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DXS_DEIRA
ID   DXS_DEIRA               Reviewed;         629 AA.
AC   Q9RUB5;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase;
DE            EC=2.2.1.7;
DE   AltName: Full=1-deoxyxylulose-5-phosphate synthase;
DE            Short=DXP synthase;
DE            Short=DXPS;
GN   Name=dxs; OrderedLocusNames=DR_1475;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP   THIAMINE PYROPHOSPHATE, COFACTOR, AND SUBUNIT.
RX   PubMed=17135236; DOI=10.1074/jbc.m610235200;
RA   Xiang S., Usunow G., Lange G., Busch M., Tong L.;
RT   "Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial
RT   enzyme for isoprenoids biosynthesis.";
RL   J. Biol. Chem. 282:2676-2682(2007).
CC   -!- FUNCTION: Catalyzes the acyloin condensation reaction between C atoms 2
CC       and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-
CC       xylulose-5-phosphate (DXP). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-
CC         xylulose 5-phosphate + CO2; Xref=Rhea:RHEA:12605, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:59776; EC=2.2.1.7;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:17135236};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:17135236};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000269|PubMed:17135236};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000269|PubMed:17135236};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-
CC       phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC       glyceraldehyde 3-phosphate and pyruvate: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17135236}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000513; AAF11042.1; -; Genomic_DNA.
DR   PIR; G75390; G75390.
DR   RefSeq; NP_295198.1; NC_001263.1.
DR   RefSeq; WP_010888114.1; NZ_CP015081.1.
DR   PDB; 2O1X; X-ray; 2.90 A; A/B/C/D=1-629.
DR   PDB; 6OUV; X-ray; 1.94 A; A/B=1-629.
DR   PDB; 6OUW; X-ray; 2.40 A; A=1-629.
DR   PDB; 6XXG; X-ray; 2.10 A; AAA/BBB=2-199, AAA/BBB=244-629.
DR   PDBsum; 2O1X; -.
DR   PDBsum; 6OUV; -.
DR   PDBsum; 6OUW; -.
DR   PDBsum; 6XXG; -.
DR   AlphaFoldDB; Q9RUB5; -.
DR   SMR; Q9RUB5; -.
DR   STRING; 243230.DR_1475; -.
DR   BindingDB; Q9RUB5; -.
DR   ChEMBL; CHEMBL3559650; -.
DR   PRIDE; Q9RUB5; -.
DR   EnsemblBacteria; AAF11042; AAF11042; DR_1475.
DR   KEGG; dra:DR_1475; -.
DR   PATRIC; fig|243230.17.peg.1675; -.
DR   eggNOG; COG1154; Bacteria.
DR   HOGENOM; CLU_009227_1_4_0; -.
DR   InParanoid; Q9RUB5; -.
DR   OMA; QVGYHAQ; -.
DR   OrthoDB; 566385at2; -.
DR   BRENDA; 2.2.1.7; 1856.
DR   UniPathway; UPA00064; UER00091.
DR   EvolutionaryTrace; Q9RUB5; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016744; F:transketolase or transaldolase activity; IBA:GO_Central.
DR   GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IBA:GO_Central.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02007; TPP_DXS; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   HAMAP; MF_00315; DXP_synth; 1.
DR   InterPro; IPR005477; Dxylulose-5-P_synthase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR43322; PTHR43322; 1.
DR   Pfam; PF13292; DXP_synthase_N; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00204; dxs; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Reference proteome; Thiamine biosynthesis; Thiamine pyrophosphate;
KW   Transferase.
FT   CHAIN           1..629
FT                   /note="1-deoxy-D-xylulose-5-phosphate synthase"
FT                   /id="PRO_0000189110"
FT   BINDING         82
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000269|PubMed:17135236"
FT   BINDING         123..125
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT   BINDING         154
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:17135236"
FT   BINDING         155..156
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:17135236"
FT   BINDING         183
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000269|PubMed:17135236"
FT   BINDING         373
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000269|PubMed:17135236"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           19..23
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           30..45
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           52..57
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           59..68
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          74..81
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           85..89
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           95..99
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   TURN            112..114
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          123..126
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           128..141
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           156..158
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           160..172
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          175..182
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          184..189
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           193..199
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           218..222
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           249..251
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          254..260
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           264..272
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   TURN            273..276
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          277..286
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   TURN            289..292
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           294..298
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           302..304
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   TURN            311..313
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           324..338
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          342..348
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   TURN            350..354
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           356..361
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           363..365
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           373..385
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          389..395
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           396..399
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           400..402
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           403..409
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   TURN            410..414
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          418..425
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   TURN            432..434
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           439..442
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   TURN            443..445
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          450..452
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           457..469
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          470..472
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          474..477
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          480..482
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          500..503
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          506..512
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           514..523
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   TURN            524..526
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          530..534
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          537..540
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           543..552
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          554..567
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           568..578
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   STRAND          584..590
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           600..607
FT                   /evidence="ECO:0007829|PDB:6OUV"
FT   HELIX           611..620
FT                   /evidence="ECO:0007829|PDB:6OUV"
SQ   SEQUENCE   629 AA;  67645 MW;  1B73A37BBB8E4870 CRC64;
     MNELPGTSDT PLLDQIHGPK DLKRLSREQL PALTEELRGE IVRVCSRGGL HLASSLGAVD
     IITALHYVLD SPRDRILFDV GHQAYAHKIL TGRRDQMADI KKEGGISGFT KVSESEHDAI
     TVGHASTSLA NALGMALARD AQGKDFHVAA VIGDGSLTGG MALAALNTIG DMGRKMLIVL
     NDNEMSISEN VGAMNKFMRG LQVQKWFQEG EGAGKKAVEA VSKPLADFMS RAKNSTRHFF
     DPASVNPFAA MGVRYVGPVD GHNVQELVWL LERLVDLDGP TILHIVTTKG KGLSYAEADP
     IYWHGPAKFD PATGEYVPSS AYSWSAAFGE AVTEWAKTDP RTFVVTPAMR EGSGLVEFSR
     VHPHRYLDVG IAEEVAVTTA AGMALQGMRP VVAIYSTFLQ RAYDQVLHDV AIEHLNVTFC
     IDRAGIVGAD GATHNGVFDL SFLRSIPGVR IGLPKDAAEL RGMLKYAQTH DGPFAIRYPR
     GNTAQVPAGT WPDLKWGEWE RLKGGDDVVI LAGGKALDYA LKAAEDLPGV GVVNARFVKP
     LDEEMLREVG GRARALITVE DNTVVGGFGG AVLEALNSMN LHPTVRVLGI PDEFQEHATA
     ESVHARAGID APAIRTVLAE LGVDVPIEV
 
 
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