(data stored in ACNUC1104 zone)

SWISSPROT: THIE_SACEN

ID   THIE_SACEN              Reviewed;         223 AA.
AC   A4F727;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 71.
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=SACE_0505;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(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}.
DR   EMBL; AM420293; CAL99851.1; -; Genomic_DNA.
DR   RefSeq; WP_009950944.1; NZ_PDBV01000001.1.
DR   SMR; A4F727; -.
DR   STRING; 405948.SACE_0505; -.
DR   EnsemblBacteria; CAL99851; CAL99851; SACE_0505.
DR   KEGG; sen:SACE_0505; -.
DR   eggNOG; ENOG4107Y5I; Bacteria.
DR   eggNOG; COG0352; LUCA.
DR   HOGENOM; HOG000155781; -.
DR   KO; K00788; -.
DR   OMA; ITAFQFR; -.
DR   OrthoDB; 1558094at2; -.
DR   BioCyc; SERY405948:SACE_RS02480-MONOMER; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000006728; 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; A4F727.
DR   SWISS-2DPAGE; A4F727.
KW   Magnesium; Metal-binding; Reference proteome; Thiamine biosynthesis;
KW   Transferase.
FT   CHAIN           1..223
FT                   /note="Thiamine-phosphate synthase"
FT                   /id="PRO_1000008167"
FT   REGION          47..51
FT                   /note="HMP-PP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   REGION          150..152
FT                   /note="THZ-P binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   METAL           85
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   METAL           104
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         84
FT                   /note="HMP-PP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         123
FT                   /note="HMP-PP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         153
FT                   /note="HMP-PP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         182
FT                   /note="THZ-P; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
SQ   SEQUENCE   223 AA;  23581 MW;  AF55067072FB1440 CRC64;
     MPGLDGFGIR ARLEEALLYL CTDARTERGD LAEFADAALD GGVDIIQLRD KSAGGAPLEA
     RHELAALEVL AEACVRHGAL LAVNDRADVA MAADADVLHL GQDDLPVELA RRIVGDQVVV
     GRSTHDVVQA DSAATEQGVD YFCTGPVWTT PTKPGREAAG LELVRHTAEH RGHGRPWFAI
     GGIGMDNIDE VVQAGARRVV VVRAITEAED PRAAAAALRT KLG
//

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