI=10.1128/jb.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(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; AM747720; CAR52027.1; -; Genomic_DNA.
DR   RefSeq; WP_006484852.1; NC_011000.1.
DR   AlphaFoldDB; B4E9C7; -.
DR   SMR; B4E9C7; -.
DR   STRING; 216591.BCAL1728; -.
DR   EnsemblBacteria; CAR52027; CAR52027; BCAL1728.
DR   KEGG; bcj:BCAL1728; -.
DR   eggNOG; COG1903; Bacteria.
DR   HOGENOM; CLU_041273_0_0_4; -.
DR   OMA; YHGKLIK; -.
DR   OrthoDB; 1282567at2; -.
DR   BioCyc; BCEN216591:G1G1V-1912-MON; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000001035; Chromosome 1.
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; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..362
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_1000133729"
SQ   SEQUENCE   362 AA;  37525 MW;  AD20FFD5528D287D CRC64;
     MRDETPEQPA PLRFGYTTGS CATATSLAAA RLLLTGHADD AVEIVLPKGQ RVMMRLEFCR
     TTADGAEAGT IKDAGDDPDV THGALIFARV ARAAAPGVRF HAGPGVGTVT RAGLTLPVGE
     PAINPVPRQM MTTHLEALAA EHGYAGGFDV TIGVEGGEAL ALKTMNPRLG IVGGLSILGT
     TGIVRPFSCS AYIASIHQGI DVARANGITH IAACTGNASE DAMRAHYQLP DMALIEMGDF
     AGAVLKHLRR APVARLSMCG GFGKLSKLAA GHLDLHSRHS SIDLPLLAQW AAEAGASDAL
     QAAMRAANTS QEALKLAQAD AVPLGDLVCA HALQVARDIV PPSVAVEMFA IDRQGRFVGA
     AR
 
 
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