GenomeNet

Database: UniProt
Entry: Q1QE21
LinkDB: Q1QE21
Original site: Q1QE21 
ID   PDXB_PSYCK              Reviewed;         386 AA.
AC   Q1QE21;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JAN-2019, entry version 82.
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=Pcryo_0298;
OS   Psychrobacter cryohalolentis (strain K5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=335284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000323; ABE74082.1; -; Genomic_DNA.
DR   RefSeq; WP_011512670.1; NC_007969.1.
DR   ProteinModelPortal; Q1QE21; -.
DR   STRING; 335284.Pcryo_0298; -.
DR   EnsemblBacteria; ABE74082; ABE74082; Pcryo_0298.
DR   KEGG; pcr:Pcryo_0298; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000002425; 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; 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:SF3; PTHR42938:SF3; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 2.
DR   Pfam; PF11890; DUF3410; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis.
FT   CHAIN         1    386       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000297458.
FT   ACT_SITE    239    239       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    267    267       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    284    284       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      59     59       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      81     81       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING     162    162       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     262    262       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     287    287       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     288    288       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   386 AA;  42643 MW;  1E2DEA4199A0EC4C CRC64;
     MKNLTIVADS NIASLDEFFN PVALGQNTEQ QVQVIRVAGR DINAQLMADV QPDVLLIRSV
     TSINESLLSD NNSVKFVGSA TIGTDHVDQE YLAERNITFA NAAGCSKHSV AQYVVTAILT
     LRPQYWQQST KPLTVGIIGL GNIGSTLAQY ANDLGWKILG YDPLLATSDI NNASLEQVLS
     QSDIVSLHVP LTDKKDTDAQ DAVSNSISNN VSDYPTRHLI NAETLTLMSP HTMLINSARG
     PVIDAAALEA DIDATERQVV LDVFEHEPQI SESLLSKLAI ATPHIAGYTL EGKLRGTQII
     YDALCEKLAV LPVLSMHQLL PLNTYLWFEL KEHPDRLQKF YDIKKDDAAL RNKITNGKVK
     GSDFDQLRRD YHLRREWQAQ TISVTI
//
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