位置:首页 > 蛋白库 > DXR_PLAF7
DXR_PLAF7
ID   DXR_PLAF7               Reviewed;         488 AA.
AC   Q8IKG4; A0A144A2T4;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic;
DE            Short=1-deoxyxylulose-5-phosphate reductoisomerase;
DE            Short=DOXP reductoisomerase;
DE            Short=DXP reductoisomerase;
DE            EC=1.1.1.267 {ECO:0000269|PubMed:25781377, ECO:0000269|PubMed:27487410};
DE   Flags: Precursor;
GN   Name=DXR; ORFNames=PF14_0641, PF3D7_1467300;
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D7;
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA   Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
RN   [2] {ECO:0007744|PDB:4Y67, ECO:0007744|PDB:4Y6P, ECO:0007744|PDB:4Y6R, ECO:0007744|PDB:4Y6S}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 75-488 IN COMPLEX WITH MANGANESE
RP   AND INHIBITORS, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP   PATHWAY.
RX   PubMed=25781377; DOI=10.1021/jm5014264;
RA   Chofor R., Sooriyaarachchi S., Risseeuw M.D., Bergfors T., Pouyez J.,
RA   Johny C., Haymond A., Everaert A., Dowd C.S., Maes L., Coenye T., Alex A.,
RA   Couch R.D., Jones T.A., Wouters J., Mowbray S.L., Van Calenbergh S.;
RT   "Synthesis and bioactivity of beta-substituted fosmidomycin analogues
RT   targeting 1-deoxy-D-xylulose-5-phosphate reductoisomerase.";
RL   J. Med. Chem. 58:2988-3001(2015).
RN   [3] {ECO:0007744|PDB:5JAZ, ECO:0007744|PDB:5JBI, ECO:0007744|PDB:5JC1, ECO:0007744|PDB:5JMP, ECO:0007744|PDB:5JMW, ECO:0007744|PDB:5JNL, ECO:0007744|PDB:5JO0}
RP   X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 75-488 IN COMPLEX WITH MANGANESE,
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, PATHWAY, AND
RP   SUBUNIT.
RX   PubMed=27487410; DOI=10.1002/cmdc.201600249;
RA   Sooriyaarachchi S., Chofor R., Risseeuw M.D., Bergfors T., Pouyez J.,
RA   Dowd C.S., Maes L., Wouters J., Jones T.A., Van Calenbergh S.,
RA   Mowbray S.L.;
RT   "Targeting an Aromatic Hotspot in Plasmodium falciparum 1-Deoxy-d-xylulose-
RT   5-phosphate Reductoisomerase with beta-Arylpropyl Analogues of
RT   Fosmidomycin.";
RL   ChemMedChem 11:2024-2036(2016).
CC   -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of
CC       1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-
CC       phosphate (MEP). {ECO:0000269|PubMed:25781377,
CC       ECO:0000269|PubMed:27487410}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-
CC         xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267;
CC         Evidence={ECO:0000269|PubMed:25781377, ECO:0000269|PubMed:27487410};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13719;
CC         Evidence={ECO:0000305|PubMed:25781377, ECO:0000305|PubMed:27487410};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O96693};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:25781377, ECO:0000269|PubMed:27487410};
CC       Note=Binds 1 divalent cation per subunit. Mg(2+) or Mn(2+).
CC       {ECO:0000269|PubMed:25781377, ECO:0000269|PubMed:27487410};
CC   -!- ACTIVITY REGULATION: Inhibited by fosmidomycin and its derivatives.
CC       {ECO:0000269|PubMed:25781377, ECO:0000269|PubMed:27487410}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 1/6. {ECO:0000305|PubMed:25781377,
CC       ECO:0000305|PubMed:27487410}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:25781377,
CC       ECO:0000305|PubMed:27487410}.
CC   -!- SUBCELLULAR LOCATION: Plastid, apicoplast
CC       {ECO:0000250|UniProtKB:O96693}.
CC   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LN999946; CZU00370.1; -; Genomic_DNA.
DR   RefSeq; XP_001348815.1; XM_001348779.1.
