ID A0A0R2TQ23_9RHOB Unreviewed; 304 AA.
AC A0A0R2TQ23;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN Name=cobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN ORFNames=ABR89_05790 {ECO:0000313|EMBL:KRO89317.1};
OS Rhodobacter sp. BACL10 MAG-120910-bin24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1655597 {ECO:0000313|EMBL:KRO89317.1, ECO:0000313|Proteomes:UP000051243};
RN [1] {ECO:0000313|EMBL:KRO89317.1, ECO:0000313|Proteomes:UP000051243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL7 MAG-120910-bin24 {ECO:0000313|EMBL:KRO89317.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRO89317.1}.
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DR EMBL; LICH01000028; KRO89317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2TQ23; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000051243; Unassembled WGS sequence.
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 58..91
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT TRANSMEM 286..303
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
SQ SEQUENCE 304 AA; 32744 MW; 28F69F8D464A9195 CRC64;
MITAAWLFCA LLLDAIFGEP KWLWGRFPHP AVLMGRAIDA LDRAFNKGEQ RRLKGLMVLA
FLVLSAWALG KLVGLLPFAN LITIAIAAML LAQKSLVTHV RAVALALRLS LNDGRLAVSM
IVGRDISSLD EAGVARGAIE SAAENLSDGV IAPAFWFLLG GLPGILIYKI TNTADSMIGH
RTPRHEEFGW ATARFDDLLN LIPARLCALL IALSAARLDA LAPILRDAPL HRSPNAGWPE
AAMAVVLNLR LSGPRSYNGQ TQDFPYLYPE GANPADASAI ETATQVLWRS WAVVLGAVAL
LALF
//