GenomeNet

Database: UniProt
Entry: Q88L20
LinkDB: Q88L20
Original site: Q88L20 
ID   PDXB_PSEPK              Reviewed;         380 AA.
AC   Q88L20;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   05-DEC-2018, entry version 106.
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=PP_2117;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 /
OS   KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M.,
RA   Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K.,
RA   Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D.,
RA   Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S.,
RA   Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B.,
RA   Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the
RT   metabolically versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN67730.1; -; Genomic_DNA.
DR   RefSeq; NP_744266.1; NC_002947.4.
DR   RefSeq; WP_010953113.1; NC_002947.4.
DR   ProteinModelPortal; Q88L20; -.
DR   SMR; Q88L20; -.
DR   STRING; 160488.PP_2117; -.
DR   PRIDE; Q88L20; -.
DR   EnsemblBacteria; AAN67730; AAN67730; PP_2117.
DR   GeneID; 1044970; -.
DR   KEGG; ppu:PP_2117; -.
DR   PATRIC; fig|160488.4.peg.2233; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   BioCyc; PPUT160488:G1G01-2257-MONOMER; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000000556; 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    380       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000075983.
FT   NP_BIND     205    207       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
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;  41614 MW;  5FB321E7709B4319 CRC64;
     MLIVADENIP LLDAFFQGFG EIRRYPGRSL DAASVKDADI LLVRSVTKVD RQLLEGSRVR
     FVGTCTIGTD HLDLDYFAEA GIHWSSAPGC NARGVVDYVL GSLLTLAELD GVALPERVYG
     VVGAGEVGGR LVRVLHGLGW KVLVCDPLRQ AAEGGDYVSL ETILQQCDVI SLHTPLQRGG
     QHPTWHLLGQ AQLAQLRPGA WLVNASRGPV VDNVALRELL LDREDVHAVL DVWEGEPQVD
     LQLADLCTLA TPHIAGYSLD GRQRGTARIY QALCRFLGVN EQVRLAELLP KPPLAQIELD
     ASTDLSWALA TLCRAVYDPR RDDADFRRSL SDDPQQQRAA FDQLRKQYPP RREIEGLAVR
     LHGEAPQLAQ LVSALGGVLV
//
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