GenomeNet

Database: UniProt
Entry: Q3K9D1
LinkDB: Q3K9D1
Original site: Q3K9D1 
ID   PDXB_PSEPF              Reviewed;         380 AA.
AC   Q3K9D1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JAN-2019, entry version 102.
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=Pfl01_3886;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA75623.1; -; Genomic_DNA.
DR   RefSeq; WP_011335202.1; NC_007492.2.
DR   ProteinModelPortal; Q3K9D1; -.
DR   SMR; Q3K9D1; -.
DR   STRING; 205922.Pfl01_3886; -.
DR   PRIDE; Q3K9D1; -.
DR   EnsemblBacteria; ABA75623; ABA75623; Pfl01_3886.
DR   KEGG; pfo:Pfl01_3886; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   BioCyc; PFLU205922:G1G4S-3958-MONOMER; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000002704; 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.
FT   CHAIN         1    380       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000297453.
FT   ACT_SITE    207    207       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    236    236       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    253    253       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      45     45       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      66     66       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING     146    146       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     174    174       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     231    231       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     256    256       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     257    257       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   380 AA;  41369 MW;  746ACD1855DD8915 CRC64;
     MLIVADENIP LLDAFFAGFG EIRRVPGRSI DRATVEQADV LLVRSVTNVN RALLEGSKVR
     FVGTCTIGTD HLDLDYFNEA GITWSSAPGC NARGVVDYVL GSLMTLAEIE GVDLRERTYG
     VIGAGEVGGR LIKVLKGLGW NVKVCDPPRQ AAEGGDYVSL EQIIAQCDVI SLHTPLTRSG
     DGATWHLFDE QRLQQLKPGA WLINAARGPV VDNTALREVL LEREDLQAVL DVWEAEPQVD
     VSLAELCVLA TPHIAGYSLD GKQRGTAQIY QAYCDFIGEP ASIQLGDLLP APWLSEVSLH
     ADSDPAWALA MLCRGVYDPR RDDADFRRTL LGSVGEQRAA FDVLRKQYPS RREIEGLKVR
     IEGDSPALRQ IVAALGAVAV
//
DBGET integrated database retrieval system