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Database: UniProt
Entry: Q56733
LinkDB: Q56733
Original site: Q56733 
ID   PDXB_SHEVD              Reviewed;         387 AA.
AC   Q56733; D4ZMF2;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   16-JAN-2019, entry version 109.
DE   RecName: Full=Erythronate-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01825};
DE            EC=1.1.1.290 {ECO:0000255|HAMAP-Rule:MF_01825};
GN   Name=pdxB {ECO:0000255|HAMAP-Rule:MF_01825};
GN   OrderedLocusNames=SVI_2880;
OS   Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 /
OS   DSS12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=637905;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12;
RX   PubMed=20458400; DOI=10.1039/c000396d;
RA   Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E.,
RA   Toyonaga H., Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M.,
RA   Kato C., Oshima T., Nakasone K., Mori H.;
RT   "Complete genome sequence and comparative analysis of Shewanella
RT   violacea, a psychrophilic and piezophilic bacterium from deep sea
RT   floor sediments.";
RL   Mol. Biosyst. 6:1216-1226(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 114-387.
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:0000255|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:0000255|HAMAP-Rule:MF_01825};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 2/5. {ECO:0000255|HAMAP-Rule:MF_01825}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01825}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01825}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. PdxB subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01825}.
DR   EMBL; AP011177; BAJ02851.1; -; Genomic_DNA.
DR   EMBL; D49540; BAA08489.1; -; Genomic_DNA.
DR   RefSeq; WP_013052150.1; NC_014012.1.
DR   ProteinModelPortal; Q56733; -.
DR   SMR; Q56733; -.
DR   STRING; 637905.SVI_2880; -.
DR   PRIDE; Q56733; -.
DR   EnsemblBacteria; BAJ02851; BAJ02851; SVI_2880.
DR   KEGG; svo:SVI_2880; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; SVIO637905:G1GKA-2734-MONOMER; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000002350; Chromosome.
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   HAMAP; MF_01825; PdxB; 1.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
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; PF00389; 2-Hacid_dh; 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   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis; Reference proteome.
FT   CHAIN         1    387       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000075989.
FT   ACT_SITE    208    208       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    237    237       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    254    254       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      45     45       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      67     67       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING     147    147       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     232    232       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     257    257       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     258    258       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   CONFLICT    302    302       S -> P (in Ref. 2; BAA08489).
FT                                {ECO:0000305}.
FT   CONFLICT    322    322       D -> G (in Ref. 2; BAA08489).
FT                                {ECO:0000305}.
FT   CONFLICT    328    328       K -> E (in Ref. 2; BAA08489).
FT                                {ECO:0000305}.
SQ   SEQUENCE   387 AA;  43147 MW;  3AF4060CEDECC3D4 CRC64;
     MKILADENMP YVQELFGDLG TIETVNGREL TPEQVKDADV LLVRSVTQVN GSLLSLNNKL
     KFVGSATIGT DHIDTDYLAS RDIPFSNAPG CNATAVGEFA FIAMLELANR FGGKLKDKTV
     GIVGAGNTGS AVAKCLQAYG VTVLLHDPVI QDSDPRDFIS LDELIARCDV ISLHVPIIKT
     GEHKTWYLFD ETRLNSLKPG TWLLNCCRGE VIDNRALIKV KQQRPDIKLV LDVWEGEPNP
     MHELIPLVEL ATPHIAGYSL EGKARGTYML YQKLMQVLGR DADKSMTTLL PSLWSVQLDI
     ESIPNEKSLL KLARFIYDLR DDDELFRKTI LDDSSKNDQV NCVNNNGFDL MRKNHQHRRE
     FRALRLVNTG HSDVNWLTNL GFSGVGQ
//
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