(data stored in ACNUC7421 zone)

SWISSPROT: A1AZ20_PARDP

ID   A1AZ20_PARDP            Unreviewed;       640 AA.
AC   A1AZ20;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 103.
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   OrderedLocusNames=Pden_0400 {ECO:0000313|EMBL:ABL68514.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68514.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) 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:
CC       Reaction=D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-
CC         D-xylulose 5-phosphate + CO2; Xref=Rhea:RHEA:12605,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57792, ChEBI:CHEBI:59776; EC=2.2.1.7;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00315,
CC         ECO:0000256|SAAS:SAAS01124449};
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|HAMAP-Rule:MF_00315, ECO:0000256|SAAS:SAAS01090559}.
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DR   EMBL; CP000489; ABL68514.1; -; Genomic_DNA.
DR   RefSeq; WP_011746747.1; NC_008686.1.
DR   STRING; 318586.Pden_0400; -.
DR   PRIDE; A1AZ20; -.
DR   EnsemblBacteria; ABL68514; ABL68514; Pden_0400.
DR   KEGG; pde:Pden_0400; -.
DR   eggNOG; ENOG4105C2V; Bacteria.
DR   eggNOG; COG1154; LUCA.
DR   HOGENOM; HOG000012988; -.
DR   KO; K01662; -.
DR   OMA; QVGYHAQ; -.
DR   BioCyc; PDEN318586:G1GW1-400-MONOMER; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000000361; Chromosome 1.
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;
DR   PRODOM; A1AZ20.
DR   SWISS-2DPAGE; A1AZ20.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
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:SAAS01130536};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS01130540};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
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:SAAS01133301};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00460013, ECO:0000313|EMBL:ABL68514.1}.
FT   DOMAIN       39     58       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
FT   REGION      124    126       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   REGION      156    157       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   METAL       155    155       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   METAL       184    184       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   BINDING      83     83       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     184    184       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     293    293       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     375    375       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   640 AA;  67980 MW;  6941482098BC999C CRC64;
     MTHETSDRPS TPILDRVHLP SDLKDLTDRE LRQLADELRA ETVSAVSVTG GHLGAGLGVV
     ELTVALHAVF DAPRDKIIWD VGHQCYPHKI LTGRRDRIRT LRMEGGLSGF TKRSESPYDP
     FGAGHSSTSI SAALGFAMAR ELGGDPGDAI AVIGDGAMSA GMAFEALNNA GDLGKRLFVV
     LNDNEMSIAP PTGALSRYLT RLYAEGPFQD LKAVAKGAVG FLPPTLQEGA RRAKEMLKGM
     TVGGTLFEEL GFSYIGPVDG HDLDQLLPLL RTVKARATGP VLLHVVTRKG KGYGPAERAA
     DKGHATAKFD VETGAQAKAK SNAPSYTSVF ARALVDQASR DARIVAVTAA MPDGTGLNLM
     AERFPRRCFD VGIAEQHAVT FSAGLAAGGM KPFCALYSTF LQRGYDQVVH DVAIQRLPVR
     FAIDRAGLVG ADGATHAGAY DVAFLANLPG MVVMAAADEA ELVHMVATAA AHDEGPIAFR
     YPRGEGTGVE MPERGEVLVI GKGRVMAEGK GVAILSFGTR LSEVMRARES LAARGVSPTV
     VDARFAKPLD RDLILRLART HEALITIEEG AVGGFGSLVA QLLADEGVFD GGLRFRQMVL
     PDTFIDHASP EAMYREARMS APDIEAKVLE VLGVALAKRA
//

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