(data stored in SCRATCH zone)

HOGENOM: EDWI9_1_PE1011

ID   EDWI9_1_PE1011                       STANDARD;      PRT;   621 AA.
AC   EDWI9_1_PE1011; C5BCH9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase; EC=2.2.1
DE   7;AltName: Full=1-deoxyxylulose-5-phosphate synthase; Short=DXP synthase;
DE   Short=DXPS; (EDWI9_1.PE1011).
GN   Name=dxs; OrderedLocusNames=NT01EI_1061;
OS   EDWARDSIELLA ICTALURI 93-146.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS EDWI9_1.PE1011.
CC       Edwardsiella ictaluri 93-146 chromosome, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:DXS_EDWI9
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 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.
CC   -!- GENE_FAMILY: HOG000012988 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C5BCH9; -.
DR   EMBL; CP001600; ACR68273.1; -; Genomic_DNA.
DR   RefSeq; YP_002932508.1; NC_012779.1.
DR   STRING; C5BCH9; -.
DR   GeneID; 7959444; -.
DR   GenomeReviews; CP001600_GR; NT01EI_1061.
DR   KEGG; eic:NT01EI_1061; -.
DR   OMA; DPILYHG; -.
DR   ProtClustDB; PRK05444; -.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:EC.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEDR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00315; DXP_synth; 1; -.
DR   InterPro; IPR001017; DH_E1.
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   InterPro; IPR005474; Transketolase_N.
DR   Gene3D; G3DSA:3.40.50.920; Transketo_C_like; 1.
DR   Pfam; PF00676; E1_dh; 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; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
DR   HOGENOMDNA; EDWI9_1.PE1011; -.
KW   1-deoxy-D-xylulose-5-phosphate synthase;
KW   Complete proteome; Isoprene biosynthesis; Thiamine biosynthesis;
KW   Thiamine pyrophosphate; Transferase.
SQ   SEQUENCE   621 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSFDIAKYPT LALVPDPDDL RLLPKESLPT LCDELRQYLL NSVSRSSGHF ASGLGAVELT
     VALHYVYQTP FDSLIWDVGH QAYPHKILTG RRDRIATIRQ KGGLHPFPWR DESEYDTLSV
     GHSSTSISAG LGMAVAAERE GLGRRTVCVI GDGAMTAGMA FEAMNHAGDI KADMLVVLND
     NEMSISENVG ALNNHLAQLL SGKLYASLRE GGKKMLSGLP PIKELVKRTE EHLKGMVVPG
     TLFEELGFNY IGPVDGHDVQ ALVATLKNMR DLKGPQLLHI MTKKGKGYAP AEKDPISWHA
     VPKFDPASGT LPKSSGTLPT YSKIFGDWLC ETAHNDDRLM GITPAMREGS GMVRFSREYP
     QQYFDVAIAE QHAVTFGAGL AIGGYHPVVA IYSSFLQRAY DQVIHDVAIQ RLPVLFAIDR
     GGIVGADGQT HQGAFDLSFL RCIPNLVIMT PSDENECRQM LQTGYEYREG PSAVRYPRGT
     GTGAPLTPPQ ALPIGKGVLR RRGERIAILN FGSLLPQALE AAERLNASVA DMRFVKPLDD
     ALVRSLAEQH EYLVTLEENA VMGGAGSGVN ELLMQLRLPR PVLNIGLQDS FVPQGSQEEI
     RRDLQLDADG ILAQLEGWLA R
//

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