ID   E4PD_SHEFN              Reviewed;         339 AA.
AC   Q087Q7;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=D-erythrose-4-phosphate dehydrogenase;
DE            Short=E4PDH;
DE            EC=1.2.1.72;
GN   Name=epd; OrderedLocusNames=Sfri_0648;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T.,
RA   Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F.,
RA   Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000447; ABI70508.1; -; Genomic_DNA.
DR   RefSeq; YP_749346.1; -.
DR   GeneID; 4278604; -.
DR   GenomeReviews; CP000447_GR; Sfri_0648.
DR   KEGG; sfr:Sfri_0648; -.
DR   NMPDR; fig|318167.10.peg.616; -.
DR   HOGENOM; Q087Q7; -.
DR   OMA; Q087Q7; 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   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    339       D-erythrose-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000293162.
FT   NP_BIND      11     12       NAD (By similarity).
FT   REGION      153    155       Substrate binding (Potential).
FT   REGION      212    213       Substrate binding (Potential).
FT   ACT_SITE    154    154       Nucleophile (By similarity).
FT   BINDING     199    199       Substrate (Potential).
FT   BINDING     235    235       Substrate (Potential).
FT   BINDING     317    317       NAD (By similarity).
FT   SITE        181    181       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   339 AA;  37508 MW;  F085995094CD2924 CRC64;
     MIRVAINGYG RIGRSILRAL YESGKRQQIQ IVAINELAKP EAICHLTQYD TTHGRFKHTV
     KLNGDQLLIG DDSILLLNQP DANLLPWAEL DIDIVYEATG SLIDRQACEA HIHAGAKQVL
     ISHPSSADVD ETIVYGVNHD LLRAEHTVIS NASCTTNCIV PVIDVLDKHF EVKSGAITTI
     HSAMNDQQVI DAYHDDLRRT RAAGQSIIPV DTKLARGIER ILPHMKDKFE AISVRVPTIN
     VTAIDLSVTL EKKVNIEQIN SVLQRASNGS FNGILGYTDE PLVSCDFNHD PRSSIVDGTQ
     TRVSAGHLVK LLLWCDNEWG FANRMLDTSL AMIQAKLDR
//