E4PD_VIBPA
ID E4PD_VIBPA Reviewed; 345 AA.
AC Q87LL0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=VP2601;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC60864.1; -; Genomic_DNA.
DR RefSeq; NP_798980.1; NC_004603.1.
DR RefSeq; WP_005461726.1; NC_004603.1.
DR AlphaFoldDB; Q87LL0; -.
DR SMR; Q87LL0; -.
DR STRING; 223926.28807611; -.
DR EnsemblBacteria; BAC60864; BAC60864; BAC60864.
DR GeneID; 1190125; -.
DR KEGG; vpa:VP2601; -.
DR PATRIC; fig|223926.6.peg.2498; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_2_6; -.
DR OMA; NAKVLAW; -.
DR UniPathway; UPA00244; UER00309.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0048001; F:erythrose-4-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis;
KW Reference proteome.
FT CHAIN 1..345
FT /note="D-erythrose-4-phosphate dehydrogenase"
FT /id="PRO_0000293175"
FT ACT_SITE 159
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 158..160
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 217..218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 322
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT SITE 186
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
SQ SEQUENCE 345 AA; 38249 MW; 75AA5F1B623DCEE5 CRC64;
MLKVAINGFG RIGRNVLRAV YESGKHQQIK VVAVNELAQP EAMAHLLQYD TSHGRFGKKI
SHDQEHLNVH HESGEYDAIR ILHLSEIELL PWRDLEVDIV LDCTGVYGSK ADGLAHIEAG
AKKVLFSHPG ANDLDNTIIY GVNHETLKDE HRVVSNGSCT TNCIVPIIKV LDEAFGIESG
TITTIHSSMN DQQVIDAYHN DLRRTRAASQ SIIPVDTKLH KGIERIFPKF SNKFEAISVR
VPTVNVTAMD LSVTINTNVK VNDVNQTIVN ASQCTLRNIV DYTESPLVSI DFNHDPHSAI
VDGTQTRVSN GQLVKMLVWC DNEWGFANRM LDTALAMKAS SQVEL
