ID A0A1U7DKU2_9RHOB Unreviewed; 363 AA.
AC A0A1U7DKU2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Cobalt-precorrin-5B C(1)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00787};
DE EC=2.1.1.195 {ECO:0000256|HAMAP-Rule:MF_00787};
DE AltName: Full=Cobalt-precorrin-6A synthase {ECO:0000256|HAMAP-Rule:MF_00787};
GN Name=cbiD {ECO:0000256|HAMAP-Rule:MF_00787};
GN ORFNames=BV394_12910 {ECO:0000313|EMBL:APX90513.1};
OS Brevirhabdus pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Brevirhabdus.
OX NCBI_TaxID=1267768 {ECO:0000313|EMBL:APX90513.1, ECO:0000313|Proteomes:UP000187266};
RN [1] {ECO:0000313|EMBL:APX90513.1, ECO:0000313|Proteomes:UP000187266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY6-4 {ECO:0000313|EMBL:APX90513.1,
RC ECO:0000313|Proteomes:UP000187266};
RA Wang X.;
RT "Genomic analysis of Xuhuaishuia manganoxidans DY6-4.";
RL Submitted (JAN-2017) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00787}.
CC -!- SIMILARITY: Belongs to the CbiD family. {ECO:0000256|HAMAP-
CC Rule:MF_00787}.
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DR EMBL; CP019124; APX90513.1; -; Genomic_DNA.
DR RefSeq; WP_076980530.1; NZ_PGFI01000012.1.
DR AlphaFoldDB; A0A1U7DKU2; -.
DR STRING; 1267768.BV394_12910; -.
DR OrthoDB; 6439987at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000187266; 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; CbiD-like; 1.
DR HAMAP; MF_00787; CbiD; 1.
DR InterPro; IPR002748; CbiD.
DR InterPro; IPR036074; CbiD_sf.
DR NCBIfam; TIGR00312; cbiD; 1.
DR PANTHER; PTHR35863; COBALT-PRECORRIN-5B C(1)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR35863:SF1; COBALT-PRECORRIN-5B C(1)-METHYLTRANSFERASE; 1.
DR Pfam; PF01888; CbiD; 1.
DR PIRSF; PIRSF026782; CbiD; 1.
DR SUPFAM; SSF111342; CbiD-like; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00787};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_00787}; Reference proteome {ECO:0000313|Proteomes:UP000187266};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00787};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00787}.
SQ SEQUENCE 363 AA; 37108 MW; 9B177DB78CC82C28 CRC64;
MARKPPGPLR TGFTTGACAT AAAAAATEAL LGGAWPDPVR IRLPRGQEPA FPLHDRLAEP
GAATATVRKD AGDDPDVTHG ALIRARVSRG AAGQGVRFHA GEGVGIVTRP GLPVPVGEPA
INPVPRRMMT ETLEGIARDH AVAADFDVTI SVPGGAELAL QTWNPRLGIE GGISILGTTG
IVRPFSCAAW IASIHRGVDV ARAGGLSHVA GSTGATSERA AQEMLGLPDH AMLDMGDFAG
GLLKYLARHP VAQLTIAGGM GKLTKLAQGA LDLHSARSQV DFAQLGEWAA GLGLDGGRIA
RANTVLEAFE IARAADPAGA DRLAGEIVAR ARDTARAALG DAPVAPRVIG FDREGGLLAD
SDV
//
