ID DXS_THET8 Reviewed; 615 AA.
AC Q5SMD7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 01-MAY-2013, entry version 59.
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=TTHA0006;
OS Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB8 / ATCC 27634 / DSM 579;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y.,
RA Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the acyloin condensation reaction between C
CC atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield
CC 1-deoxy-D-xylulose-5-phosphate (DXP) (By similarity).
CC -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC deoxy-D-xylulose 5-phosphate + CO(2).
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC similarity).
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose
CC 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC glyceraldehyde 3-phosphate and pyruvate: step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
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DR EMBL; AP008226; BAD69829.1; -; Genomic_DNA.
DR RefSeq; YP_143272.1; NC_006461.1.
DR ProteinModelPortal; Q5SMD7; -.
DR SMR; Q5SMD7; 2-608.
DR STRING; 300852.TTHA0006; -.
DR EnsemblBacteria; BAD69829; BAD69829; BAD69829.
DR GeneID; 3167954; -.
DR KEGG; ttj:TTHA0006; -.
DR PATRIC; 23954939; VBITheThe93045_0006.
DR eggNOG; COG1154; -.
DR HOGENOM; HOG000012986; -.
DR KO; K01662; -.
DR OMA; PVAYHGP; -.
DR ProtClustDB; PRK05444; -.
DR UniPathway; UPA00064; UER00091.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:HAMAP.
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:HAMAP.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.50.920; -; 1.
DR HAMAP; MF_00315; DXP_synth; 1; -.
DR InterPro; IPR005477; Dxylulose-5-P_synthase.
DR InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR InterPro; IPR015941; Transketolase-like_C.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR005476; Transketolase_C.
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; SSF52922; Transketo_C_like; 1.
DR TIGRFAMs; TIGR00204; dxs; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; FALSE_NEG.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Isoprene biosynthesis; Magnesium; Metal-binding;
KW Reference proteome; Thiamine biosynthesis; Thiamine pyrophosphate;
KW Transferase.
FT CHAIN 1 615 1-deoxy-D-xylulose-5-phosphate synthase.
FT /FTId=PRO_0000256498.
FT REGION 113 115 Thiamine pyrophosphate binding (By
FT similarity).
FT REGION 145 146 Thiamine pyrophosphate binding (By
FT similarity).
FT METAL 144 144 Magnesium (By similarity).
FT METAL 173 173 Magnesium (By similarity).
FT BINDING 72 72 Thiamine pyrophosphate (By similarity).
FT BINDING 173 173 Thiamine pyrophosphate (By similarity).
FT BINDING 281 281 Thiamine pyrophosphate (By similarity).
FT BINDING 360 360 Thiamine pyrophosphate (By similarity).
SQ SEQUENCE 615 AA; 67657 MW; 778F43F0B155F4D1 CRC64;
MILDKVNSPE DLKRLSLEEL LLLAEEIRSE IIRVTAQNGG HLASSLGAVE LVLALHRVFD
SPRDRILFDV GHQAYAHKLV TGRKDRFHTL RKEGGISGFT KVSESPHDAI TAGHASTSLA
NALGMVLARD LMGEDYHVVA VIGDGALTGG MALAALNKIG ELQKRMLIVL NDNEMSISEN
VGALNKYFKE LQIRKWVQDA EKLGKNILER ISPQLFGLVD RAKEAAKFLL HQENPFYAWG
IRYVGPVDGH DLKGLVHILE HLKALDGPTL LHVVTKKGKG YKVAEADPIY WHGPPGFDPK
KPEKVSKGYT WSQAFGDAVT ELAHMEPRLF VLTPAMREGS GLVRYSLEHP ERYLDVGICE
DVAVTTAAGL ALRGMKPIVA IYSTFLQRAY DQVIHDVAIE NLPVVFAIDR AGIVGADGAT
HHGVFDIAYL RTVPNLQIAA PKDALELRAM LKKALEVGGP VAIRYPRDNV ERAPEGVWPE
IAWGKWEVLK EGTEAYILAF GKTLRYALEA AGDDPRVGVV NARFLKPLDR EMLRELSRYK
LLTVEDHQKM GGFGSAVLEA LNEMGLKPEV QILGLPDRFF EHGAIPSLHR QAGIDAEGIR
KALAAMGVAL VHERA
//
