ID A0A0X8GT13_9BURK Unreviewed; 315 AA.
AC A0A0X8GT13;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN Name=cobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN ORFNames=VN23_19675 {ECO:0000313|EMBL:AMC36648.1};
OS Janthinobacterium sp. B9-8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1236179 {ECO:0000313|EMBL:AMC36648.1, ECO:0000313|Proteomes:UP000069577};
RN [1] {ECO:0000313|EMBL:AMC36648.1, ECO:0000313|Proteomes:UP000069577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B9-8 {ECO:0000313|EMBL:AMC36648.1,
RC ECO:0000313|Proteomes:UP000069577};
RA Xu X., Jin W., Wu Q., Jiang L., Huang H.;
RT "The whole genome sequence of Janthinbacterium sp. B9-8, a bacterium
RT isolated from low temperature sewage.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC aminopropanol on the F carboxylic group. {ECO:0000256|HAMAP-
CC Rule:MF_00024}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00024}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|HAMAP-Rule:MF_00024}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|HAMAP-Rule:MF_00024}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CobD/CbiB family.
CC {ECO:0000256|ARBA:ARBA00006263, ECO:0000256|HAMAP-Rule:MF_00024}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00024}.
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DR EMBL; CP014222; AMC36648.1; -; Genomic_DNA.
DR RefSeq; WP_046350559.1; NZ_CP014222.1.
DR AlphaFoldDB; A0A0X8GT13; -.
DR STRING; 1236179.VN23_19675; -.
DR KEGG; jab:VN23_19675; -.
DR OrthoDB; 9811967at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000069577; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048472; F:threonine-phosphate decarboxylase activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00024; CobD_CbiB; 1.
DR InterPro; IPR004485; Cobalamin_biosynth_CobD/CbiB.
DR NCBIfam; TIGR00380; cobal_cbiB; 1.
DR PANTHER; PTHR34308; COBALAMIN BIOSYNTHESIS PROTEIN CBIB; 1.
DR PANTHER; PTHR34308:SF1; COBALAMIN BIOSYNTHESIS PROTEIN CBIB; 1.
DR Pfam; PF03186; CobD_Cbib; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00024};
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00024};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00024};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00024};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00024}.
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT TRANSMEM 160..178
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT TRANSMEM 295..314
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
SQ SEQUENCE 315 AA; 34029 MW; D3D3D08D24D62C57 CRC64;
MLNLNPTHWL FAFALALLLE LCLGEPKRFH PLVGFGWLAS KLERRFNPAH LSQIAGQSNL
HNILRGALAW LLLTGASLAA FALLKNFTGW LADALALWFA LGARSLFEHV RAIAQPLSAG
DLPAARLAVS RIVSRNCTEL DETGVAKAGL ESTLENGADA IFASLFFFAL FGGYGVLLHR
LANTLDAMWG YKTPRLFHFG RIAARADDVL NFIPARLTAL SYALLGHSRS AFSCWQNQAP
LWDSPNAGPV MASGAGALQV SLGGEATYHG EIHSRPQLGC GPVPSAHDLQ RGIVLVQKTL
ALWIALLFGG SLWML
//