DXS_SYNP6
ID DXS_SYNP6 Reviewed; 636 AA.
AC Q9R6S7; Q5N343;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE EC=2.2.1.7 {ECO:0000255|HAMAP-Rule:MF_00315};
DE AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE Short=DXP synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE Short=DXPS {ECO:0000255|HAMAP-Rule:MF_00315};
GN Name=dxs {ECO:0000255|HAMAP-Rule:MF_00315}; OrderedLocusNames=syc1087_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10556522; DOI=10.1016/s0014-5793(99)01397-6;
RA Miller B., Heuser T., Zimmer W.;
RT "A Synechococcus leopoliensis SAUG 1402-1 operon harboring the 1-
RT deoxyxylulose 5-phosphate synthase gene and two additional open reading
RT frames is functionally involved in the dimethylallyl diphosphate
RT synthesis.";
RL FEBS Lett. 460:485-490(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
CC -!- FUNCTION: Catalyzes the acyloin condensation reaction between C atoms 2
CC and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-
CC xylulose-5-phosphate (DXP). {ECO:0000255|HAMAP-Rule:MF_00315}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-
CC xylulose 5-phosphate + CO2; Xref=Rhea:RHEA:12605, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57792,
CC ChEBI:CHEBI:59776; EC=2.2.1.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00315};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00315};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00315};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00315};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00315};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-
CC phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC glyceraldehyde 3-phosphate and pyruvate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00315}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00315}.
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00315}.
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DR EMBL; Y18874; CAB60078.1; -; Genomic_DNA.
DR EMBL; AP008231; BAD79277.1; -; Genomic_DNA.
DR RefSeq; WP_011243398.1; NC_006576.1.
DR AlphaFoldDB; Q9R6S7; -.
DR SMR; Q9R6S7; -.
DR STRING; 269084.syc1087_c; -.
DR EnsemblBacteria; BAD79277; BAD79277; syc1087_c.
DR KEGG; syc:syc1087_c; -.
DR eggNOG; COG1154; Bacteria.
DR OMA; QVGYHAQ; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000001175; 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 Isoprene biosynthesis; Magnesium; Metal-binding; Thiamine biosynthesis;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..636
FT /note="1-deoxy-D-xylulose-5-phosphate synthase"
FT /id="PRO_0000189160"
FT BINDING 72
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 113..115
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 145..146
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 174
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 287
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 370
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT CONFLICT 100
FT /note="L -> P (in Ref. 1; CAB60078)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="A -> G (in Ref. 1; CAB60078)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="H -> Y (in Ref. 1; CAB60078)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 68902 MW; B766839481BF7E27 CRC64;
MHLSEITHPN QLHGLSVAQL EQIGHQIREK HLQTVAATGG HLGPGLGVVE LTLALYQTLD
LDRDKVVWDV GHQAYPHKLL TGRYHNFHTL RQKDGIAGYL KRTENRFDHF GAGHASTSIS
AALGMALARD AQGEDYRCVA VIGDGSLTGG MALEAINHAG HLPKTRLLVV LNDNDMSISP
NVGALSRYLN KIRVSEPMQL LTDGLTQGMQ QIPFVGGAIT QGFEPVKEGM KRLSYSKIGA
VFEELGFTYM GPVDGHNLEE LIATFREAHK HTGPVLVHVA TTKGKGYPYA EEDQVGYHAQ
NPFDLATGKA KPASKPKPPS HSKVFGQTLT TLAKSDRRIV GITAAMATGT GLDILQKALP
KQYIDVGIAE QHAVVLAAGM ACDGMRPVVA IYSTFLQRAF DQVIHDVCIQ KLPVFFCLDR
AGIVGADGPT HQGMYDIAYL RLIPNMVLMA PKDEAELQRM LVTGIEYDGP IAMRFPRGNG
IGVPLPEEGW ESLPIGKAEQ LRQGDDLLML AYGSMVYPAL QTAELLNEHG ISATVINARF
AKPLDEELIV PLARQIGKVV TFEEGCLPGG FGSAIMESLQ AHDLQVPVLP IGVPDLLVEH
ASPDESKQEL GLTPRQMADR ILEKFGSRQR IGAASA
