E4PD_SHEON
ID E4PD_SHEON Reviewed; 338 AA.
AC Q8EIB2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=D-erythrose-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01640};
DE Short=E4PDH {ECO:0000255|HAMAP-Rule:MF_01640};
DE EC=1.2.1.72 {ECO:0000255|HAMAP-Rule:MF_01640};
GN Name=epd {ECO:0000255|HAMAP-Rule:MF_01640}; OrderedLocusNames=SO_0931;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
CC -!- FUNCTION: Catalyzes the NAD-dependent conversion of D-erythrose 4-
CC phosphate to 4-phosphoerythronate. {ECO:0000255|HAMAP-Rule:MF_01640}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrose 4-phosphate + H2O + NAD(+) = 4-phospho-D-
CC erythronate + 2 H(+) + NADH; Xref=Rhea:RHEA:12056, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16897, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58766; EC=1.2.1.72;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01640};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 1/5.
CC {ECO:0000255|HAMAP-Rule:MF_01640}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01640}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01640}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. Epd subfamily. {ECO:0000255|HAMAP-Rule:MF_01640}.
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DR EMBL; AE014299; AAN54005.1; -; Genomic_DNA.
DR RefSeq; NP_716560.1; NC_004347.2.
DR RefSeq; WP_011071211.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EIB2; -.
DR SMR; Q8EIB2; -.
DR STRING; 211586.SO_0931; -.
DR PaxDb; Q8EIB2; -.
DR KEGG; son:SO_0931; -.
DR PATRIC; fig|211586.12.peg.893; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_0_6; -.
DR OMA; YVQITTI; -.
DR OrthoDB; 944149at2; -.
DR PhylomeDB; Q8EIB2; -.
DR BioCyc; SONE211586:G1GMP-868-MON; -.
DR UniPathway; UPA00244; UER00309.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0048001; F:erythrose-4-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01640; E4P_dehydrog; 1.
DR InterPro; IPR006422; E4P_DH_bac.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43148; PTHR43148; 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 SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01532; E4PD_g-proteo; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis;
KW Reference proteome.
FT CHAIN 1..338
FT /note="D-erythrose-4-phosphate dehydrogenase"
FT /id="PRO_0000293164"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 153..155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 212..213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 317
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT SITE 181
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
SQ SEQUENCE 338 AA; 37241 MW; FB58AA57643E8006 CRC64;
MIRVAINGYG RIGRSILRAL YESGKRQQIQ IVAINELAKP EAIIHLTQYD TTHGRFQPRV
KLVDGQMQIG DDTIKIFHEP DPAKLPWREL DIDIVYEATG AILDRQSCEA HIHAGAKQVL
ISHPSSADVD GTIVYGVNHD LLRAEHTVVS NASCTTNCIV PVIDVLDKHF GVKSGAITTI
HSAMNDQQVI DAYHDDLRRT RAAGQSIIPV DTKLARGIER ILPHMKDKFE AISVRVPTIN
VTAIDLSVTL DKTVDIATVN QVLELAANGR FNGILGYTDE PLVSCDFNHD PRSSIVDGTQ
TRVSAGQLVK LLLWCDNEWG FANRMLDTSL AMIAAKQS
