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Database: UniProt
Entry: Q6LMN0
LinkDB: Q6LMN0
Original site: Q6LMN0 
ID   E4PD_PHOPR              Reviewed;         360 AA.
AC   Q6LMN0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   19-FEB-2014, entry version 71.
DE   RecName: Full=D-erythrose-4-phosphate dehydrogenase;
DE            Short=E4PDH;
DE            EC=1.2.1.72;
GN   Name=epd; OrderedLocusNames=PBPRA3132;
OS   Photobacterium profundum (Photobacterium sp. (strain SS9)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=74109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N.,
RA   Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N.,
RA   Romualdi C., Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and
RT   expression analysis.";
RL   Science 307:1459-1461(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   -!- SEQUENCE CAUTION:
CC       Sequence=CAG21447.1; Type=Erroneous initiation;
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DR   EMBL; CR378673; CAG21447.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_131249.2; NC_006370.1.
DR   ProteinModelPortal; Q6LMN0; -.
DR   STRING; 298386.PBPRA3132; -.
DR   PRIDE; Q6LMN0; -.
DR   EnsemblBacteria; CAG21447; CAG21447; PBPRA3132.
DR   GeneID; 3123661; -.
DR   KEGG; ppr:PBPRA3132; -.
DR   PATRIC; 22937319; VBIPhoPro109272_3284.
DR   eggNOG; COG0057; -.
DR   HOGENOM; HOG000071679; -.
DR   KO; K03472; -.
DR   OMA; TTHGRFQ; -.
DR   OrthoDB; EOG66TG3S; -.
DR   ProtClustDB; PRK13535; -.
DR   UniPathway; UPA00244; UER00309.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0048001; F:erythrose-4-phosphate dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.720; -; 1.
DR   HAMAP; MF_01640; E4P_dehydrog; 1.
DR   InterPro; IPR006422; E4P_DH_bac.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR10836; PTHR10836; 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   SMART; SM00846; Gp_dh_N; 1.
DR   TIGRFAMs; TIGR01532; E4PD_g-proteo; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis.
FT   CHAIN         1    360       D-erythrose-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000293152.
FT   NP_BIND      12     13       NAD (By similarity).
FT   REGION      159    161       Substrate binding (Potential).
FT   REGION      218    219       Substrate binding (Potential).
FT   ACT_SITE    160    160       Nucleophile (By similarity).
FT   BINDING     205    205       Substrate (Potential).
FT   BINDING     241    241       Substrate (Potential).
FT   BINDING     323    323       NAD (By similarity).
FT   SITE        187    187       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   360 AA;  39834 MW;  71F1F3068FD89B04 CRC64;
     MTLKVAINGF GRIGRSVLRA LYESGKHHHI NVVAVNELAE PEAMAHLLQY DSSHGRFFKP
     VSHDQEHLFI AHENGERDDI RILHQSDITL LPWHDLDVDI VLDCTGVYGS REDGLAHIKA
     GAKKVLFSHP AANDIDNTII YGVNHKTLTS EHRIVSNGSC TTNCIVPVIK IIDDAFGIES
     GTITTIHSAM NDQQVIDGYH SDLRRTRAAS QSIIPVDTKL HLGIGRIFPK FVDKFEAISV
     RVPTINVTAM DLSVTVKTNV KVNDVNQALS EVSRCTLEGI VDYTEAPLVS IDFNHDPHSA
     IVDGTQTRVS NKHLIKLLVW CDNEWGFANR MLDTALAMHA SDAAQHSNKE LRSKIAIKNS
//
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