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Database: UniProt
Entry: B5R3Q1
LinkDB: B5R3Q1
Original site: B5R3Q1 
ID   PDXB_SALEP              Reviewed;         378 AA.
AC   B5R3Q1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   05-DEC-2018, entry version 67.
DE   RecName: Full=Erythronate-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01825};
DE            EC=1.1.1.290 {ECO:0000255|HAMAP-Rule:MF_01825};
GN   Name=pdxB {ECO:0000255|HAMAP-Rule:MF_01825};
GN   OrderedLocusNames=SEN2352;
OS   Salmonella enteritidis PT4 (strain P125109).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P125109;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K.,
RA   Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A.,
RA   Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G.,
RA   Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and
RT   Salmonella gallinarum 287/91 provides insights into evolutionary and
RT   host adaptation pathways.";
RL   Genome Res. 18:1624-1637(2008).
CC   -!- FUNCTION: Catalyzes the oxidation of erythronate-4-phosphate to 3-
CC       hydroxy-2-oxo-4-phosphonooxybutanoate. {ECO:0000255|HAMAP-
CC       Rule:MF_01825}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-
CC         phosphooxybutanoate + H(+) + NADH; Xref=Rhea:RHEA:18829,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58538, ChEBI:CHEBI:58766; EC=1.1.1.290;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01825};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 2/5. {ECO:0000255|HAMAP-Rule:MF_01825}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01825}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01825}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. PdxB subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01825}.
DR   EMBL; AM933172; CAR33936.1; -; Genomic_DNA.
DR   RefSeq; WP_000699176.1; NC_011294.1.
DR   ProteinModelPortal; B5R3Q1; -.
DR   SMR; B5R3Q1; -.
DR   EnsemblBacteria; CAR33936; CAR33936; SEN2352.
DR   KEGG; set:SEN2352; -.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   BioCyc; SENT550537:G1G1W-2582-MONOMER; -.
DR   UniPathway; UPA00244; UER00310.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd12158; ErythrP_dh; 1.
DR   Gene3D; 3.30.1370.170; -; 1.
DR   HAMAP; MF_01825; PdxB; 1.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR020921; Erythronate-4-P_DHase.
DR   InterPro; IPR024531; Erythronate-4-P_DHase_dimer.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR038251; PdxB_dimer_sf.
DR   PANTHER; PTHR42938:SF3; PTHR42938:SF3; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF11890; DUF3410; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis.
FT   CHAIN         1    378       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_1000188276.
FT   ACT_SITE    208    208       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    237    237       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    254    254       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      45     45       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      66     66       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING     146    146       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     175    175       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     232    232       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     257    257       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     258    258       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   378 AA;  41279 MW;  CDA527833ED2825A CRC64;
     MKILVDENMP YARELFSRLG EVKAVPGRPI PVEELNHADA LMVRSVTKVN ESLLSGTPIN
     FVGTATAGTD HVDEAWLKQA GIGFSAAPGC NAIAVVEYVF SALLMLAERD GFSLRDRTIG
     IVGVGNVGSR LQTRLEALGI RTLLCDPPRA ARGDEGDFRT LDELVQEADV LTFHTPLYKD
     GPYKTLHLAD ETLIRRLKPG AILINACRGP VVDNAALLAR LNAGQPLSVV LDVWEGEPDL
     NVALLEAVDI GTSHIAGYTL EGKARGTTQV FEAYSAFIGR EQHVALETLL PAPEFGRITL
     HGPLDQPTLK RLAHLVYDVR RDDAPLRKVA GIPGEFDKLR KNYLERREWS SLYVMCDDET
     AAALLCKLGF NAVHHPAH
//
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