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Database: UniProt
Entry: F9EKD4_FUSNU
LinkDB: F9EKD4_FUSNU
Original site: F9EKD4_FUSNU 
ID   F9EKD4_FUSNU            Unreviewed;       584 AA.
AC   F9EKD4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   07-JUN-2017, entry version 34.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|SAAS:SAAS00767547};
DE            EC=2.2.1.7 {ECO:0000256|SAAS:SAAS00767547};
GN   Name=dxs {ECO:0000313|EMBL:EGQ80591.1};
GN   ORFNames=HMPREF9094_0388 {ECO:0000313|EMBL:EGQ80591.1};
OS   Fusobacterium nucleatum subsp. animalis ATCC 51191.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=997347 {ECO:0000313|EMBL:EGQ80591.1, ECO:0000313|Proteomes:UP000005392};
RN   [1] {ECO:0000313|EMBL:EGQ80591.1, ECO:0000313|Proteomes:UP000005392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51191 {ECO:0000313|EMBL:EGQ80591.1,
RC   ECO:0000313|Proteomes:UP000005392};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z.,
RA   Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L.,
RA   Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
RA   Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
RA   San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
RA   Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
RA   Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (MAY-2011) 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).
CC       {ECO:0000256|SAAS:SAAS00767580}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC       deoxy-D-xylulose 5-phosphate + CO(2).
CC       {ECO:0000256|SAAS:SAAS00767589}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00651192};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|SAAS:SAAS00651232};
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       {ECO:0000256|SAAS:SAAS00767582}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|SAAS:SAAS00767578}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000256|SAAS:SAAS00767545}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EGQ80591.1}.
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DR   EMBL; AFQD01000061; EGQ80591.1; -; Genomic_DNA.
DR   EnsemblBacteria; EGQ80591; EGQ80591; HMPREF9094_0388.
DR   PATRIC; fig|997347.4.peg.363; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000005392; Unassembled WGS sequence.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:InterPro.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd02007; TPP_DXS; 1.
DR   Gene3D; 3.40.50.920; -; 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; IPR033248; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43322; PTHR43322; 1.
DR   Pfam; PF13292; DXP_synthase_N; 2.
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   PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005392};
KW   Isoprene biosynthesis {ECO:0000256|SAAS:SAAS00767552};
KW   Magnesium {ECO:0000256|SAAS:SAAS00651250};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00651225};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005392};
KW   Thiamine biosynthesis {ECO:0000256|SAAS:SAAS00767540};
KW   Thiamine pyrophosphate {ECO:0000256|SAAS:SAAS00651235};
KW   Transferase {ECO:0000256|SAAS:SAAS00651241,
KW   ECO:0000313|EMBL:EGQ80591.1}.
FT   DOMAIN       28     47       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
SQ   SEQUENCE   584 AA;  64871 MW;  7A3CA1885E66B165 CRC64;
     MYLEKINSPE DVKKLNIEEM KVLAQEIREA IITRDAKHGG HFGPNLGIVE ATIALHYVFN
     SPKDKFVFDV SHQSYPHKML TGRRQAFTDE THYDDVTGYS NQNESEHDHF ILGHTSTSIS
     LALGLAKARD VKEEKGNVVA IIGDGSLSGG EALEGLDFAG GELKSNFIIV ANDNDMSIAE
     NHGGLYKNLK LLRETDGKAE TNLFKAMGLD YIFVKDGNSL EELIEVFKKV KDINHPVVVH
     ICTQKGKGYK LAEIDKEPWH YTMPFNIENG KPLNVDDSED YTDVTKEYLI KKMKEDKTVV
     TITSGTPGAV GFNKKDRDEV GSQFIDVGIA EETAVAIASG MASKGAKPVY TVVSTFLQRT
     YDQLSQDLCI NNNPATIVVY YAGAIGMTDV THLGWFDIAM MGNIPNLVYL APTTKEEHLA
     MLEWSIEQQE HPVAIRIPGG KMVSTGKKVT KDFSKLNTYE VSQKGEKVAI IGLGTFYQLG
     EKVATLYEEK TGVKATVINP MYITGVDEKL LEELKKDHSL VITLEDGVLD GGFGEKIARF
     YGNSDMKVLN YGLKKEFLDR YDIGKLLTKN RLKADLIVED LLKF
//
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