DR   PDB; 4Y67; X-ray; 1.60 A; A/B=75-488.
DR   PDB; 4Y6P; X-ray; 1.90 A; A/B=75-488.
DR   PDB; 4Y6R; X-ray; 1.90 A; A/B=75-488.
DR   PDB; 4Y6S; X-ray; 2.10 A; A/B=75-488.
DR   PDB; 5JAZ; X-ray; 1.40 A; A/B=75-488.
DR   PDB; 5JBI; X-ray; 1.70 A; A/B=75-488.
DR   PDB; 5JC1; X-ray; 1.65 A; A/B=75-488.
DR   PDB; 5JMP; X-ray; 1.70 A; A/B=75-488.
DR   PDB; 5JMW; X-ray; 1.55 A; A/B=75-488.
DR   PDB; 5JNL; X-ray; 1.60 A; A/B=75-488.
DR   PDB; 5JO0; X-ray; 1.80 A; A/B=75-488.
DR   PDBsum; 4Y67; -.
DR   PDBsum; 4Y6P; -.
DR   PDBsum; 4Y6R; -.
DR   PDBsum; 4Y6S; -.
DR   PDBsum; 5JAZ; -.
DR   PDBsum; 5JBI; -.
DR   PDBsum; 5JC1; -.
DR   PDBsum; 5JMP; -.
DR   PDBsum; 5JMW; -.
DR   PDBsum; 5JNL; -.
DR   PDBsum; 5JO0; -.
DR   AlphaFoldDB; Q8IKG4; -.
DR   SMR; Q8IKG4; -.
DR   STRING; 5833.PF14_0641; -.
DR   BindingDB; Q8IKG4; -.
DR   ChEMBL; CHEMBL4295619; -.
DR   PRIDE; Q8IKG4; -.
DR   EnsemblProtists; CZU00370; CZU00370; PF3D7_1467300.
DR   GeneID; 812223; -.
DR   KEGG; pfa:PF3D7_1467300; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1467300; -.
DR   HOGENOM; CLU_035714_4_0_1; -.
DR   InParanoid; Q8IKG4; -.
DR   OMA; PIDSEHF; -.
DR   PhylomeDB; Q8IKG4; -.
DR   BRENDA; 1.1.1.267; 4889.
DR   UniPathway; UPA00056; UER00092.
DR   Proteomes; UP000001450; Chromosome 14.
DR   GO; GO:0020011; C:apicoplast; IDA:GeneDB.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IDA:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR   GO; GO:0070402; F:NADPH binding; IBA:GO_Central.
DR   GO; GO:0051484; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process; IBA:GO_Central.
DR   HAMAP; MF_00183; DXP_reductoisom; 1.
DR   InterPro; IPR003821; DXP_reductoisomerase.
DR   InterPro; IPR013644; DXP_reductoisomerase_C.
DR   InterPro; IPR013512; DXP_reductoisomerase_N.
DR   InterPro; IPR026877; DXPR_C.
DR   InterPro; IPR036169; DXPR_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR30525; PTHR30525; 1.
DR   Pfam; PF08436; DXP_redisom_C; 1.
DR   Pfam; PF02670; DXP_reductoisom; 1.
DR   Pfam; PF13288; DXPR_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF69055; SSF69055; 1.
