ID   E4PD_SHIFL              Reviewed;         339 AA.
AC   P0A9B9; P11603;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 36.
DE   RecName: Full=D-erythrose-4-phosphate dehydrogenase;
DE            Short=E4PDH;
DE            EC=1.2.1.72;
GN   Name=epd; OrderedLocusNames=SF2911.1, S3112;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   MEDLINE=22272406; PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   MEDLINE=22590274; PubMed=12704152;
RX   DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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.
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DR   EMBL; AE005674; AAN44394.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014073; AAP18216.1; -; Genomic_DNA.
DR   RefSeq; NP_708687.2; -.
DR   RefSeq; NP_838406.1; -.
DR   HSSP; P00362; 1NQO.
DR   GeneID; 1025918; -.
DR   GeneID; 1079373; -.
DR   GenomeReviews; AE005674_GR; SF2911.1.
DR   GenomeReviews; AE014073_GR; S3112.
DR   KEGG; sfx:S3112; -.
DR   HOGENOM; P0A9B9; -.
DR   BioCyc; SFLE198214:AAN44394.1-MON; -.
DR   BRENDA; 1.2.1.72; 189495.
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   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
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   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    339       D-erythrose-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000145679.
FT   NP_BIND      12     13       NAD (By similarity).
FT   REGION      154    156       Substrate binding (Potential).
FT   REGION      213    214       Substrate binding (Potential).
FT   BINDING      81     81       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     200    200       Substrate (Potential).
FT   BINDING     236    236       Substrate (Potential).
FT   BINDING     318    318       NAD (By similarity).
FT   SITE        182    182       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   339 AA;  37299 MW;  4CFC4BD2267EA2A2 CRC64;
     MTVRVAINGF GRIGRNVVRA LYESGRRAEI TVVAINELAD AAGMAHLLKY DTSHGRFAWE
     VRQERDQLFV GDDAIRVLHE RSLQSLPWRE LGVDVVLDCT GVYGSREHGE AHIAAGAKKV
     LFSHPGSNDL DATVVYGVNQ DQLRAEHRIV SNASCTTNCI IPVIKLLDDA YGIESGTVTT
     IHSAMHDQQV IDAYHPDLRR TRAASQSIIP VDTKLAAGIT RFFPQFNDRF EAIAVRVPTI
     NVTAIDLSVT VKKPVKANEV NLLLQKAAQG AFHGIVDYTE LPLVSVDFNH DPHSAIVDGT
     QTRVSGAHLI KTLVWCDNEW GFANRMLDTT LAMATVAFR
//