ID   E4PD_IDILO              Reviewed;         341 AA.
AC   Q5QVL6;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-JUN-2009, entry version 35.
DE   RecName: Full=D-erythrose-4-phosphate dehydrogenase;
DE            Short=E4PDH;
DE            EC=1.2.1.72;
GN   Name=epd; OrderedLocusNames=IL2213;
OS   Idiomarina loihiensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=135577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-TR / ATCC BAA-735 / DSM 15497;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S.,
RA   Campbell S., Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV83045.1; -; Genomic_DNA.
DR   RefSeq; YP_156594.1; -.
DR   GeneID; 3174021; -.
DR   GenomeReviews; AE017340_GR; IL2213.
DR   KEGG; ilo:IL2213; -.
DR   NMPDR; fig|283942.3.peg.2200; -.
DR   HOGENOM; Q5QVL6; -.
DR   OMA; Q5QVL6; AMDLSVT.
DR   BioCyc; ILOI283942:IL2213-MON; -.
DR   BRENDA; 1.2.1.72; 280818.
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    341       D-erythrose-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000293150.
FT   NP_BIND      14     15       NAD (By similarity).
FT   REGION      156    158       Substrate binding (Potential).
FT   REGION      215    216       Substrate binding (Potential).
FT   ACT_SITE    157    157       Nucleophile (By similarity).
FT   BINDING     202    202       Substrate (Potential).
FT   BINDING     238    238       Substrate (Potential).
FT   BINDING     320    320       NAD (By similarity).
FT   SITE        184    184       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   341 AA;  37680 MW;  5E307654A8D8D1B8 CRC64;
     MSEPARIAIN GFGRIGRSFL RALYENGYRD SVQVVLINEP AASEAIAHLL KYDSSHGRFG
     EKVTQSGDAL TVAGDNIALT HQTEIEAIDW RAHEVDFVVD CTGVFGSQAD GQLYLQQGVK
     RVLFSHPGKP DVDFTAIYGV NEKELTVDHK VVSNGSCTTN CIVPVIKVLD DAFGIDSGAI
     TTIHSAMHDQ QVIDAYHPDL RRTRAAGRSI IPVDTRLARG IERILPHLEG RFEAIAVRVP
     TTNVTAMDLS VTLNSDATIE QINQVLREQS ERQLAGILDY TEEPLVSIDF NHDPHSSIVD
     GTQTRVSHKR LVKLLCWCDN EWGFANRLLD TAKTMAEQTE H
//