ID   COBD_PYRAB              Reviewed;         290 AA.
AC   Q9V2M8; G8ZFM8;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Probable cobalamin biosynthesis protein CobD;
GN   Name=cobD; Synonyms=cbib; OrderedLocusNames=PYRAB00470; ORFNames=PAB0025;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC       aminopropanol on the F carboxylic group. {ECO:0000250}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CobD/CbiB family. {ECO:0000305}.
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DR   EMBL; AJ248283; CAB48970.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69419.1; -; Genomic_DNA.
DR   PIR; C75190; C75190.
DR   RefSeq; WP_010867171.1; NC_000868.1.
DR   AlphaFoldDB; Q9V2M8; -.
DR   STRING; 272844.PAB0025; -.
DR   EnsemblBacteria; CAB48970; CAB48970; PAB0025.
DR   GeneID; 1494930; -.
DR   KEGG; pab:PAB0025; -.
DR   PATRIC; fig|272844.11.peg.54; -.
DR   eggNOG; arCOG04274; Archaea.
DR   HOGENOM; CLU_054212_0_2_2; -.
DR   OMA; NSGYTMA; -.
DR   OrthoDB; 101304at2157; -.
DR   PhylomeDB; Q9V2M8; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..290
FT                   /note="Probable cobalamin biosynthesis protein CobD"
FT                   /id="PRO_0000150943"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   290 AA;  32994 MW;  43CFA216E45B8871 CRC64;
     MNPLILLGLA LIWDLLLGEP PAKIHPVVWF GKIAGFLDNR WRRRGKIGFL AGAFVTFIIV
     ALAFFLSLIP SYLTFPLDYL LAIYLLKSSF AIRSLYEHVA RTVTEDIEEK RKTVSMIVSR
     DVKVLDLAHL NSAAIESLAE NLNDSVVAPL FYFMLFGLPG AMVYRAVNTL DAMFGYRDER
     YEYFGKFPAR LDDILNFIPA RLTVLLYLPF GVKVLKYYKL ARFKINSDKP IAAMSAVLGV
     WLEKPGAYRF PGREPRDEDI KRALDVYKLV VAEYLSIVFV LKVVQLCLNP