位置:首页 > 蛋白库 > TPS1_ORYSJ
TPS1_ORYSJ
ID   TPS1_ORYSJ              Reviewed;         548 AA.
AC   Q2QWK9; A0A0P0Y7Y2; Q0IPK3;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Probable thiamine biosynthetic bifunctional enzyme, chloroplastic;
DE   Includes:
DE     RecName: Full=Thiamine-phosphate synthase;
DE              Short=TP synthase;
DE              Short=TPS;
DE              EC=2.5.1.3 {ECO:0000250|UniProtKB:Q5M731};
DE     AltName: Full=Thiamine-phosphate pyrophosphorylase;
DE              Short=TMP pyrophosphorylase;
DE              Short=TMP-PPase;
DE   Includes:
DE     RecName: Full=Hydroxymethylpyrimidine kinase;
DE              Short=HMP kinase;
DE              EC=2.7.1.49 {ECO:0000250|UniProtKB:P30137};
DE   Flags: Precursor;
GN   OrderedLocusNames=Os12g0192500, LOC_Os12g09000; ORFNames=OsJ_35490;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: Essential for thiamine biosynthesis. Bifunctional enzyme that
CC       catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate
CC       (HMP-P) to HMP-PP and condenses 4-methyl-5-(beta-hydroxyethyl)thiazole
CC       monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine
CC       pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
CC       {ECO:0000250|UniProtKB:Q5M731}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl
CC         phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2
CC         H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3;
CC         Evidence={ECO:0000250|UniProtKB:Q5M731};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-
CC         methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate
CC         + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575,
CC         ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3;
CC         Evidence={ECO:0000250|UniProtKB:Q5M731};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl-
CC         5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine
CC         phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841,
CC         ChEBI:CHEBI:58296; EC=2.5.1.3;
CC         Evidence={ECO:0000250|UniProtKB:Q5M731};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC         methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC         Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC         EC=2.7.1.49; Evidence={ECO:0000250|UniProtKB:P30137};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC       thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine
CC       and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC       amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DP000011; ABA96049.2; -; Genomic_DNA.
DR   EMBL; AP008218; BAF29362.2; -; Genomic_DNA.
DR   EMBL; AP014968; BAT16214.1; -; Genomic_DNA.
DR   EMBL; CM000149; EEE52897.1; -; Genomic_DNA.
DR   EMBL; AK066087; BAG89812.1; -; mRNA.
DR   RefSeq; XP_015618273.1; XM_015762787.1.
DR   AlphaFoldDB; Q2QWK9; -.
DR   SMR; Q2QWK9; -.
DR   STRING; 4530.OS12T0192500-02; -.
DR   PaxDb; Q2QWK9; -.
DR   PRIDE; Q2QWK9; -.
DR   EnsemblPlants; Os12t0192500-02; Os12t0192500-02; Os12g0192500.
DR   GeneID; 4351707; -.
DR   Gramene; Os12t0192500-02; Os12t0192500-02; Os12g0192500.
DR   KEGG; osa:4351707; -.
DR   eggNOG; KOG2598; Eukaryota.
DR   HOGENOM; CLU_018272_7_0_1; -.
DR   InParanoid; Q2QWK9; -.
DR   OMA; GHIFPTN; -.
DR   OrthoDB; 1245353at2759; -.
DR   PlantReactome; R-OSA-1119629; Thiamine biosynthesis.
DR   UniPathway; UPA00060; UER00137.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000000763; Chromosome 12.
DR   Proteomes; UP000007752; Chromosome 12.
DR   Proteomes; UP000059680; Chromosome 12.
DR   ExpressionAtlas; Q2QWK9; baseline and differential.
DR   Genevisible; Q2QWK9; OS.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IBA:GO_Central.
DR   GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01169; HMPP_kinase; 1.
DR   CDD; cd00564; TMP_TenI; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   HAMAP; MF_00097; TMP_synthase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR045029; HMP/HMP-P_kinase.
DR   InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR036206; ThiamineP_synth_sf.
DR   InterPro; IPR022998; ThiamineP_synth_TenI.
DR   InterPro; IPR034291; TMP_synthase.
DR   PANTHER; PTHR20858; PTHR20858; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   Pfam; PF02581; TMP-TENI; 1.
DR   SUPFAM; SSF51391; SSF51391; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR00097; HMP-P_kinase; 1.
DR   TIGRFAMs; TIGR00693; thiE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; Kinase; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Plastid; Reference proteome;
KW   Thiamine biosynthesis; Transferase; Transit peptide.
FT   TRANSIT         1..47
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..548
FT                   /note="Probable thiamine biosynthetic bifunctional enzyme,
FT                   chloroplastic"
FT                   /id="PRO_0000420254"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         372..376
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000250"
FT   BINDING         404
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000250"
FT   BINDING         405
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         424
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         443
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000250"
FT   BINDING         469..471
FT                   /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT                   ylidene]ethyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:62899"
FT                   /evidence="ECO:0000250"
FT   BINDING         472
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000250"
FT   BINDING         499
FT                   /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT                   ylidene]ethyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:62899"
FT                   /evidence="ECO:0000250"
FT   BINDING         522..523
FT                   /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT                   ylidene]ethyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:62899"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   548 AA;  57804 MW;  9B5204B75835A72E CRC64;
     MAAAPQQSVH PSLPSSTSTL RLLISSSPRR PPPPPPRARR YNRLAASASA AREMPWPHVL
     TVAGSDSGGG AGIQADIKAC AALGAYCSSV VTAVTAQNTA GVQGIHVVPE EFIREQLNSV
     LSDMSVDVVK TGMLPSIGVV RVLCESLKKF PVKALVVDPV MVSTSGDTLS ESSTLSVYRD
     ELFAMADIVT PNVKEASRLL GGVSLRTVSD MRNAAESIYK FGPKHVLVKG GDMLESSDAT
     DVFFDGKEFI ELHAHRIKTH NTHGTGCTLA SCIASELAKG ATMLHAVQVA KNFVESALHH
     SKDLVVGNGP QGPFDHLFKL KCPPYNVGSQ PSFKPDQLFL YAVTDSGMNK KWGRSIKEAV
     QAAIEGGATI VQLREKDSET REFLEAAKAC MEICKSSGVP LLINDRVDIA LACNADGVHV
     GQLDMSAHEV RELLGPGKII GVSCKTPAQA QQAWNDGADY IGCGGVFPTS TKANNPTLGF
     DGLKTVCLAS KLPVVAIGGI NASNAGSVME LGLPNLKGVA VVSALFDRPS VVAETRNMKS
     ILTNTSRT
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024