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Database: UniProt
Entry: Q56731
LinkDB: Q56731
Original site: Q56731 
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   05-DEC-2018, entry version 89.
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
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       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}.
DR   EMBL; D49539; BAA08487.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q56731; -.
DR   SMR; Q56731; -.
DR   PRIDE; 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   PANTHER; PTHR42938:SF3; PTHR42938:SF3; 1.
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       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000075988.
FT   ACT_SITE     95     95       {ECO:0000250}.
FT   ACT_SITE    124    124       {ECO:0000250}.
FT   ACT_SITE    141    141       Proton donor. {ECO:0000250}.
FT   BINDING      34     34       NAD. {ECO:0000250}.
FT   BINDING     119    119       NAD. {ECO:0000250}.
FT   BINDING     144    144       NAD; via amide nitrogen. {ECO:0000250}.
FT   BINDING     145    145       Substrate. {ECO:0000250}.
FT   NON_TER       1      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
//
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