THI21_YEAST
ID THI21_YEAST Reviewed; 551 AA.
AC Q08975; D6W3B1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI21;
DE EC=2.7.1.49 {ECO:0000305};
DE EC=2.7.4.7 {ECO:0000305};
DE AltName: Full=Hydroxymethylpyrimidine kinase;
DE Short=HMP kinase;
DE AltName: Full=Hydroxymethylpyrimidine phosphate kinase;
DE Short=HMP-P kinase;
DE Short=HMP-phosphate kinase;
DE Short=HMPP kinase;
GN Name=THI21; OrderedLocusNames=YPL258C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 FUNCTION AS A HMPP KINASE, AND INDUCTION.
RX PubMed=10383756; DOI=10.1046/j.1365-2958.1999.01412.x;
RA Llorente B., Fairhead C., Dujon B.;
RT "Genetic redundancy and gene fusion in the genome of the Baker's yeast
RT Saccharomyces cerevisiae: functional characterization of a three-member
RT gene family involved in the thiamine biosynthetic pathway.";
RL Mol. Microbiol. 32:1140-1152(1999).
CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine
CC phosphate (HMP-P) to HMP-PP, and also probably that of HMP to HMP-P.
CC {ECO:0000269|PubMed:10383756}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC EC=2.7.1.49; Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-
CC amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP;
CC Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole: step 2/3.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole: step 3/3.
CC -!- INTERACTION:
CC Q08975; P39940: RSP5; NbExp=3; IntAct=EBI-30327, EBI-16219;
CC -!- INDUCTION: By absence of thiamine. {ECO:0000269|PubMed:10383756}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ThiD family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the thiaminase-2
CC family. {ECO:0000305}.
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DR EMBL; Z73614; CAA97986.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11177.1; -; Genomic_DNA.
DR PIR; S65289; S65289.
DR RefSeq; NP_015065.1; NM_001184072.1.
DR AlphaFoldDB; Q08975; -.
DR SMR; Q08975; -.
DR BioGRID; 35954; 54.
DR DIP; DIP-5635N; -.
DR IntAct; Q08975; 41.
DR MINT; Q08975; -.
DR STRING; 4932.YPL258C; -.
DR PaxDb; Q08975; -.
DR PRIDE; Q08975; -.
DR EnsemblFungi; YPL258C_mRNA; YPL258C; YPL258C.
DR GeneID; 855870; -.
DR KEGG; sce:YPL258C; -.
DR SGD; S000006179; THI21.
DR VEuPathDB; FungiDB:YPL258C; -.
DR eggNOG; KOG2598; Eukaryota.
DR GeneTree; ENSGT00940000176386; -.
DR HOGENOM; CLU_020520_2_1_1; -.
DR InParanoid; Q08975; -.
DR OMA; CELEANF; -.
DR BioCyc; MetaCyc:MON3O-81; -.
DR BioCyc; YEAST:MON3O-81; -.
DR UniPathway; UPA00060; UER00137.
DR UniPathway; UPA00060; UER00138.
DR PRO; PR:Q08975; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08975; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IDA:SGD.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IDA:SGD.
DR GO; GO:0050334; F:thiaminase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; 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 CDD; cd01169; HMPP_kinase; 1.
DR Gene3D; 1.20.910.10; -; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR045029; HMP/HMP-P_kinase.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
DR InterPro; IPR027574; Thiaminase_II.
DR PANTHER; PTHR20858; PTHR20858; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR Pfam; PF03070; TENA_THI-4; 1.
DR SUPFAM; SSF48613; SSF48613; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1.
DR TIGRFAMs; TIGR04306; salvage_TenA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..551
FT /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine
FT kinase THI21"
FT /id="PRO_0000192042"
FT BINDING 64
FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"
FT /ligand_id="ChEBI:CHEBI:16892"
FT /evidence="ECO:0000250"
SQ SEQUENCE 551 AA; 61334 MW; B8FD8D7DF6A25961 CRC64;
MTYSTVNINT PPPYLALASN EKLPTVLSIA GTDPSGGAGV EADVKTITAH RCYAMTCITA
LNAQTPVKVY SINNTPKEVV SQILDANLQD MKCDVIKTGM LTTAAIEVLH EKLLQLGENR
PKLVVDPVLV ATSGSSLAGK DIASLITEKI APFADILTPN IPECFKLLGE DREISKLRDI
FEVAKDLAKI TKCSNILVKG GHIPWNDEEG KYITDVLYLG AEQRFITFKG NFVNTTHTHG
TGCTLASAIA SNLARGYSLP QSVYGGIEYV QNAVAIGCDV TKETVKDNGP INHVYAIEIP
LEKMLSDECF TASDAVHKKP VKSSLNKIPG GSFYKYLINH PKVKPHWDSY VNHDFVRKVA
DGSLEPKKFQ FFIEQDYLYL VNYARISCIA GSKSPCLEDL EKELVIVECV RNGLCQHERR
LREEFGIKDP DYLQKIQRGP ALRAYCRYFN DVSRRGNWQE LVIALNPCLM GYVHALTKIK
DEVTAAEGSV YREWCETYSS SWCHEAMLEG EKLLNHILET YPPEKLDTLV TIYAEVCELE
ANFWTAALEY E
