THI11_YEAST
ID THI11_YEAST Reviewed; 340 AA.
AC P47183; D6VWX5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI11 {ECO:0000250|UniProtKB:P43534};
DE Short=HMP-P synthase {ECO:0000250|UniProtKB:P43534};
DE Short=Hydroxymethylpyrimidine phosphate synthase {ECO:0000250|UniProtKB:P43534};
DE EC=2.-.-.- {ECO:0000250|UniProtKB:P43534};
DE AltName: Full=Thiamine biosynthesis protein 11 {ECO:0000303|PubMed:12777485};
DE AltName: Full=Thiamine pyrimidine synthase {ECO:0000250|UniProtKB:C4YMW2};
GN Name=THI11 {ECO:0000303|PubMed:12777485};
GN OrderedLocusNames=YJR156C {ECO:0000312|SGD:S000003917}; ORFNames=J2250;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PATHWAY.
RX PubMed=12777485; DOI=10.1099/mic.0.26194-0;
RA Wightman R., Meacock P.A.;
RT "The THI5 gene family of Saccharomyces cerevisiae: distribution of
RT homologues among the hemiascomycetes and functional redundancy in the
RT aerobic biosynthesis of thiamin from pyridoxine.";
RL Microbiology 149:1447-1460(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Responsible for the formation of the pyrimidine heterocycle
CC in the thiamine biosynthesis pathway. Catalyzes the formation of
CC hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal
CC phosphate (PLP). The protein uses PLP and the active site histidine to
CC form HMP-P, generating an inactive enzyme. The enzyme can only undergo
CC a single turnover, which suggests it is a suicide enzyme.
CC {ECO:0000250|UniProtKB:P43534}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(3+) + 4 H2O + L-histidyl-[4-amino-5-hydroxymethyl-2-
CC methylpyrimidine phosphate synthase] + N(6)-(pyridoxal phosphate)-L-
CC lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase]
CC = (2S)-2-amino-5-hydroxy-4-oxopentanoyl-[4-amino-5-hydroxymethyl-2-
CC methylpyrimidine phosphate synthase] + 3-oxopropanoate + 4-amino-2-
CC methyl-5-(phosphooxymethyl)pyrimidine + 2 Fe(2+) + 2 H(+) + L-lysyl-
CC [4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase];
CC Xref=Rhea:RHEA:65756, Rhea:RHEA-COMP:16892, Rhea:RHEA-COMP:16893,
CC Rhea:RHEA-COMP:16894, Rhea:RHEA-COMP:16895, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:29979, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:58354, ChEBI:CHEBI:143915, ChEBI:CHEBI:157692;
CC Evidence={ECO:0000250|UniProtKB:P43534};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65757;
CC Evidence={ECO:0000250|UniProtKB:P43534};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:P43534};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000305|PubMed:12777485}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P43534}.
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NMT1/THI5 family. {ECO:0000305}.
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DR EMBL; Z49656; CAA89689.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08941.1; -; Genomic_DNA.
DR RefSeq; NP_012690.3; NM_001181814.3.
DR AlphaFoldDB; P47183; -.
DR SMR; P47183; -.
DR BioGRID; 33911; 30.
DR IntAct; P47183; 2.
DR MINT; P47183; -.
DR STRING; 4932.YJR156C; -.
DR PaxDb; P47183; -.
DR PRIDE; P47183; -.
DR EnsemblFungi; YJR156C_mRNA; YJR156C; YJR156C.
DR GeneID; 853621; -.
DR KEGG; sce:YJR156C; -.
DR SGD; S000003917; THI11.
DR VEuPathDB; FungiDB:YJR156C; -.
DR eggNOG; ENOG502QQ87; Eukaryota.
DR GeneTree; ENSGT00940000176330; -.
DR HOGENOM; CLU_028871_6_3_1; -.
DR InParanoid; P47183; -.
DR OMA; DASRVMW; -.
DR BioCyc; YEAST:MON3O-9135; -.
DR UniPathway; UPA00060; -.
DR PRO; PR:P47183; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47183; protein.
DR GO; GO:0106344; F:4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IGI:SGD.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR027939; NMT1/THI5.
DR InterPro; IPR015168; SsuA/THI5.
DR PANTHER; PTHR31528; PTHR31528; 1.
DR Pfam; PF09084; NMT1; 1.
PE 1: Evidence at protein level;
KW Iron; Metal-binding; Pyridoxal phosphate; Reference proteome;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..340
FT /note="4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate
FT synthase THI11"
FT /id="PRO_0000211619"
FT MOTIF 195..199
FT /note="CCCFC; essential for catalytic activity, may be the
FT site of iron coordination"
FT /evidence="ECO:0000250|UniProtKB:P43534"
FT ACT_SITE 66
FT /evidence="ECO:0000250|UniProtKB:P43534"
FT BINDING 115..118
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P43534"
FT MOD_RES 62
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43534"
SQ SEQUENCE 340 AA; 38632 MW; 1BA0A2D2A6D112D7 CRC64;
MSTDKITFLL NWQPTPYHIP IFLAQTKGYF KEQGLDIAIL EPTNPSDVTE LIGSGKVDMG
LKAMIHTLAA KARGFPVTSV ASLLDEPFTG VLYLKGSGIT EDFQSLKGKK IGYVGEFGKI
QIDELTKHYG MKPEDYTAVR CGMNVAKYII EDKIDAGIGI ECMQQVELEE YLAKQGRPAS
DAKMLRIDKL ACLGCCCFCT VLYICNDEFL KKNPEKVRKF LKAIKKATDY VLADPVKAWK
EYIDFKPQLN NDLSYKQYQR CYAYFSSSLY NVHRDWKKVT GYGKRLAILP PDYVSNYTNE
YLSWPEPEEV SDPLEAQRLM AIHQEKCRQE GTFKRLALPA
