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Database: UniProt
Entry: DXS_MYCTU
LinkDB: DXS_MYCTU
Original site: DXS_MYCTU 
ID   DXS_MYCTU               Reviewed;         638 AA.
AC   P9WNS3; L0TAC0; O07184; P0A554;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   23-MAY-2018, entry version 28.
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=Rv2682c;
GN   ORFNames=MTCY05A6.03c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.M111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
RA   Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
RA   Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
RA   Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
RA   Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high
RT   resolution mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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:
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-
CC       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.
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}.
DR   EMBL; AL123456; CCP45480.1; -; Genomic_DNA.
DR   PIR; E70528; E70528.
DR   RefSeq; WP_003413891.1; NZ_KK339370.1.
DR   RefSeq; YP_177898.1; NC_000962.3.
DR   ProteinModelPortal; P9WNS3; -.
DR   SMR; P9WNS3; -.
DR   STRING; 83332.Rv2682c; -.
DR   BindingDB; P9WNS3; -.
DR   ChEMBL; CHEMBL5091; -.
DR   SwissLipids; SLP:000001173; -.
DR   PaxDb; P9WNS3; -.
DR   PRIDE; P9WNS3; -.
DR   EnsemblBacteria; CCP45480; CCP45480; Rv2682c.
DR   GeneID; 887461; -.
DR   KEGG; mtu:Rv2682c; -.
DR   TubercuList; Rv2682c; -.
DR   eggNOG; ENOG4105C2V; Bacteria.
DR   eggNOG; COG1154; LUCA.
DR   KO; K01662; -.
DR   OMA; AINHAGH; -.
DR   PhylomeDB; P9WNS3; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IDA:MTBBASE.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR   GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
DR   GO; GO:0030975; F:thiamine binding; IDA:MTBBASE.
DR   GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0040007; P:growth; IMP:MTBBASE.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IDA:MTBBASE.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
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; 3.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00204; dxs; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Reference proteome; Thiamine biosynthesis; Thiamine pyrophosphate;
KW   Transferase.
FT   CHAIN         1    638       1-deoxy-D-xylulose-5-phosphate synthase.
FT                                /FTId=PRO_0000189130.
FT   REGION      112    114       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   REGION      145    146       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   METAL       144    144       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   METAL       173    173       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   BINDING      71     71       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     173    173       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     284    284       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     365    365       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   638 AA;  67885 MW;  6F8DC2A78290873F CRC64;
     MLQQIRGPAD LQHLSQAQLR ELAAEIREFL IHKVAATGGH LGPNLGVVEL TLALHRVFDS
     PHDPIIFDTG HQAYVHKMLT GRSQDFATLR KKGGLSGYPS RAESEHDWVE SSHASAALSY
     ADGLAKAFEL TGHRNRHVVA VVGDGALTGG MCWEALNNIA ASRRPVIIVV NDNGRSYAPT
     IGGVADHLAT LRLQPAYEQA LETGRDLVRA VPLVGGLWFR FLHSVKAGIK DSLSPQLLFT
     DLGLKYVGPV DGHDERAVEV ALRSARRFGA PVIVHVVTRK GMGYPPAEAD QAEQMHSTVP
     IDPATGQATK VAGPGWTATF SDALIGYAQK RRDIVAITAA MPGPTGLTAF GQRFPDRLFD
     VGIAEQHAMT SAAGLAMGGL HPVVAIYSTF LNRAFDQIMM DVALHKLPVT MVLDRAGITG
     SDGASHNGMW DLSMLGIVPG IRVAAPRDAT RLREELGEAL DVDDGPTALR FPKGDVGEDI
     SALERRGGVD VLAAPADGLN HDVLLVAIGA FAPMALAVAK RLHNQGIGVT VIDPRWVLPV
     SDGVRELAVQ HKLLVTLEDN GVNGGAGSAV SAALRRAEID VPCRDVGLPQ EFYEHASRSE
     VLADLGLTDQ DVARRITGWV AALGTGVCAS DAIPEHLD
//
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