ID G7G5X9_9GAMM Unreviewed; 338 AA.
AC G7G5X9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=D-erythrose-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01640};
DE Short=E4PDH {ECO:0000256|HAMAP-Rule:MF_01640};
DE EC=1.2.1.72 {ECO:0000256|HAMAP-Rule:MF_01640};
GN Name=epd {ECO:0000256|HAMAP-Rule:MF_01640,
GN ECO:0000313|EMBL:GAA80802.1};
GN ORFNames=P20495_3321 {ECO:0000313|EMBL:GAA80802.1};
OS Pseudoalteromonas sp. BSi20495.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=386429 {ECO:0000313|EMBL:GAA80802.1, ECO:0000313|Proteomes:UP000003050};
RN [1] {ECO:0000313|Proteomes:UP000003050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSi20495 {ECO:0000313|Proteomes:UP000003050};
RX PubMed=22275105; DOI=10.1128/JB.06427-11;
RA Bian F., Xie B.B., Qin Q.L., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA Chen X.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of six Pseudoalteromonas strains isolated from Arctic sea
RT ice.";
RL J. Bacteriol. 194:908-909(2012).
CC -!- FUNCTION: Catalyzes the NAD-dependent conversion of D-erythrose 4-
CC phosphate to 4-phosphoerythronate. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01640}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01640}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01640}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. Epd subfamily. {ECO:0000256|HAMAP-Rule:MF_01640}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01640}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAA80802.1}.
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DR EMBL; BADY01000129; GAA80802.1; -; Genomic_DNA.
DR RefSeq; WP_002961528.1; NZ_BADY01000129.1.
DR AlphaFoldDB; G7G5X9; -.
DR UniPathway; UPA00244; UER00309.
DR Proteomes; UP000003050; Unassembled WGS sequence.
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:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01532; E4PD_g-proteo; 1.
DR NCBIfam; TIGR01534; GAPDH-I; 1.
DR PANTHER; PTHR43148:SF3; D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01640};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01640};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01640};
KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096, ECO:0000256|HAMAP-
KW Rule:MF_01640}.
FT DOMAIN 3..155
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 155
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640,
FT ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640,
FT ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 154..156
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640"
FT BINDING 213..214
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640"
FT BINDING 318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640,
FT ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 182
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640,
FT ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 338 AA; 37177 MW; 23FF90B007827C32 CRC64;
MAIKLAINGF GRIGRNIVRA LYESGLSDDI KIVAINELAD PEAIAHLLKY DTSHGRFSFP
VKLGEDTISV AGDTIALFCE ENPIELPWQT LDVDVVLECT GVYHSREHAQ LHITAGAKKV
LFSHPADNDV DATIVYGIND DELKSEHTIV SNGSCTTNCV VPVIKVLDDA FGIESGAITT
IHASMNDQQV IDGYHHDLRR TRAASQSIIP VDTKLARGID RILPKFKGRF EAIAVRVPTI
NVTAMDLSVT VNTDVDLNAV NNALKAQAKD RLEGILSYTE EPLVSVDFNH DPHSCIIDGT
QTRVSHKRLI KLLVWCDNEW GFANRMLDTA RAMMAVNK
//