GenomeNet

Database: UniProt
Entry: S5TJU8_9CORY
LinkDB: S5TJU8_9CORY
Original site: S5TJU8_9CORY 
ID   S5TJU8_9CORY            Unreviewed;       616 AA.
AC   S5TJU8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   07-NOV-2018, entry version 36.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE            EC=2.2.1.7 {ECO:0000256|HAMAP-Rule:MF_00315};
DE   AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE            Short=DXP synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE            Short=DXPS {ECO:0000256|HAMAP-Rule:MF_00315};
GN   Name=dxs {ECO:0000256|HAMAP-Rule:MF_00315};
GN   ORFNames=B841_07525 {ECO:0000313|EMBL:AGS34978.1};
OS   Corynebacterium maris DSM 45190.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS34978.1, ECO:0000313|Proteomes:UP000015388};
RN   [1] {ECO:0000313|EMBL:AGS34978.1, ECO:0000313|Proteomes:UP000015388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA   Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT   "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT   45190).";
RL   Submitted (NOV-2012) 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). {ECO:0000256|HAMAP-
CC       Rule:MF_00315, ECO:0000256|SAAS:SAAS01090567}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC       deoxy-D-xylulose 5-phosphate + CO(2). {ECO:0000256|HAMAP-
CC       Rule:MF_00315, ECO:0000256|SAAS:SAAS01090541}.
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|HAMAP-Rule:MF_00315, ECO:0000256|SAAS:SAAS01090565}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00315,
CC       ECO:0000256|SAAS:SAAS01090540}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000256|SAAS:SAAS01090559}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP003924; AGS34978.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGS34978; AGS34978; B841_07525.
DR   KEGG; cmd:B841_07525; -.
DR   PATRIC; fig|1224163.3.peg.1512; -.
DR   KO; K01662; -.
DR   OrthoDB; POG091H015K; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000015388; Chromosome.
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   Complete proteome {ECO:0000313|Proteomes:UP000015388};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS01090549};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00086467};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00086515};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015388};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS01090534};
KW   Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00086495};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00086511, ECO:0000313|EMBL:AGS34978.1}.
FT   DOMAIN       10     29       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
FT   REGION       95     97       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   REGION      128    129       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   METAL       127    127       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   METAL       156    156       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   BINDING      54     54       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     156    156       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     267    267       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     349    349       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   616 AA;  65391 MW;  B180AAFB4D67522F CRC64;
     MLNDLAAEVR ALLVEKVSAT GGHLGPNLGV VELSIALHRV FDSPQEPIIF DTSHQSYVHK
     MLTGRSHQFD TLRKKGGLSG YTDRAESEHD WTESSHASAA LSYADGLAKA KELTGDGERN
     VVAVVGDGAL TGGMCWEALN NIASGDRNVV VVINDNGRSY SPTIGGIADN LSAIRTRHGY
     DELMEEGKKR LKQMGWVGER TYEALAAFKE GVKSQLVPTE MFSDLGLKYV GPVNGHDLDH
     LLHDLEYAKG YDGPIIVHVV TEKGHGFAPA VNDVKDQMHA TGIIDPVTGL PSGNAPGPKW
     TSAFSEELIQ AGRDRDDIVA ITAAMAGPTG LQPFADEFPD RFFDVGIAEA HALTSAAGLA
     LGGMHPVVAL YSTFLNRGFD QLLMDVGLLK LPVTLVLDRA GVTGSDGASH NGVWDLAIAS
     IVPGIRIAAP RDGARLREQF QEAITVDDGP TAVRFPKGEL PADVEAVSRL NDGVDILRYS
     DAGDEDPDAV SVLIVSVGAL ADVALAVAES LAEEHVDVTV VDPRWVAPVP GSVLALADDH
     DLVVTVEDGV IRGGVGSLIS EAMNAAEIDT PIRHLAFPDV FPKHASRSEL LAEVGLDAEG
     ATASVMGWME NIFDRD
//
DBGET integrated database retrieval system