ID   E4PD_SHEON              Reviewed;         338 AA.
AC   Q8EIB2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 50.
DE   RecName: Full=D-erythrose-4-phosphate dehydrogenase;
DE            Short=E4PDH;
DE            EC=1.2.1.72;
GN   Name=epd; OrderedLocusNames=SO_0931;
OS   Shewanella oneidensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=70863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   MEDLINE=22297686; PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A.,
RA   Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S.,
RA   Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A.,
RA   White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M.,
RA   Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J.,
RA   Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O.,
RA   Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN54005.1; -; Genomic_DNA.
DR   RefSeq; NP_716560.1; -.
DR   HSSP; P00362; 1DBV.
DR   GeneID; 1168777; -.
DR   GenomeReviews; AE014299_GR; SO_0931.
DR   KEGG; son:SO_0931; -.
DR   NMPDR; fig|211586.1.peg.868; -.
DR   TIGR; SO_0931; -.
DR   HOGENOM; Q8EIB2; -.
DR   OMA; Q8EIB2; AMDLSVT.
DR   BioCyc; SONE211586:SO_0931-MON; -.
DR   BRENDA; 1.2.1.72; 257422.
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    338       D-erythrose-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000293164.
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;  37241 MW;  FB58AA57643E8006 CRC64;
     MIRVAINGYG RIGRSILRAL YESGKRQQIQ IVAINELAKP EAIIHLTQYD TTHGRFQPRV
     KLVDGQMQIG DDTIKIFHEP DPAKLPWREL DIDIVYEATG AILDRQSCEA HIHAGAKQVL
     ISHPSSADVD GTIVYGVNHD LLRAEHTVVS NASCTTNCIV PVIDVLDKHF GVKSGAITTI
     HSAMNDQQVI DAYHDDLRRT RAAGQSIIPV DTKLARGIER ILPHMKDKFE AISVRVPTIN
     VTAIDLSVTL DKTVDIATVN QVLELAANGR FNGILGYTDE PLVSCDFNHD PRSSIVDGTQ
     TRVSAGQLVK LLLWCDNEWG FANRMLDTSL AMIAAKQS
//