ID A0A0P7XSY8_9RHOB Unreviewed; 315 AA.
AC A0A0P7XSY8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN Name=cbiB {ECO:0000313|EMBL:KPQ07288.1};
GN Synonyms=cobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN ORFNames=HLUCCA12_05615 {ECO:0000313|EMBL:KPQ07288.1};
OS Rhodobacteraceae bacterium HLUCCA12.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666916 {ECO:0000313|EMBL:KPQ07288.1, ECO:0000313|Proteomes:UP000050476};
RN [1] {ECO:0000313|EMBL:KPQ07288.1, ECO:0000313|Proteomes:UP000050476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA12 {ECO:0000313|EMBL:KPQ07288.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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:KPQ07288.1}.
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DR EMBL; LJSV01000004; KPQ07288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7XSY8; -.
DR STRING; 1666916.HLUCCA12_05615; -.
DR PATRIC; fig|1666916.3.peg.1290; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000050476; 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 57..80
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; 32820 MW; 2B1497525E3A677B CRC64;
MSFATVMLIA LALDAVLGWP DALFRRIGHP VTWIGQMIAA ADRRLNRAQD TPARRRALGL
IAAIAIIALC AALGGSVQWI LPDSSLGTLV AGVLAWPLLA MRSLHDHVKA VATPLMAGDM
AAARRAVSMI VGRDPAALEA GGIGGAAIES LAENTSDGVV APLVWGVVLG LPGIAAYKAI
NTLDSMIGHR TARHAAFGWA AARIDDLANL VPARLTGLLF VLVSVHARRA WACMRQDASK
HRSPNAGWPE AAMAGAIGVR LSGPRVYGGA SSPEPWLNAN AADPQPADLR RALSLFRRAM
AAMACGLVLI MLVGG
//