ID   E4PD_COLP3              Reviewed;         339 AA.
AC   Q47XD5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=D-erythrose-4-phosphate dehydrogenase;
DE            Short=E4PDH;
DE            EC=1.2.1.72;
GN   Name=epd; OrderedLocusNames=CPS_3873;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ24567.1; -; Genomic_DNA.
DR   RefSeq; YP_270535.1; -.
DR   GeneID; 3519039; -.
DR   GenomeReviews; CP000083_GR; CPS_3873.
DR   KEGG; cps:CPS_3873; -.
DR   NMPDR; fig|167879.3.peg.3513; -.
DR   TIGR; CPS_3873; -.
DR   HOGENOM; Q47XD5; -.
DR   OMA; Q47XD5; AMDLSVT.
DR   BioCyc; CPSY167879:CPS_3873-MON; -.
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    339       D-erythrose-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000293145.
FT   NP_BIND      12     13       NAD (By similarity).
FT   REGION      154    156       Substrate binding (Potential).
FT   REGION      213    214       Substrate binding (Potential).
FT   ACT_SITE    155    155       Nucleophile (By similarity).
FT   BINDING     236    236       Substrate (Potential).
FT   BINDING     319    319       NAD (By similarity).
FT   SITE        182    182       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   339 AA;  37222 MW;  C5220CA76AD269FD CRC64;
     MTIRIAINGF GRIGRSVVRA LYESGKTDLF TLVSINELAP ASGIAHLLKY DSTHGRFPFS
     VSEKENQLII NGDEIALTHI GNLNSLPWQQ QNIDIVLDCT GKYGNKADGL SHINRGAKKV
     LFSHPGSQDI DATIIYGINH QTLTSSDRVV SNGSCTTNCI VPVIKVIDEA FGVESGSITT
     IHSSMHDQQV IDAYHKDLRL SRAASQSIIP VDTKLAAGIE RILPKFKGRF EAIAVRVPTI
     NVTAMDLSLT VNNDVCICDI NQAIQAATSN HDLYGVLSYT EEPLVSVDFN HDPHSCIVDG
     NQTRVSHKRL IKMLVWCDNE WGFANRMLDT AMAMHQAEN
//