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Database: UniProt
Entry: Q9I3W9
LinkDB: Q9I3W9
Original site: Q9I3W9 
ID   PDXB_PSEAE              Reviewed;         380 AA.
AC   Q9I3W9;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   16-JAN-2019, entry version 115.
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}; OrderedLocusNames=PA1375;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
OS   JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   CRYSTALLIZATION, AND SUBUNIT.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=16511285; DOI=10.1107/S1744309106000649;
RA   Ha J.Y., Lee J.H., Kim K.H., Kim D.J., Lee H.H., Kim H.-K.,
RA   Yoon H.-J., Suh S.W.;
RT   "Overexpression, crystallization and preliminary X-ray
RT   crystallographic analysis of erythronate-4-phosphate dehydrogenase
RT   from Pseudomonas aeruginosa.";
RL   Acta Crystallogr. F 62:139-141(2006).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NAD AND
RP   PHOSPHATE OR SUBSTRATE ANALOG, SUBUNIT, CATALYTIC MECHANISM, DOMAIN,
RP   ACTIVE SITE, AND DISULFIDE BOND.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=17217963; DOI=10.1016/j.jmb.2006.12.038;
RA   Ha J.Y., Lee J.H., Kim K.H., Kim D.J., Lee H.H., Kim H.-K.,
RA   Yoon H.-J., Suh S.W.;
RT   "Crystal structure of D-erythronate-4-phosphate dehydrogenase
RT   complexed with NAD.";
RL   J. Mol. Biol. 366:1294-1304(2007).
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       ECO:0000269|PubMed:16511285, ECO:0000269|PubMed:17217963}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01825}.
CC   -!- DOMAIN: Each subunit can be divided into three discernible
CC       structural domains: the lid domain, the nucleotide-binding domain,
CC       and the C-terminal dimerization domain. PdxB has a unique dimeric
CC       structure among NAD-dependent D-isomer specific 2-hydroxyacid
CC       dehydrogenases due to the presence of its dimerization domain at
CC       its C-terminus. {ECO:0000305|PubMed:17217963}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. PdxB subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01825}.
DR   EMBL; AE004091; AAG04764.1; -; Genomic_DNA.
DR   PIR; C83473; C83473.
DR   RefSeq; NP_250066.1; NC_002516.2.
DR   RefSeq; WP_003112396.1; NC_002516.2.
DR   PDB; 2O4C; X-ray; 2.30 A; A/B=1-380.
DR   PDBsum; 2O4C; -.
DR   ProteinModelPortal; Q9I3W9; -.
DR   SMR; Q9I3W9; -.
DR   STRING; 208964.PA1375; -.
DR   PaxDb; Q9I3W9; -.
DR   PRIDE; Q9I3W9; -.
DR   EnsemblBacteria; AAG04764; AAG04764; PA1375.
DR   GeneID; 881132; -.
DR   KEGG; pae:PA1375; -.
DR   PATRIC; fig|208964.12.peg.1427; -.
DR   PseudoCAP; PA1375; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   InParanoid; Q9I3W9; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   PhylomeDB; Q9I3W9; -.
DR   BioCyc; PAER208964:G1FZ6-1401-MONOMER; -.
DR   BRENDA; 1.1.1.290; 5087.
DR   UniPathway; UPA00244; UER00310.
DR   EvolutionaryTrace; Q9I3W9; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0036001; P:'de novo' pyridoxal 5'-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; Disulfide bond; NAD;
KW   Oxidoreductase; Pyridoxine biosynthesis; Reference proteome.
FT   CHAIN         1    380       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000075982.
FT   NP_BIND     126    127       NAD. {ECO:0000255|HAMAP-Rule:MF_01825,
FT                                ECO:0000269|PubMed:17217963}.
FT   NP_BIND     206    208       NAD. {ECO:0000255|HAMAP-Rule:MF_01825,
FT                                ECO:0000269|PubMed:17217963}.
FT   ACT_SITE    208    208       {ECO:0000255|HAMAP-Rule:MF_01825,
FT                                ECO:0000305|PubMed:17217963}.
FT   ACT_SITE    237    237       {ECO:0000255|HAMAP-Rule:MF_01825,
FT                                ECO:0000305|PubMed:17217963}.
FT   ACT_SITE    254    254       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825,
FT                                ECO:0000305|PubMed:17217963}.
FT   BINDING      45     45       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825,
FT                                ECO:0000305|PubMed:17217963}.
FT   BINDING      66     66       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825,
FT                                ECO:0000305|PubMed:17217963}.
FT   BINDING     146    146       NAD. {ECO:0000255|HAMAP-Rule:MF_01825,
FT                                ECO:0000269|PubMed:17217963}.
