ID   E4PD_PSEA6              Reviewed;         342 AA.
AC   Q15QK3;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=D-erythrose-4-phosphate dehydrogenase;
DE            Short=E4PDH;
DE            EC=1.2.1.72;
GN   Name=epd; OrderedLocusNames=Patl_3329;
OS   Pseudoalteromonas atlantica (strain T6c / BAA-1087).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=342610;
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.;
RT   "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL   Submitted (JUN-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; CP000388; ABG41835.1; -; Genomic_DNA.
DR   RefSeq; YP_662889.1; -.
DR   GeneID; 4175106; -.
DR   GenomeReviews; CP000388_GR; Patl_3329.
DR   KEGG; pat:Patl_3329; -.
DR   NMPDR; fig|342610.3.peg.1260; -.
DR   HOGENOM; Q15QK3; -.
DR   OMA; Q15QK3; AMDLSVT.
DR   BioCyc; PATL342610:PATL_3329-MON; -.
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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis.
FT   CHAIN         1    342       D-erythrose-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000293153.
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   342 AA;  37500 MW;  E5283885B5CC349A CRC64;
     MIRVAINGFG RVGRNVLRAL YETGQNKQIQ IVAINELAEP EGVAHLLKYD TAHGRFRFPV
     VLDNQQLVVA GDHITLLQQE NIRDLPWAQL DIDVVLECTG VNNERVHGEQ HIAQGAKKVL
     FSQPCGPDVD ATIIMGINEE SLKASDSIVS AGSCTTNCIV PVIQVLDEAF SVSSGTITTI
     HSSMHDQQVI DAYHPDLRRT RAASQSIIPV DTKLARGIER VLPKFAGKFE AIAVRVPTIN
     VSAMDLSVTL DAKVTIDDVN QALKTVKNGR LNGILDFTEE PLVSVDFNHD AHSCIVDGTQ
     TRVSHKQLVK LLVWCDNEWG FSNRMIDIVL VMNTLSLGNT GK
//