CBID_BRUA4
ID CBID_BRUA4 Reviewed; 368 AA.
AC A6X049;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Oant_1887;
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(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; CP000758; ABS14603.1; -; Genomic_DNA.
DR RefSeq; WP_012091866.1; NC_009667.1.
DR AlphaFoldDB; A6X049; -.
DR SMR; A6X049; -.
DR STRING; 439375.Oant_1887; -.
DR EnsemblBacteria; ABS14603; ABS14603; Oant_1887.
DR KEGG; oan:Oant_1887; -.
DR PATRIC; fig|439375.7.peg.1987; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_0_0_5; -.
DR OMA; YHGKLIK; -.
DR OrthoDB; 1282567at2; -.
DR PhylomeDB; A6X049; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000002301; 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; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..368
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_1000046868"
SQ SEQUENCE 368 AA; 38543 MW; 756AFC98868A2425 CRC64;
MNDETAPTNK SQEKAELRRG WTTGACATAA TKAALTALIT GEFPDPVGII LPKGEVPYFQ
LAYEGLGDGY AMAGIVKDAG DDPDVTHGAT IISTVFPAPP GTGVVFRAGE GVGTVTRPGL
QIPPGEAAIN PVPRRMMTEI CEQICAEYGL PADIVITISV PGGEEIAKKT WNPRLGIVGG
ISILGTTGVV HPFSCSAWIH SIHRGIDVAR AAGQKHVLGA TGSTSEDAAQ ALYDLPDFAI
LDMGDFAGGV LKYLREHPID KLTIAGGFAK LTKLAQGALD LHSSRSQVDK SFLWTLAEKA
GAPESMKDQI LFANTALEVL ELTQSIGLDM ATPIALKAKE TALETLRGAP VAVEIIVTDR
SGNILARV
