CBID_BRUC2
ID CBID_BRUC2 Reviewed; 368 AA.
AC A9M5W0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=BCAN_A1321;
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854;
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000872; ABX62365.1; -; Genomic_DNA.
DR RefSeq; WP_004689777.1; NC_010103.1.
DR AlphaFoldDB; A9M5W0; -.
DR SMR; A9M5W0; -.
DR EnsemblBacteria; ABX62365; ABX62365; BCAN_A1321.
DR GeneID; 45052327; -.
DR GeneID; 55590967; -.
DR KEGG; bcs:BCAN_A1321; -.
DR HOGENOM; CLU_041273_0_0_5; -.
DR OMA; YHGKLIK; -.
DR PhylomeDB; A9M5W0; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000001385; Chromosome I.
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..368
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_1000083589"
SQ SEQUENCE 368 AA; 38588 MW; 5DE0427251BDFFDC CRC64;
MNDETTPANK NPEKAELRCG WTTGACATAA TKAALTALIT GEFPDPVGII LPKGEVPYFQ
LAYEGLGEGY AMAGIVKDAG DDPDVTHGAT IISTVYPAPP GTGIIFRAGE GVGTVTREGL
AIPPGEAAIN PVPRRMMTEI CEAICAEYGL PADLVITISV PGGEEIAQKT WNPRLGIIGG
ISILGTTGVV HPFSCSAWIH SIHRGIDVAR AAGQKHVLGA TGSTSEDAAQ ALYNLPDFAI
LDMGDFAGGV LKYLREHPID RLTIAGGFAK LTKLAQGALD LHSSRSQVDK GFLWQIAERA
GAPADMKERI LLANTAMEVL ELTQSIGIDI AGPIALEARQ TALKTLRGAP VEVEIIVTDR
KGNILARV