DR   TIGRFAMs; TIGR00243; Dxr; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Apicoplast; Isoprene biosynthesis; Magnesium; Manganese;
KW   Metal-binding; NADP; Oxidoreductase; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..72
FT                   /note="Apicoplast"
FT                   /evidence="ECO:0000305"
FT   CHAIN           73..488
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase,
FT                   apicoplastic"
FT                   /id="PRO_0000415609"
FT   REGION          306..312
FT                   /note="Binding to substrate phosphate group"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         86..89
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O96693"
FT   BINDING         115..117
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O96693"
FT   BINDING         205
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         206
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O96693"
FT   BINDING         231
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000269|PubMed:25781377,
FT                   ECO:0000269|PubMed:27487410, ECO:0007744|PDB:4Y67,
FT                   ECO:0007744|PDB:4Y6P, ECO:0007744|PDB:4Y6R,
FT                   ECO:0007744|PDB:4Y6S, ECO:0007744|PDB:5JAZ,
FT                   ECO:0007744|PDB:5JBI, ECO:0007744|PDB:5JC1,
FT                   ECO:0007744|PDB:5JMP, ECO:0007744|PDB:5JMW,
FT                   ECO:0007744|PDB:5JNL, ECO:0007744|PDB:5JO0"
FT   BINDING         233
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         233
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000269|PubMed:25781377,
FT                   ECO:0000269|PubMed:27487410, ECO:0007744|PDB:4Y67,
FT                   ECO:0007744|PDB:4Y6P, ECO:0007744|PDB:4Y6R,
FT                   ECO:0007744|PDB:4Y6S, ECO:0007744|PDB:5JAZ,
FT                   ECO:0007744|PDB:5JBI, ECO:0007744|PDB:5JC1,
FT                   ECO:0007744|PDB:5JMP, ECO:0007744|PDB:5JMW,
FT                   ECO:0007744|PDB:5JNL, ECO:0007744|PDB:5JO0"
FT   BINDING         270
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         293
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         299
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O96693"
FT   BINDING         315
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         315
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000269|PubMed:25781377,
FT                   ECO:0000269|PubMed:27487410, ECO:0007744|PDB:4Y67,
FT                   ECO:0007744|PDB:4Y6P, ECO:0007744|PDB:4Y6R,
FT                   ECO:0007744|PDB:4Y6S, ECO:0007744|PDB:5JAZ,
FT                   ECO:0007744|PDB:5JBI, ECO:0007744|PDB:5JC1,
FT                   ECO:0007744|PDB:5JMP, ECO:0007744|PDB:5JMW,
FT                   ECO:0007744|PDB:5JNL, ECO:0007744|PDB:5JO0"
FT   STRAND          78..84
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           88..103
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   STRAND          107..116
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           118..128
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   STRAND          131..136
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           141..148
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:5JNL"
FT   STRAND          157..160
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           161..170
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   STRAND          176..179
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           184..195
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   STRAND          199..202
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           205..221
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   STRAND          226..229
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           232..239
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           243..246
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   STRAND          251..253
FT                   /evidence="ECO:0007829|PDB:5JMW"
FT   HELIX           256..259
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   STRAND          262..269
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   TURN            273..276
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           279..284
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           287..291
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           300..308
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           310..323
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           327..329
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   STRAND          330..334
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   STRAND          340..346
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   STRAND          351..355
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           361..369
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           383..386
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   STRAND          388..390
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   TURN            396..398
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           400..411
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           415..431
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           437..450
FT                   /evidence="ECO:0007829|PDB:5JAZ"
FT   HELIX           460..485
FT                   /evidence="ECO:0007829|PDB:5JAZ"
SQ   SEQUENCE   488 AA;  55757 MW;  4E280C81CDFAD3EF CRC64;
     MKKYIYIYFF FITITINDLV INNTSKCVSI ERRKNNAYIN YGIGYNGPDN KITKSRRCKR
     IKLCKKDLID IGAIKKPINV AIFGSTGSIG TNALNIIREC NKIENVFNVK ALYVNKSVNE
     LYEQAREFLP EYLCIHDKSV YEELKELVKN IKDYKPIILC GDEGMKEICS SNSIDKIVIG
     IDSFQGLYST MYAIMNNKIV ALANKESIVS AGFFLKKLLN IHKNAKIIPV DSEHSAIFQC
     LDNNKVLKTK CLQDNFSKIN NINKIFLCSS GGPFQNLTMD ELKNVTSENA LKHPKWKMGK
     KITIDSATMM NKGLEVIETH FLFDVDYNDI EVIVHKECII HSCVEFIDKS VISQMYYPDM
     QIPILYSLTW PDRIKTNLKP LDLAQVSTLT FHKPSLEHFP CIKLAYQAGI KGNFYPTVLN
     ASNEIANNLF LNNKIKYFDI SSIISQVLES FNSQKVSENS EDLMKQILQI HSWAKDKATD
     IYNKHNSS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024