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THIE_NOSS1
ID   THIE_NOSS1              Reviewed;         351 AA.
AC   Q8YX72;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Thiamine-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01327};
DE            Short=TP synthase {ECO:0000255|HAMAP-Rule:MF_01327};
DE            Short=TPS {ECO:0000255|HAMAP-Rule:MF_01327};
DE            EC=2.5.1.3 {ECO:0000255|HAMAP-Rule:MF_01327};
DE   AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01327};
DE            Short=TMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01327};
DE            Short=TMP-PPase {ECO:0000255|HAMAP-Rule:MF_01327};
GN   Name=thiE {ECO:0000255|HAMAP-Rule:MF_01327}; OrderedLocusNames=alr1343;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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_01327}.
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_01327};
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_01327};
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_01327};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01327};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01327};
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_01327}.
CC   -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01327}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB73300.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000019; BAB73300.1; ALT_INIT; Genomic_DNA.
DR   PIR; AD1974; AD1974.
DR   AlphaFoldDB; Q8YX72; -.
DR   SMR; Q8YX72; -.
DR   STRING; 103690.17130690; -.
DR   EnsemblBacteria; BAB73300; BAB73300; BAB73300.
DR   KEGG; ana:alr1343; -.
DR   eggNOG; COG0352; Bacteria.
DR   OMA; EEWCRFG; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000002483; Chromosome.
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   HAMAP; MF_01327; TMP_synthase_cyanobact; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036206; ThiamineP_synth_sf.
DR   InterPro; IPR022998; ThiamineP_synth_TenI.
DR   InterPro; IPR041397; ThiD2.
DR   InterPro; IPR034291; TMP_synthase.
DR   InterPro; IPR016229; TMP_synthase_cyanobac_bac.
DR   Pfam; PF17792; ThiD2; 1.
DR   Pfam; PF02581; TMP-TENI; 1.
DR   PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1.
DR   SUPFAM; SSF51391; SSF51391; 1.
DR   TIGRFAMs; TIGR00693; thiE; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Reference proteome; Thiamine biosynthesis;
KW   Transferase.
FT   CHAIN           1..351
FT                   /note="Thiamine-phosphate synthase"
FT                   /id="PRO_0000157078"
FT   REGION          1..129
FT                   /note="Unknown"
FT   REGION          130..351
FT                   /note="Thiamine-phosphate synthase"
FT   BINDING         177..181
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT   BINDING         209
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT   BINDING         210
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT   BINDING         229
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT   BINDING         248
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT   BINDING         274..276
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_01327"
FT   BINDING         277
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT   BINDING         304
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_01327"
SQ   SEQUENCE   351 AA;  39251 MW;  8F2A372F5F947546 CRC64;
     MVEPYSQQKQ IQQVVYRILD ANLDRAREGL RIIEEWCRFG LNSGQLAGEC KYLRQEVAVW
     HTEELRAARD TAGDPGTDLS HPQEEQRSSI KALLQANFCR VEEALRVLEE YGKLYHPKMG
     QACKQMRYRV YSLETNLMGH QRHQLLRRSR LYLVTSPSES LLPTVEAALK GGLTLLQYRD
     KDTDDFVRLE LATKLRQLCH SYGALFIIND RVDLALAVDA DGVHLGQQDM PIATARQLLG
     PQRLIGRSTT NADEMQKAIA EGADYIGVGP VYETPTKIGK AAAGLGYVSY AAQHSSVPWF
     AIGGIDANNI NDVIDAGAER VAVVRSLMQA EQPTLVTQYL ISQLNRIKPE S
 
 
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