ID   E4PD_VIBPA              Reviewed;         345 AA.
AC   Q87LL0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-NOV-2008, entry version 38.
DE   RecName: Full=D-erythrose-4-phosphate dehydrogenase;
DE            Short=E4PDH;
DE            EC=1.2.1.72;
GN   Name=epd; OrderedLocusNames=VP2601;
OS   Vibrio parahaemolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 / Serotype O3:K6;
RX   MEDLINE=22508454; PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BA000031; BAC60864.1; -; Genomic_DNA.
DR   RefSeq; NP_798980.1; -.
DR   HSSP; P00362; 1GD1.
DR   GeneID; 1190125; -.
DR   GenomeReviews; BA000031_GR; VP2601.
DR   KEGG; vpa:VP2601; -.
DR   NMPDR; fig|223926.1.peg.2601; -.
DR   HOGENOM; Q87LL0; -.
DR   BioCyc; VPAR223926:VP2601-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
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 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_DHase_bac.
DR   InterPro; IPR000173; GlycerAld_3-P_DHase.
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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis.
FT   CHAIN         1    345       D-erythrose-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000293175.
FT   NP_BIND      11     12       NAD (By similarity).
FT   REGION      158    160       Substrate binding (Potential).
FT   REGION      217    218       Substrate binding (Potential).
FT   ACT_SITE    159    159       Nucleophile (By similarity).
FT   BINDING     204    204       Substrate (Potential).
FT   BINDING     240    240       Substrate (Potential).
FT   BINDING     322    322       NAD (By similarity).
FT   SITE        186    186       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   345 AA;  38249 MW;  75AA5F1B623DCEE5 CRC64;
     MLKVAINGFG RIGRNVLRAV YESGKHQQIK VVAVNELAQP EAMAHLLQYD TSHGRFGKKI
     SHDQEHLNVH HESGEYDAIR ILHLSEIELL PWRDLEVDIV LDCTGVYGSK ADGLAHIEAG
     AKKVLFSHPG ANDLDNTIIY GVNHETLKDE HRVVSNGSCT TNCIVPIIKV LDEAFGIESG
     TITTIHSSMN DQQVIDAYHN DLRRTRAASQ SIIPVDTKLH KGIERIFPKF SNKFEAISVR
     VPTVNVTAMD LSVTINTNVK VNDVNQTIVN ASQCTLRNIV DYTESPLVSI DFNHDPHSAI
     VDGTQTRVSN GQLVKMLVWC DNEWGFANRM LDTALAMKAS SQVEL
//