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THIE_STRS2
ID   THIE_STRS2              Reviewed;         229 AA.
AC   A4W0K4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Thiamine-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00097};
DE            Short=TP synthase {ECO:0000255|HAMAP-Rule:MF_00097};
DE            Short=TPS {ECO:0000255|HAMAP-Rule:MF_00097};
DE            EC=2.5.1.3 {ECO:0000255|HAMAP-Rule:MF_00097};
DE   AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00097};
DE            Short=TMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00097};
DE            Short=TMP-PPase {ECO:0000255|HAMAP-Rule:MF_00097};
GN   Name=thiE {ECO:0000255|HAMAP-Rule:MF_00097}; OrderedLocusNames=SSU98_0735;
OS   Streptococcus suis (strain 98HAH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391296;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98HAH33;
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA   Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA   Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA   Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT   of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(2007).
CC   -!- FUNCTION: 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:0000255|HAMAP-Rule:MF_00097}.
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:0000255|HAMAP-Rule:MF_00097};
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:0000255|HAMAP-Rule:MF_00097};
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00097};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00097};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00097};
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00097}.
CC   -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00097}.
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DR   EMBL; CP000408; ABP91893.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4W0K4; -.
DR   SMR; A4W0K4; -.
DR   KEGG; ssv:SSU98_0735; -.
DR   HOGENOM; CLU_018272_3_2_9; -.
DR   OMA; ITAFQFR; -.
DR   UniPathway; UPA00060; UER00141.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00564; TMP_TenI; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00097; TMP_synthase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036206; ThiamineP_synth_sf.
DR   InterPro; IPR022998; ThiamineP_synth_TenI.
DR   InterPro; IPR034291; TMP_synthase.
DR   Pfam; PF02581; TMP-TENI; 1.
DR   SUPFAM; SSF51391; SSF51391; 1.
DR   TIGRFAMs; TIGR00693; thiE; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Thiamine biosynthesis; Transferase.
FT   CHAIN           1..229
FT                   /note="Thiamine-phosphate synthase"
FT                   /id="PRO_0000336430"
FT   BINDING         38..42
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         73
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         74
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         93
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         111
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         137..139
FT                   /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT                   ylidene]ethyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:62899"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         140
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         169
FT                   /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT                   ylidene]ethyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:62899"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         189..190
FT                   /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT                   ylidene]ethyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:62899"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
SQ   SEQUENCE   229 AA;  24866 MW;  13EC09C5B3734B31 CRC64;
     MNRKMLQVYF ICGTSDCPKG KFLDVLEKAL QAGITCFQFR EKGEQGLTGA DKLLLAKQVQ
     HLCHRYQVPL IINDDVELAR AIDADGIHLG QEDLSVVEAR QLFPGKIIGL SVGTKEEYLN
     SPIDLVDYIG SGPVFPTLSK DDASPAIGMD GLKQLRKLNS DIPMVAIGGL SAKDCKEVLQ
     AGADGIAVIS AISHAEDPYK ATKILVDGMQ AMILKFNQVE SNKQILKNP
 
 
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