ID A0A0M0HST5_VIBNE Unreviewed; 341 AA.
AC A0A0M0HST5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=gapA {ECO:0000313|EMBL:KOO05124.1};
GN Synonyms=epd {ECO:0000256|HAMAP-Rule:MF_01640};
GN ORFNames=AKJ17_02735 {ECO:0000313|EMBL:KOO05124.1};
OS Vibrio nereis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=693 {ECO:0000313|EMBL:KOO05124.1, ECO:0000313|Proteomes:UP000037515};
RN [1] {ECO:0000313|Proteomes:UP000037515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19584 {ECO:0000313|Proteomes:UP000037515};
RA Giubergia S., Machado H., Mateiu R.V., Gram L.;
RT "Vibrio galatheae sp. nov., a novel member of the Vibrionaceae family
RT isolated from the Solomon Islands.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KOO05124.1}.
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DR EMBL; LHPJ01000002; KOO05124.1; -; Genomic_DNA.
DR RefSeq; WP_053394254.1; NZ_LHPJ01000002.1.
DR AlphaFoldDB; A0A0M0HST5; -.
DR STRING; 693.AKJ17_02735; -.
DR PATRIC; fig|693.5.peg.557; -.
DR OrthoDB; 9803304at2; -.
DR UniPathway; UPA00244; UER00309.
DR Proteomes; UP000037515; 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: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; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01532; E4PD_g-proteo; 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}; Reference proteome {ECO:0000313|Proteomes:UP000037515}.
FT DOMAIN 2..159
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 159
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640,
FT ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 11..12
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 127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 158..160
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640"
FT BINDING 217..218
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640"
FT BINDING 322
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 186
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640,
FT ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 341 AA; 37507 MW; F6EFBAA3F12C6C84 CRC64;
MLKVAINGFG RIGRNVLRAI YESGKSQQIK VVAVNELAQP DAMAHLLQYD TTHGRFGKKV
TNDQEHIYIH HDSGEFDPIR ILHLSEINLL PWRDLEVDIV LDCTGVFGSQ ADGQEHIEAG
AKKVLFSHPG ANDVDNTIIY GVNHDTLTAE HNVVSNGSCT TNCIVPIIKA LDDAFGIDSG
TITTIHSSMN DQQVIDAYHS DLRRTRAASQ SIIPVDTKLH KGIERIFPKF SNKFEAISVR
VPTVNVTAMD LSVTINTNVK VNDVNQTIVN ASQCTLQGIV DYTEAPLVSI DFNHDPHSAI
VDGSQTRVSN GQLVKMLVWC DNEWGFANRM LDTALAMQAA K
//
