(data stored in ACNUC7421 zone)

SWISSPROT: C5BHE5_EDWI9

ID   C5BHE5_EDWI9            Unreviewed;       214 AA.
AC   C5BHE5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 66.
DE   RecName: Full=Thiamine-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TP synthase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TPS {ECO:0000256|HAMAP-Rule:MF_00097};
DE            EC=2.5.1.3 {ECO:0000256|HAMAP-Rule:MF_00097};
DE   AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TMP pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TMP-PPase {ECO:0000256|HAMAP-Rule:MF_00097};
GN   Name=thiE {ECO:0000256|HAMAP-Rule:MF_00097};
GN   OrderedLocusNames=NT01EI_0176 {ECO:0000313|EMBL:ACR67423.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67423.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole
CC       monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl
CC       pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate
CC       (TMP). {ECO:0000256|HAMAP-Rule:MF_00097,
CC       ECO:0000256|SAAS:SAAS00709677}.
CC   -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine +
CC       2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate
CC       = diphosphate + thiamine phosphate + CO(2). {ECO:0000256|HAMAP-
CC       Rule:MF_00097, ECO:0000256|RuleBase:RU003826,
CC       ECO:0000256|SAAS:SAAS00709728}.
CC   -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine +
CC       2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = diphosphate +
CC       thiamine phosphate + CO(2). {ECO:0000256|HAMAP-Rule:MF_00097,
CC       ECO:0000256|RuleBase:RU003826, ECO:0000256|SAAS:SAAS00709678}.
CC   -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine +
CC       4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00097,
CC       ECO:0000256|RuleBase:RU003826, ECO:0000256|SAAS:SAAS00709726}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00097};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00097};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC       thiamine phosphate from 4-amino-2-methyl-5-
CC       diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-
CC       thiazole: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00097,
CC       ECO:0000256|RuleBase:RU004253, ECO:0000256|SAAS:SAAS00709682}.
CC   -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00097, ECO:0000256|RuleBase:RU003826}.
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DR   EMBL; CP001600; ACR67423.1; -; Genomic_DNA.
DR   RefSeq; WP_015869635.1; NC_012779.2.
DR   ProteinModelPortal; C5BHE5; -.
DR   STRING; 634503.NT01EI_0176; -.
DR   EnsemblBacteria; ACR67423; ACR67423; NT01EI_0176.
DR   GeneID; 7958768; -.
DR   KEGG; eic:NT01EI_0176; -.
DR   PATRIC; fig|634503.3.peg.159; -.
DR   eggNOG; ENOG4108UV6; Bacteria.
DR   eggNOG; COG0352; LUCA.
DR   HOGENOM; HOG000155781; -.
DR   KO; K00788; -.
DR   OMA; ITAFQFR; -.
DR   OrthoDB; POG091H01SL; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP.
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; 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;
DR   PRODOM; C5BHE5.
DR   SWISS-2DPAGE; C5BHE5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00097,
KW   ECO:0000256|SAAS:SAAS00709725};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00097,
KW   ECO:0000256|SAAS:SAAS00709674};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00097,
KW   ECO:0000256|RuleBase:RU003826, ECO:0000256|SAAS:SAAS00709833};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00097,
KW   ECO:0000256|RuleBase:RU003826, ECO:0000256|SAAS:SAAS00709679,
KW   ECO:0000313|EMBL:ACR67423.1}.
FT   DOMAIN       20    189       TMP-TENI. {ECO:0000259|Pfam:PF02581}.
FT   REGION       37     41       HMP-PP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   REGION      134    136       THZ-P binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   REGION      186    187       THZ-P binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   METAL        70     70       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   METAL        89     89       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING      69     69       HMP-PP. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     108    108       HMP-PP. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     137    137       HMP-PP. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     166    166       THZ-P; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00097}.
SQ   SEQUENCE   214 AA;  23465 MW;  D3A7AE9EA1D75AE6 CRC64;
     MAQPVFAPVP MRLGLYPIVD SVEWIERLLR AGVRTLQLRI KDCREDQIGD EIAQAIALGR
     HYQARLFIND YWRPAIRLGA YGVHLGQEDL DQADLAAIRR AGLRLGLSTH DDAEMDRALA
     EGPSYVALGH VFPTDSKLMD TAPQGLSDLR RQMTRLDTYP SVAIGGISIA RVPDVLACGV
     GSIALVSAIT RAPDWLAATD TLLQLIEGRR ANDV
//

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