FT   BINDING     175    175       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825,
FT                                ECO:0000269|PubMed:17217963}.
FT   BINDING     232    232       NAD. {ECO:0000255|HAMAP-Rule:MF_01825,
FT                                ECO:0000269|PubMed:17217963}.
FT   BINDING     257    257       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825,
FT                                ECO:0000269|PubMed:17217963}.
FT   BINDING     258    258       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825,
FT                                ECO:0000305|PubMed:17217963}.
FT   DISULFID     65     90       {ECO:0000269|PubMed:17217963}.
FT   STRAND        2      6       {ECO:0000244|PDB:2O4C}.
FT   HELIX        12     16       {ECO:0000244|PDB:2O4C}.
FT   HELIX        17     19       {ECO:0000244|PDB:2O4C}.
FT   STRAND       20     25       {ECO:0000244|PDB:2O4C}.
FT   HELIX        27     29       {ECO:0000244|PDB:2O4C}.
FT   TURN         32     37       {ECO:0000244|PDB:2O4C}.
FT   STRAND       39     43       {ECO:0000244|PDB:2O4C}.
FT   HELIX        51     54       {ECO:0000244|PDB:2O4C}.
FT   STRAND       61     64       {ECO:0000244|PDB:2O4C}.
FT   HELIX        74     80       {ECO:0000244|PDB:2O4C}.
FT   STRAND       83     85       {ECO:0000244|PDB:2O4C}.
FT   TURN         88     91       {ECO:0000244|PDB:2O4C}.
FT   HELIX        92    110       {ECO:0000244|PDB:2O4C}.
FT   HELIX       114    116       {ECO:0000244|PDB:2O4C}.
FT   STRAND      118    122       {ECO:0000244|PDB:2O4C}.
FT   HELIX       126    137       {ECO:0000244|PDB:2O4C}.
FT   STRAND      141    145       {ECO:0000244|PDB:2O4C}.
FT   HELIX       147    152       {ECO:0000244|PDB:2O4C}.
FT   HELIX       161    167       {ECO:0000244|PDB:2O4C}.
FT   STRAND      169    173       {ECO:0000244|PDB:2O4C}.
FT   STRAND      179    183       {ECO:0000244|PDB:2O4C}.
FT   HELIX       191    195       {ECO:0000244|PDB:2O4C}.
FT   STRAND      201    205       {ECO:0000244|PDB:2O4C}.
FT   HELIX       209    211       {ECO:0000244|PDB:2O4C}.
FT   HELIX       214    222       {ECO:0000244|PDB:2O4C}.
FT   STRAND      227    232       {ECO:0000244|PDB:2O4C}.
FT   TURN        235    238       {ECO:0000244|PDB:2O4C}.
FT   HELIX       242    245       {ECO:0000244|PDB:2O4C}.
FT   STRAND      249    251       {ECO:0000244|PDB:2O4C}.
FT   HELIX       260    278       {ECO:0000244|PDB:2O4C}.
FT   HELIX       286    288       {ECO:0000244|PDB:2O4C}.
FT   STRAND      294    300       {ECO:0000244|PDB:2O4C}.
FT   HELIX       306    317       {ECO:0000244|PDB:2O4C}.
FT   HELIX       321    329       {ECO:0000244|PDB:2O4C}.
FT   HELIX       335    347       {ECO:0000244|PDB:2O4C}.
FT   HELIX       355    357       {ECO:0000244|PDB:2O4C}.
FT   STRAND      359    361       {ECO:0000244|PDB:2O4C}.
FT   HELIX       366    375       {ECO:0000244|PDB:2O4C}.
FT   STRAND      378    380       {ECO:0000244|PDB:2O4C}.
SQ   SEQUENCE   380 AA;  41002 MW;  36F6B0F68909D05D CRC64;
     MRILADENIP VVDAFFADQG SIRRLPGRAI DRAALAEVDV LLVRSVTEVS RAALAGSPVR
     FVGTCTIGTD HLDLDYFAEA GIAWSSAPGC NARGVVDYVL GCLLAMAEVR GADLAERTYG
     VVGAGQVGGR LVEVLRGLGW KVLVCDPPRQ AREPDGEFVS LERLLAEADV ISLHTPLNRD
     GEHPTRHLLD EPRLAALRPG TWLVNASRGA VVDNQALRRL LEGGADLEVA LDVWEGEPQA
     DPELAARCLI ATPHIAGYSL EGKLRGTAQI YQAYCAWRGI AERVSLQDVL PETWLAGLQL
     NPGCDPAWAL ATLCRAVYDP RSDDAAFRRS LTGDSATRRA AFDALRKHYP PRREITGLRV
     ATGGQAELQR VVRALGAQLV
//
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