ID A4ES59_9RHOB Unreviewed; 303 AA.
AC A4ES59;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN Name=cobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN ORFNames=RSK20926_05822 {ECO:0000313|EMBL:EBA17229.1};
OS Roseobacter sp. SK209-2-6.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=388739 {ECO:0000313|EMBL:EBA17229.1, ECO:0000313|Proteomes:UP000005964};
RN [1] {ECO:0000313|EMBL:EBA17229.1, ECO:0000313|Proteomes:UP000005964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK209-2-6 {ECO:0000313|EMBL:EBA17229.1,
RC ECO:0000313|Proteomes:UP000005964};
RA Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2006) 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:EBA17229.1}.
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DR EMBL; AAYC01000003; EBA17229.1; -; Genomic_DNA.
DR RefSeq; WP_008205025.1; NZ_AAYC01000003.1.
DR AlphaFoldDB; A4ES59; -.
DR eggNOG; COG1270; Bacteria.
DR OrthoDB; 9811967at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000005964; 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 Reference proteome {ECO:0000313|Proteomes:UP000005964};
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 57..90
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT TRANSMEM 148..166
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT TRANSMEM 284..302
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
SQ SEQUENCE 303 AA; 32303 MW; BF2A727EDBEB6EC7 CRC64;
MSQASLLIAA LILDALVGEP NWLWSRLPHP AVLMGKCVSW LDHTLNSGAK KRLKGCLAAA
ALLLGGLCIG WLLSFLGPIA EVLIAAILLA QRSLVEHIKA VAIGLGQSLA QGQKAVSMIV
SRDTGEMTAP QVARSAIESG SENMSDGVIA PAFWFLVAGL PGLIAYKMIN TGDSMIGYHN
DRYEEFGWGT ARLDDLVNLL PARLTGLLLA AVGGSLRQWP EIAADARRHR SPNAGWPEAA
IARALGLSLA GPRSYDGEMR DFPWVNAKGA KSSTGYSILR AAEMLWRAWG LALALLVAFA
LIF
//
