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Database: UniProt
Entry: Q2RR29
LinkDB: Q2RR29
Original site: Q2RR29 
ID   DXS2_RHORT              Reviewed;         645 AA.
AC   Q2RR29;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   01-OCT-2014, entry version 63.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXP synthase 2 {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXPS 2 {ECO:0000255|HAMAP-Rule:MF_00315};
GN   Name=dxs2 {ECO:0000255|HAMAP-Rule:MF_00315};
GN   OrderedLocusNames=Rru_A2619;
OS   Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S.1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G.,
RA   Reslewic S., Zhou S., Schwartz D.C.;
RT   "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC
RT   11170.";
RL   Submitted (DEC-2005) 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:0000255|HAMAP-
CC       Rule:MF_00315}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC       deoxy-D-xylulose 5-phosphate + CO(2). {ECO:0000255|HAMAP-
CC       Rule:MF_00315}.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00315}.
CC   -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00315}.
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:0000255|HAMAP-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; CP000230; ABC23416.1; -; Genomic_DNA.
DR   RefSeq; YP_427703.1; NC_007643.1.
DR   ProteinModelPortal; Q2RR29; -.
DR   STRING; 269796.Rru_A2619; -.
DR   EnsemblBacteria; ABC23416; ABC23416; Rru_A2619.
DR   GeneID; 3836054; -.
DR   KEGG; rru:Rru_A2619; -.
DR   PATRIC; 23328982; VBIRhoRub82919_2729.
DR   eggNOG; COG1154; -.
DR   HOGENOM; HOG000012988; -.
DR   KO; K01662; -.
DR   OMA; GHQTYAH; -.
DR   OrthoDB; EOG6BKJ6P; -.
DR   BioCyc; RRUB269796:GCN1-2662-MONOMER; -.
DR   UniPathway; UPA00064; UER00091.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 3.
DR   HAMAP; MF_00315; DXP_synth; 1.
DR   InterPro; IPR005477; Dxylulose-5-P_synthase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR005476; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
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; 3.
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; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Reference proteome; Thiamine biosynthesis; Thiamine pyrophosphate;
KW   Transferase.
FT   CHAIN         1    645       1-deoxy-D-xylulose-5-phosphate synthase
FT                                2.
FT                                /FTId=PRO_0000256474.
FT   REGION      120    122       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   REGION      152    153       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   METAL       151    151       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   METAL       180    180       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   BINDING      79     79       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     180    180       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     291    291       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     373    373       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   645 AA;  68164 MW;  13A41BA0A605F3D4 CRC64;
     MTSRPITPLL DTIRGPSDTR GLSVAQLEQL AREVRAEMID AVSVTGGHLG SGLGVVELTV
     ALHHVFDTPD DRIIWDVGHQ CYPHKILTGR RDRIRTLRQG GGLSGFTLRE ESPYDPFGAG
     HSSTSISAGL GMAIGSALAG DARDVVAVIG DGSMSAGMAY EAMNNAGAAK SRLIVILNDN
     DMSIAPPVGA MSAYLSRLLS SKSWLSIRTL AKEIVARLPD ALERTAKRAE EYARGMVTGG
     GTLFEEMGFY YVGPIDGHRM DHLVPVLRNV REAGRDGPVL IHVVTQKGKG YAPAENAPDK
     YHGVSRFNVV TGVQEKAKPQ APSYTAVFGK QLVAAAAKDH RIVAVTAAMP GGTGLDKLAA
     AYPQRCFDVG IAEQHAVTFA AGLACEGLKP FVALYSSFLQ RGYDQVVHDV VLQKLPVRFA
     IDRAGFVGAD GATHGGVFDM AFLGCLPNLV VMCAADEAEL ARMVVTAAGH DSGPIALRYP
     RGEGVGVEIP EDPQPLAIGK GRIVREGKGV ALLSIGTRLQ SCLEACEILA ARGLTPTVAD
     ARFLKPFDEE LVADLAARHE VLIVVEEGAI GGFCSHVATW LANQGLLDGG LKLRALHIPD
     RFFEHDAPEV QCAKAGIDAQ AITTAVLDAL KLETSATIDA GALKA
//
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