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DXS2_KITGR
ID   DXS2_KITGR              Reviewed;         633 AA.
AC   Q8VUR8;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase 2 {ECO:0000255|HAMAP-Rule:MF_00315};
DE            EC=2.2.1.7 {ECO:0000255|HAMAP-Rule:MF_00315};
DE   AltName: Full=1-deoxyxylulose-5-phosphate synthase 2 {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXP synthase 2 {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXPS 2 {ECO:0000255|HAMAP-Rule:MF_00315};
GN   Name=dxs2 {ECO:0000255|HAMAP-Rule:MF_00315};
OS   Kitasatospora griseola (Streptomyces griseolosporeus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Kitasatospora.
OX   NCBI_TaxID=2064;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MF730-N6;
RX   PubMed=12036054; DOI=10.1271/bbb.66.808;
RA   Hamano Y., Dairi T., Yamamoto M., Kuzuyama T., Itoh N., Seto H.;
RT   "Growth-phase dependent expression of the mevalonate pathway in a terpenoid
RT   antibiotic-producing Streptomyces strain.";
RL   Biosci. Biotechnol. Biochem. 66:808-819(2002).
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:0000255|HAMAP-Rule:MF_00315}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00315};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00315};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00315};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00315};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00315};
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00315}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00315}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00315}.
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DR   EMBL; AB064999; BAB83664.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8VUR8; -.
DR   SMR; Q8VUR8; -.
DR   STRING; 2064.TR51_08925; -.
DR   UniPathway; UPA00064; UER00091.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-UniRule.
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:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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   InterPro; IPR005474; Transketolase_N.
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; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis; Magnesium; Metal-binding; Thiamine biosynthesis;
KW   Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..633
FT                   /note="1-deoxy-D-xylulose-5-phosphate synthase 2"
FT                   /id="PRO_0000189122"
FT   BINDING         73
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         113..115
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         145
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         146..147
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         175
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         175
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         286
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         367
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
SQ   SEQUENCE   633 AA;  67639 MW;  E521138A3751FE86 CRC64;
     MALLTRIRGP RDLDRLTPAQ LAELAEEIRA FLVEEVSKTG GHLGPNLGVV ELTLAMHRVF
     DSPRDRILFD TGHQSYVHKL LTGRQDFSRL KMKGGLSGYP SRAESEHDVI ENSHASTVLG
     YADGLAKANK IQGHKDRPVV AVIGDGALTG GMAWEALNNI ADSQDLPIVI VVNDNERSYS
     PTIGGLANHL ATLRTTQGYE RFLSWGKDAL QRTPVVGQAM FDTLHGAKKG LKDFIAPQGM
     FEDLGLKYLG PIDGHDLQAL ESAFTKARNF GGPVIVHCIT EKGRGYHAAE NNDEDRFHAV
     GVIHPDTGLP VKTSGKDWTS VFGEEMVALG RERRDLVAIT AAMLHPVGLA PFAKAYPERI
     FDVGIAEQHA AVCAAGLATN GLHPVVAVYA TFLNRAFDQV LMDVALHKLG VTFVLDRAGV
     TGTDGASHNG MWDMSILQVV PGLRLAAPRD AEQVRLQLRE AVEVADAPTV VRYSKGNVGP
     AVPAVGTVGG MDVLRRPEAD SADEAADVLI VSIGAMAPTC LEAAELLAQQ GISSTVVDPR
     WVKPVDAALP GLAAQHRLVV TVEDNGRAGG VGSAIAQALR DADVDVPLRD FGIPQEFLDH
     ASRGEILDEI GLTAPAIAKK IEALVSTRSF ARS
 
 
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