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-MAY-2013, entry version 56.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase 2;
DE EC=2.2.1.7;
DE AltName: Full=1-deoxyxylulose-5-phosphate synthase 2;
DE Short=DXP synthase 2;
DE Short=DXPS 2;
GN Name=dxs2; 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) (By similarity).
CC -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC deoxy-D-xylulose 5-phosphate + CO(2).
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC similarity).
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 -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
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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; HGAFDIS; -.
DR ProtClustDB; PRK05444; -.
DR UniPathway; UPA00064; UER00091.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA: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:HAMAP.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.50.920; -; 1.
DR HAMAP; MF_00315; DXP_synth; 1; -.
DR InterPro; IPR005477; Dxylulose-5-P_synthase.
DR InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR InterPro; IPR015941; Transketolase-like_C.
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; SSF52922; Transketo_C_like; 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 (By
FT similarity).
FT REGION 152 153 Thiamine pyrophosphate binding (By
FT similarity).
FT METAL 151 151 Magnesium (By similarity).
FT METAL 180 180 Magnesium (By similarity).
FT BINDING 79 79 Thiamine pyrophosphate (By similarity).
FT BINDING 180 180 Thiamine pyrophosphate (By similarity).
FT BINDING 291 291 Thiamine pyrophosphate (By similarity).
FT BINDING 373 373 Thiamine pyrophosphate (By similarity).
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
//
