ID   E4PD_SHESR              Reviewed;         338 AA.
AC   Q0HRM3;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-NOV-2008, entry version 20.
DE   RecName: Full=D-erythrose-4-phosphate dehydrogenase;
DE            Short=E4PDH;
DE            EC=1.2.1.72;
GN   Name=epd; OrderedLocusNames=Shewmr7_3249;
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481;
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., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
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.
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; CP000444; ABI44232.1; -; Genomic_DNA.
DR   RefSeq; YP_739289.1; -.
DR   GeneID; 4256941; -.
DR   GenomeReviews; CP000444_GR; Shewmr7_3249.
DR   KEGG; shm:Shewmr7_3249; -.
DR   NMPDR; fig|60481.10.peg.3063; -.
DR   HOGENOM; Q0HRM3; -.
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; 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_0000293167.
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   338 AA;  37229 MW;  792397BC6A173702 CRC64;
     MIRVAINGYG RIGRSILRAL YESGKRQQIQ IVAINELAKP EAIVHLTQYD TTHGRFQPRV
     KLVDDQMLIG DDVIKILHEP DPAKLPWREM DIDIVYEATG AILDRNSCEA HIHAGAKQVL
     ISHPSSADVD GTIVYGVNQD LLRAEHTVVS NASCTTNCIV PVIDVLDKHF GVKSGAITTI
     HSAMNDQQVI DAYHDDLRRT RAAGQSIIPV DTKLARGIER ILPHMKDKFE AISVRVPTIN
     VTAIDLSVTL DKTVDIATVN QVLELAANGR FNGILGYTDE PLVSCDFNHD PRSSIVDGTQ
     TRVSAGQLVK LLLWCDNEWG FANRMLDTSL AMIAAKQS
//