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Database: UniProt
Entry: A0A2D0KWL3_9GAMM
LinkDB: A0A2D0KWL3_9GAMM
Original site: A0A2D0KWL3_9GAMM 
ID   A0A2D0KWL3_9GAMM        Unreviewed;       375 AA.
AC   A0A2D0KWL3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Erythronate-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01825};
DE            EC=1.1.1.290 {ECO:0000256|HAMAP-Rule:MF_01825};
GN   Name=pdxB {ECO:0000256|HAMAP-Rule:MF_01825};
GN   ORFNames=Xsto_00116 {ECO:0000313|EMBL:PHM67826.1};
OS   Xenorhabdus stockiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351614 {ECO:0000313|EMBL:PHM67826.1, ECO:0000313|Proteomes:UP000222366};
RN   [1] {ECO:0000313|EMBL:PHM67826.1, ECO:0000313|Proteomes:UP000222366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17904 {ECO:0000313|EMBL:PHM67826.1,
RC   ECO:0000313|Proteomes:UP000222366};
RX   PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA   Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA   Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA   Ebersberger I., Bode H.B.;
RT   "Natural product diversity associated with the nematode symbionts
RT   Photorhabdus and Xenorhabdus.";
RL   Nat. Microbiol. 2:1676-1685(2017).
CC   -!- FUNCTION: Catalyzes the oxidation of erythronate-4-phosphate to 3-
CC       hydroxy-2-oxo-4-phosphonooxybutanoate. {ECO:0000256|HAMAP-
CC       Rule:MF_01825}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-
CC         phosphooxybutanoate + H(+) + NADH; Xref=Rhea:RHEA:18829,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58538, ChEBI:CHEBI:58766; EC=1.1.1.290;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01825};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
CC       {ECO:0000256|HAMAP-Rule:MF_01825}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01825}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01825}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. PdxB subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01825}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01825}.
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:PHM67826.1}.
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DR   EMBL; NJAJ01000001; PHM67826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D0KWL3; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000222366; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd12158; ErythrP_dh; 1.
DR   Gene3D; 3.30.1370.170; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   HAMAP; MF_01825; PdxB; 1.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR020921; Erythronate-4-P_DHase.
DR   InterPro; IPR024531; Erythronate-4-P_DHase_dimer.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR038251; PdxB_dimer_sf.
DR   PANTHER; PTHR42938:SF40; ERYTHRONATE-4-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF11890; DUF3410; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01825};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01825};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01825};
KW   Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096, ECO:0000256|HAMAP-
KW   Rule:MF_01825}.
FT   DOMAIN          5..280
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          111..256
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   DOMAIN          289..369
FT                   /note="Erythronate-4-phosphate dehydrogenase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF11890"
FT   ACT_SITE        208
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT   ACT_SITE        254
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT   BINDING         146
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT   BINDING         175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT   BINDING         206..208
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT   BINDING         232
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT   BINDING         257
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
SQ   SEQUENCE   375 AA;  41053 MW;  B1126F5C39AE7C76 CRC64;
     MKILVDENMP YAEQLFKQLG EVQAIPGRPV PEGVLEHADA FMVRSVTKVS ESLLKGSAVK
     FVGTATAGMD HVDQPWLEQA GIGFSAAPGC NAIAVVEYVF SALMILAEQD QFQLKDKTVG
     IVGVGNVGGR LAARLAALGV KTLLCDPPRA DRGDEGEFWP LEKLVKEADI LTFHTPLNTS
     GPYQTYHLAD AELLSALPDN RILINASRGE VVDNQALLSA LQNGKKLRVV LDVWEPEPNL
     SLPLLERVDI GTPHIAGYTL EGKARGTTQV FEAYCEFLGK PQKTALSDLL PESDFSHITV
     RGEVTQSILK RLMHLVYDVR RDDAPLRQVA GQNGAFDQLR KNYPERREWS SLTVHCDSES
     SAQLLSQIGF DAKVI
//
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