ID   E4PD_SHEDO              Reviewed;         342 AA.
AC   Q12QA4;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=D-erythrose-4-phosphate dehydrogenase;
DE            Short=E4PDH;
DE            EC=1.2.1.72;
GN   Name=epd; OrderedLocusNames=Sden_1084;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
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., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-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; CP000302; ABE54372.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_562095.1; -.
DR   GeneID; 4017367; -.
DR   GenomeReviews; CP000302_GR; Sden_1084.
DR   KEGG; sdn:Sden_1084; -.
DR   NMPDR; fig|318161.14.peg.1066; -.
DR   HOGENOM; Q12QA4; -.
DR   BioCyc; SDEN318161:SDEN_1084-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; 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   PROSITE; PS00071; GAPDH; 1.
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_0000293161.
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;  37587 MW;  CB10920796C0C700 CRC64;
     MIRVAINGYG RIGRSILRAL YESGKRQQIQ IVAINELAKP EAIRHLTQYD TTHGRFGQTV
     ELQEGKLHIG DDAIALFHQS DATKLPWGEL DIDIVFEASG SLIEREACEA HIISGAKQVL
     ISHPSSQDVD ATIVYGVNHH LLAAEHTVVS NASCTTNCIV PVIDVLDSHF GVISGAITTI
     HSAMNDQQVI DAYHDDLRRT RAAGQSIIPV DTKLARGIER ILPKMKDKFE AISVRVPTIN
     VTAIDVSVTL RDRVDISIIN SVLQQAAKGR FDGILGYTDE PLVSCDFNHD PRSSIVDATQ
     TRVSDGHLVK LLLWCDNEWG FANRMLDTSL AMIRAKSAKS VK
//