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Database: UniProt
Entry: R6N5U6_9CLOT
LinkDB: R6N5U6_9CLOT
Original site: R6N5U6_9CLOT 
ID   R6N5U6_9CLOT            Unreviewed;       433 AA.
AC   R6N5U6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   07-NOV-2018, entry version 23.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|SAAS:SAAS01090563};
DE            EC=2.2.1.7 {ECO:0000256|SAAS:SAAS01090563};
GN   ORFNames=BN615_01427 {ECO:0000313|EMBL:CDC07398.1};
OS   Clostridium sp. CAG:343.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium; environmental samples.
OX   NCBI_TaxID=1262796 {ECO:0000313|EMBL:CDC07398.1, ECO:0000313|Proteomes:UP000018148};
RN   [1] {ECO:0000313|EMBL:CDC07398.1, ECO:0000313|Proteomes:UP000018148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:343 {ECO:0000313|Proteomes:UP000018148};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
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).
CC       {ECO:0000256|SAAS:SAAS01090567}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC       deoxy-D-xylulose 5-phosphate + CO(2).
CC       {ECO:0000256|SAAS:SAAS01090541}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS01090564};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|SAAS:SAAS01090562};
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:SAAS01090565}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|SAAS:SAAS01090540}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000256|SAAS:SAAS01090559}.
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:CDC07398.1}.
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DR   EMBL; CBEQ010000070; CDC07398.1; -; Genomic_DNA.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000018148; 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   InterPro; IPR005477; Dxylulose-5-P_synthase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43322; PTHR43322; 1.
DR   Pfam; PF13292; DXP_synthase_N; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   TIGRFAMs; TIGR00204; dxs; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000018148};
KW   Isoprene biosynthesis {ECO:0000256|SAAS:SAAS01090549};
KW   Magnesium {ECO:0000256|SAAS:SAAS01090547};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01090551};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018148};
KW   Thiamine biosynthesis {ECO:0000256|SAAS:SAAS01090534};
KW   Thiamine pyrophosphate {ECO:0000256|SAAS:SAAS01090548};
KW   Transferase {ECO:0000256|SAAS:SAAS01090542}.
FT   DOMAIN       27     46       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
SQ   SEQUENCE   433 AA;  47919 MW;  D6A6437B3A828BE3 CRC64;
     MIEKINSAKD VKKLNIEEQK QLAEEIRKYI LEIVSKNGGH LASNLGVVEL TIALHTVFDL
     PKDKIVWDVG HQTYVHKIIT GRREQLNTLR QLNGIAGFPK TNESETDCFN TGHSSTSISA
     ALGMARARDI KGEKNNVIAV IGDGALTGGM ALEALNDAGS SQTRLTVILN DNEMSISKNI
     GGVNMLLSKL RTKKTYTKSN VSMKNIINKV PIIGQPFVKI VQRLKRSIKQ LIIPKMFFED
     IGFRYLGPVD GHNIEELERM LNISKQLEGP VLIHVLTKKG KGYKIAEENP DKFHATGPFE
     IETGKPKKEK SKDYSKVFGD KLVELAKKND KIVAITASMK DGTGLTKFAK EFPDRFFDIG
     IAEQHALGLA AGMAKEGVIP VVPIYSSFYQ RAYDQVIHDI AIQNLPVIMC VDRAGVVGAD
     RRNTSRSSRY GVF
//
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