E4PD_VIBC3
ID E4PD_VIBC3 Reviewed; 341 AA.
AC A5F9G1; C3LX29; P96153; Q9KUN9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 88.
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};
GN OrderedLocusNames=VC0395_A0029, VC395_0520;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RX PubMed=8982014; DOI=10.1128/jb.179.1.293-296.1997;
RA Carroll P.A., Zhao G., Boyko S.A., Winkler M.E., Calderwood S.B.;
RT "Identification, sequencing, and enzymatic activity of the erythrose-4-
RT phosphate dehydrogenase gene of Vibrio cholerae.";
RL J. Bacteriol. 179:293-296(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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 ECO:0000269|PubMed:8982014};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABQ20538.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ACP08539.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U72152; AAC44767.1; -; Genomic_DNA.
DR EMBL; CP000627; ABQ20538.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001235; ACP08539.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000946626.1; NZ_JAACZH010000029.1.
DR AlphaFoldDB; A5F9G1; -.
DR SMR; A5F9G1; -.
DR STRING; 345073.VC395_0520; -.
DR PRIDE; A5F9G1; -.
DR EnsemblBacteria; ABQ20538; ABQ20538; VC0395_A0029.
DR GeneID; 57739222; -.
DR KEGG; vco:VC0395_A0029; -.
DR KEGG; vcr:VC395_0520; -.
DR PATRIC; fig|345073.21.peg.508; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_2_6; -.
DR UniPathway; UPA00244; UER00309.
DR Proteomes; UP000000249; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0048001; F:erythrose-4-phosphate dehydrogenase activity; IDA:CACAO.
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 1: Evidence at protein level;
KW Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis.
FT CHAIN 1..341
FT /note="D-erythrose-4-phosphate dehydrogenase"
FT /id="PRO_0000321845"
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 341 AA; 37773 MW; 91DD2A7442C4891D CRC64;
MLRVAINGFG RIGRNVLRAV YESGKRDRIQ VVAVNELAKP DAMAHLLQYD TSHGRFGKKI
SHDQQHIYVH HQNGEYDSIR ILHLSEIPLL PWRDLGVDLV LDCTGVYGCQ EDGQQHIDAG
AKLVLFSHPG ASDLDNTIIY GVNHETLTAE HKIVSNGSCT TNCIVPIIKV LDDAFGIDSG
TITTIHSSMN DQQVIDAYHN DLRRTRAASQ SIIPVDTKLH KGIERIFPKF SNKFEAISVR
VPTVNVTAMD LSVTIKSNVK VNDVNQTIVN ASQCTLRGIV DYTEAPLVSI DFNHDPHSAI
VDGTQTRVSN GQLVKMLVWC DNEWGFANRM LDTALAMQAT Q
