(data stored in ACNUC7421 zone)

SWISSPROT: THIE_ALCBS

ID   THIE_ALCBS              Reviewed;         217 AA.
AC   Q0VSP5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   11-DEC-2019, 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=ABO_0355;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAL15803.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AM286690; CAL15803.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041704752.1; NC_008260.1.
DR   SMR; Q0VSP5; -.
DR   STRING; 393595.ABO_0355; -.
DR   EnsemblBacteria; CAL15803; CAL15803; ABO_0355.
DR   KEGG; abo:ABO_0355; -.
DR   eggNOG; ENOG4108UV6; Bacteria.
DR   eggNOG; COG0352; LUCA.
DR   HOGENOM; HOG000155781; -.
DR   KO; K00788; -.
DR   OrthoDB; 1558094at2; -.
DR   BioCyc; ABOR393595:ABO_RS01810-MONOMER; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000008871; 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   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;
DR   PRODOM; Q0VSP5.
DR   SWISS-2DPAGE; Q0VSP5.
KW   Magnesium; Metal-binding; Reference proteome; Thiamine biosynthesis;
KW   Transferase.
FT   CHAIN           1..217
FT                   /note="Thiamine-phosphate synthase"
FT                   /id="PRO_0000336369"
FT   REGION          39..43
FT                   /note="HMP-PP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   REGION          137..139
FT                   /note="THZ-P binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   METAL           72
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   METAL           91
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         71
FT                   /note="HMP-PP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         110
FT                   /note="HMP-PP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         140
FT                   /note="HMP-PP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         167
FT                   /note="THZ-P; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
SQ   SEQUENCE   217 AA;  22906 MW;  948E8089D223AD50 CRC64;
     MPLHRLHGLY AITDPALTPD EHLLPAAEAA LRGGAKLLQY RDKTASPTQR EYRAAQLRQL
     CHQYHALFIV NDDPALAAQV NADGVHIGQS DGGIKAARDQ LGGSRIIGVT CHGDLTLAAR
     AAEAGADYLA MGRFFTSHTK PLAPPASLAL LRQACQQFHQ PVVAIGGVNP DNAPQLINAG
     AVSVAVIHAL FGQTDTDAIE AAARQLSACF QTNRSAP
//

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