ID   COBD_PSEU5              Reviewed;         303 AA.
AC   A4VJ38;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000255|HAMAP-Rule:MF_00024};
GN   Name=cobD {ECO:0000255|HAMAP-Rule:MF_00024}; OrderedLocusNames=PST_1295;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP78989.1; -; Genomic_DNA.
DR   RefSeq; WP_011912473.1; NC_009434.1.
DR   AlphaFoldDB; A4VJ38; -.
DR   STRING; 379731.PST_1295; -.
DR   EnsemblBacteria; ABP78989; ABP78989; PST_1295.
DR   KEGG; psa:PST_1295; -.
DR   eggNOG; COG1270; Bacteria.
DR   HOGENOM; CLU_054212_1_0_6; -.
DR   OMA; WGYRNER; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000233; 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; IPR031347; AmpE.
DR   InterPro; IPR004485; Cobalamin_biosynth_CobD/CbiB.
DR   PANTHER; PTHR34308; PTHR34308; 1.
DR   Pfam; PF17113; AmpE; 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..303
FT                   /note="Cobalamin biosynthesis protein CobD"
FT                   /id="PRO_1000090207"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
SQ   SEQUENCE   303 AA;  32866 MW;  C0EC2DC37BFCBA4E CRC64;
     MSVFLSVIGA LLLDALLGEP KRAHPLVAFG RLADRLEQHF NGAAGRGWRS HGVTAWCLAV
     LPLTLLAWLL SLLPGIGWLA EIVLLYLALG LRSLGEHALP VAQALWRHDL PEARRRVACI
     VSRDTSQLDE EGVARAATES VLENGSDAVF AALFWFIVAG APGVVLYRLS NTLDAMWGYR
     NARFERFGWA AARIDDLLNY VPARLVAVTY ALLGRTRRAL RCWRTQAPLW DSPNAGPVMA
     AGAGALGVVL GGAAIYHGEL HARPELGRGS APQARHIEHA LDLVWAGVGV WLLVLLFGGW
     LYA