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Database: UniProt
Entry: A0A0L0W784_CLOPU
LinkDB: A0A0L0W784_CLOPU
Original site: A0A0L0W784_CLOPU 
ID   A0A0L0W784_CLOPU        Unreviewed;       624 AA.
AC   A0A0L0W784;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   07-NOV-2018, entry version 19.
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   ECO:0000313|EMBL:KNF07408.1};
GN   ORFNames=CLPU_17c00330 {ECO:0000313|EMBL:KNF07408.1};
OS   Clostridium purinilyticum (Gottschalkia purinilyticum).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Gottschalkiaceae;
OC   Gottschalkia.
OX   NCBI_TaxID=1503 {ECO:0000313|EMBL:KNF07408.1, ECO:0000313|Proteomes:UP000037267};
RN   [1] {ECO:0000313|Proteomes:UP000037267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1384 {ECO:0000313|Proteomes:UP000037267};
RA   Poehlein A., Schiel-Bengelsdorf B., Bengelsdorf F.R., Daniel R.,
RA   Duerre P.;
RT   "Draft genome sequence of the purine-degrading Gottschalkia
RT   purinilyticum DSM 1384 (formerly Clostridium purinilyticum).";
RL   Submitted (JUL-2015) 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   -!- 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:KNF07408.1}.
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DR   EMBL; LGSS01000017; KNF07408.1; -; Genomic_DNA.
DR   EnsemblBacteria; KNF07408; KNF07408; CLPU_17c00330.
DR   PATRIC; fig|1503.3.peg.713; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000037267; Unassembled WGS sequence.
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:UP000037267};
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:UP000037267};
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:KNF07408.1}.
FT   DOMAIN       30     49       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
FT   REGION      115    117       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   REGION      147    148       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   METAL       146    146       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   METAL       175    175       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   BINDING      74     74       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     175    175       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     286    286       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     367    367       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   624 AA;  69072 MW;  2891E7A89A0585B4 CRC64;
     MKNLLSNYVG LEEIKNMDTK ELTFLAEDIR KFIIDSVSRT GGHLASNLGV VELTIAIHRV
     FDSGKDRIIW DVGHQSYVHK ILTGRKDKFH TLRQYKGLSG FPKRKESSHD AFDTGHSSTS
     ISAGLGYALS RDIKKEDYDV VCVIGDGAMT AGMAFEALNH AGDTKTDLIV ILNDNEMSIS
     ENVGGLSKYL DKIRTTPTYF KMKEDVESIL NSIPAIGKRM FKTAEKAKDS LKYFLLPGMF
     FEDLGFKYLG PVDGHNINEI IDALERAKSV KGPVLIHAVT KKGKGYKPAE QYPDKFHGAS
     SFDVETGLSL SKETNLTYSD VLGNTLVDLA KKDDKILAIT AAMPSGTGLD DFKEKFTNRF
     FDVGIAEQHG VTLAAGFAAN GMKPFFAVYS TFLQRAYDQI LHDVCIQNLP VTFAIDRAGL
     VGNDGETHHG AFDLSYLSHI PNMTIIAPKD KNEFIKMIKF ASEFNGPIAI RYAKGNCYDL
     SLVKNDDLPI EYGKGELLNQ GRDIAMIATG KMVEQGYKVL ERLKAKGKNI TLVNARFIKP
     LDEELILKIS KSHSIIMTME DNAKIGGLGS LVNSLLMRNG YKGEVINIGL PDEFIEHGSV
     EELFKEHGMD IDSITNLVMD KFNI
//
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