ID   E4PD_VIBCH              Reviewed;         341 AA.
AC   P0C6C2; P96153; Q9KUN9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   16-JUN-2009, entry version 12.
DE   RecName: Full=D-erythrose-4-phosphate dehydrogenase;
DE            Short=E4PDH;
DE            EC=1.2.1.72;
GN   Name=epd; OrderedLocusNames=VC_0476;
OS   Vibrio cholerae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961 / Serotype O1;
RX   MEDLINE=20406833; PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A.,
RA   Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
RA   Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
RA   Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
RA   Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
RA   Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF93649.1; ALT_INIT; Genomic_DNA.
DR   PIR; E82317; E82317.
DR   RefSeq; NP_230130.2; -.
DR   HSSP; P17721; 1HDG.
DR   GeneID; 2615270; -.
DR   GenomeReviews; AE003852_GR; VC_0476.
DR   KEGG; vch:VC0476; -.
DR   TIGR; VC_0476; -.
DR   BRENDA; 1.2.1.72; 19019.
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_0000293173.
FT   NP_BIND      11     12       NAD (By similarity).
FT   REGION      158    160       Substrate binding (Potential).
FT   REGION      217    218       Substrate binding (Potential).
FT   ACT_SITE    159    159       Nucleophile (By similarity).
FT   BINDING     204    204       Substrate (Potential).
FT   BINDING     240    240       Substrate (Potential).
FT   BINDING     322    322       NAD (By similarity).
FT   SITE        186    186       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   341 AA;  37773 MW;  91DD2A7442C4891D CRC64;
     MLRVAINGFG RIGRNVLRAV YESGKRDRIQ VVAVNELAKP DAMAHLLQYD TSHGRFGKKI
     SHDQQHIYVH HQNGEYDSIR ILHLSEIPLL PWRDLGVDLV LDCTGVYGCQ EDGQQHIDAG
     AKLVLFSHPG ASDLDNTIIY GVNHETLTAE HKIVSNGSCT TNCIVPIIKV LDDAFGIDSG
     TITTIHSSMN DQQVIDAYHN DLRRTRAASQ SIIPVDTKLH KGIERIFPKF SNKFEAISVR
     VPTVNVTAMD LSVTIKSNVK VNDVNQTIVN ASQCTLRGIV DYTEAPLVSI DFNHDPHSAI
     VDGTQTRVSN GQLVKMLVWC DNEWGFANRM LDTALAMQAT Q
//