PDXB_SHESP
ID PDXB_SHESP Reviewed; 274 AA.
AC Q56731;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Erythronate-4-phosphate dehydrogenase;
DE EC=1.1.1.290;
DE Flags: Fragment;
GN Name=pdxB;
OS Shewanella sp. (strain DB6705).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=126830;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9163523; DOI=10.1093/oxfordjournals.jbchem.a021645;
RA Kato C., Smorawinska M., Li L., Horikoshi K.;
RT "Comparison of the gene expression of aspartate beta-D-semialdehyde
RT dehydrogenase at elevated hydrostatic pressure in deep-sea bacteria.";
RL J. Biochem. 121:717-723(1997).
CC -!- FUNCTION: Catalyzes the oxidation of erythronate-4-phosphate to 3-
CC hydroxy-2-oxo-4-phosphonooxybutanoate. {ECO:0000250}.
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 -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. PdxB subfamily. {ECO:0000305}.
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DR EMBL; D49539; BAA08487.1; -; Genomic_DNA.
DR AlphaFoldDB; Q56731; -.
DR SMR; Q56731; -.
DR UniPathway; UPA00244; UER00310.
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-KW.
DR CDD; cd12158; ErythrP_dh; 1.
DR Gene3D; 3.30.1370.170; -; 1.
DR InterPro; IPR029753; D-isomer_DH_CS.
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 Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF11890; DUF3410; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis.
FT CHAIN <1..274
FT /note="Erythronate-4-phosphate dehydrogenase"
FT /id="PRO_0000075988"
FT ACT_SITE 95
FT /evidence="ECO:0000250"
FT ACT_SITE 124
FT /evidence="ECO:0000250"
FT ACT_SITE 141
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 274 AA; 30717 MW; 0370BEC6CD6A0D4A CRC64;
KLKDKTVGIV GAGNTGSAVA KCLQAYGVTV LLHDPVIQDS DPRDFISLDE LIACCDVISL
HVPITKTGEH KTWYLFDEAR LNSLKQGTWL LNCCRGEVID NQALIKVKLE RPDIKLVLDV
WEGEPNPMHE LIPLVELATP HIAGYSLEGK ARGTFMLYQK LMQVLGKDAD KSMTALLPSL
WSVQLDVESI PDQKSLLQLA RFIYDLRDDD ELFRKTILDD SSKNPQVNSL NNNGFDLMRK
NHLHRREFSA LRLVNTGHSD VNWLTNLGFS GIGQ
