ID   COBD_CITK8              Reviewed;         319 AA.
AC   A8AEP3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000255|HAMAP-Rule:MF_00024};
GN   Name=cobD {ECO:0000255|HAMAP-Rule:MF_00024}; OrderedLocusNames=CKO_00804;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) 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:0000255|HAMAP-
CC       Rule:MF_00024}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00024}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00024};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00024}.
CC   -!- SIMILARITY: Belongs to the CobD/CbiB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00024}.
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DR   EMBL; CP000822; ABV11956.1; -; Genomic_DNA.
DR   RefSeq; WP_012131777.1; NC_009792.1.
DR   AlphaFoldDB; A8AEP3; -.
DR   STRING; 290338.CKO_00804; -.
DR   EnsemblBacteria; ABV11956; ABV11956; CKO_00804.
DR   GeneID; 45135001; -.
DR   KEGG; cko:CKO_00804; -.
DR   HOGENOM; CLU_054212_0_0_6; -.
DR   OMA; WGYRNER; -.
DR   OrthoDB; 2029688at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000008148; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   PANTHER; PTHR34308; PTHR34308; 1.
DR   Pfam; PF03186; CobD_Cbib; 1.
DR   TIGRFAMs; TIGR00380; cobD; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cobalamin biosynthesis; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..319
FT                   /note="Cobalamin biosynthesis protein CobD"
FT                   /id="PRO_1000074378"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
SQ   SEQUENCE   319 AA;  35395 MW;  8491E062B6FA8B04 CRC64;
     MTVLAWCIAW LLDFVIGDPQ NWPHPVRWIG NLISATQRVV RRYCHSDRSL RIGGAVMWLV
     VVGVTWAVSW GVLALASEIH PWFGWLVEIW MIFTVLAGRC LANAARDVER PLRAGDLAES
     REKLSWIVGR DTSQLQPEQV NRAVVETVAE NTVDGIIAPL FFLFLGGAPL AMAYKAVNTL
     DSMVGYKHEK YRAIGMVSAR LDDIANVIPA RLSWLLLSIA AALCRYDGYR ALHIGWRDRY
     NHSSPNCAWS EASVAGALGI RLGGPNDYFG ERVEKPWIGD AQRGISVDDI SRTIRLMWVA
     STLALALFIA VRCLLVGAA