ID   E4PD_YERE8              Reviewed;         338 AA.
AC   A1JPR1;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=D-erythrose-4-phosphate dehydrogenase;
DE            Short=E4PDH;
DE            EC=1.2.1.72;
GN   Name=epd; OrderedLocusNames=YE3415;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain 8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the
RT   high pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Catalyzes the NAD-dependent conversion of D-erythrose 4-
CC       phosphate to 4-phosphoerythronate (By similarity).
CC   -!- CATALYTIC ACTIVITY: D-erythrose 4-phosphate + NAD(+) + H(2)O = 4-
CC       phosphoerythronate + NADH.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 1/5.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family. Epd subfamily.
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DR   EMBL; AM286415; CAL13439.1; -; Genomic_DNA.
DR   RefSeq; YP_001007581.1; -.
DR   GeneID; 4713807; -.
DR   GenomeReviews; AM286415_GR; YE3415.
DR   KEGG; yen:YE3415; -.
DR   NMPDR; fig|630.2.peg.3340; -.
DR   OMA; A1JPR1; AMDLSVT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0048001; F:erythrose-4-phosphate dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:InterPro.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01640; -; 1.
DR   InterPro; IPR006422; E4P_DH_bac.
DR   InterPro; IPR000173; GlycerAld_3-P_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR10836; GAP_DH; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   TIGRFAMs; TIGR01532; E4PD_g-proteo; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis.
FT   CHAIN         1    338       D-erythrose-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000293178.
FT   NP_BIND      12     13       NAD (By similarity).
FT   REGION      154    156       Substrate binding (Potential).
FT   REGION      213    214       Substrate binding (Potential).
FT   ACT_SITE    155    155       Nucleophile (By similarity).
FT   BINDING     200    200       Substrate (Potential).
FT   BINDING     236    236       Substrate (Potential).
FT   BINDING     318    318       NAD (By similarity).
FT   SITE        182    182       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   338 AA;  37075 MW;  D4D3E2DF8E0237D0 CRC64;
     MTIRIAINGF GRIGRSVLRA LYESGRRAEI SVVAINELAN AEGMAHLLKY DSSHGRFAWD
     VRQECDKLYV GDDIIRLIHQ PEIEQLPWGE LGIDVVLDCS GVYGSRADGE AHLTSGAKKV
     LFAHPGGHDL DATVVYGVNH QDLQADHRIV SNASCTTNCI IPIIQLLDVA FGIESGTVTT
     IHSSMNDQPV IDAYHQDLRR TRAASQSIIP VDTKLAAGIT RIFPKFCDRF EAISVRVPTI
     NVTAIDLSVS VTSPVDVAEV NQLLQKAARG SFRGIVDYTE LPLVSTDFNH DPHSAIVDCT
     QTRVSGQHLI KTLVWCDNEW GFANRMLDTT LAMARSGF
//