THI20_YEAST
ID THI20_YEAST Reviewed; 551 AA.
AC Q08224; D6W212; Q05664; Q6B2F0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20;
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=THI20; OrderedLocusNames=YOL055C; ORFNames=O1239;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8789261;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<67::aid-yea884>3.0.co;2-f;
RA Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.;
RT "Analysis of a 26 kb region on the left arm of yeast chromosome XV.";
RL Yeast 12:67-76(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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).
RN [6]
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: 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 -!- INDUCTION: By absence of thiamine. {ECO:0000269|PubMed:10383756}.
CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA62531.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X91067; CAA62531.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z74797; CAA99063.1; -; Genomic_DNA.
DR EMBL; AY692780; AAT92799.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10728.1; -; Genomic_DNA.
DR PIR; S66740; S66740.
DR RefSeq; NP_014586.1; NM_001183310.1.
DR PDB; 3RM5; X-ray; 2.68 A; A/B=2-551.
DR PDBsum; 3RM5; -.
DR AlphaFoldDB; Q08224; -.
DR SMR; Q08224; -.
DR BioGRID; 34346; 81.
DR DIP; DIP-8852N; -.
DR IntAct; Q08224; 94.
DR STRING; 4932.YOL055C; -.
DR MaxQB; Q08224; -.
DR PaxDb; Q08224; -.
DR PRIDE; Q08224; -.
DR EnsemblFungi; YOL055C_mRNA; YOL055C; YOL055C.
DR GeneID; 854099; -.
DR KEGG; sce:YOL055C; -.
DR SGD; S000005416; THI20.
DR VEuPathDB; FungiDB:YOL055C; -.
DR eggNOG; KOG2598; Eukaryota.
DR GeneTree; ENSGT00940000176386; -.
DR HOGENOM; CLU_020520_2_1_1; -.
DR InParanoid; Q08224; -.
DR OMA; FWEMFPY; -.
DR BioCyc; MetaCyc:MON3O-77; -.
DR BioCyc; YEAST:MON3O-77; -.
DR BRENDA; 2.7.1.49; 984.
DR BRENDA; 2.7.4.7; 984.
DR BRENDA; 3.5.99.2; 984.
DR UniPathway; UPA00060; UER00137.
DR UniPathway; UPA00060; UER00138.
DR PRO; PR:Q08224; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08224; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IMP:SGD.
DR GO; GO:0009230; P:thiamine catabolic process; IDA: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 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..551
FT /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine
FT kinase THI20"
FT /id="PRO_0000192041"
FT BINDING 64
FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"
FT /ligand_id="ChEBI:CHEBI:16892"
FT /evidence="ECO:0000250"
FT CONFLICT 323
FT /note="S -> G (in Ref. 4; AAT92799)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:3RM5"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:3RM5"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:3RM5"
FT STRAND 53..64
FT /evidence="ECO:0007829|PDB:3RM5"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:3RM5"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3RM5"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:3RM5"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:3RM5"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:3RM5"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:3RM5"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:3RM5"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 241..254
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 259..276
FT /evidence="ECO:0007829|PDB:3RM5"
FT TURN 293..296
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 300..305
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 333..339
FT /evidence="ECO:0007829|PDB:3RM5"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 344..351
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 366..393
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 397..423
FT /evidence="ECO:0007829|PDB:3RM5"
FT TURN 430..434
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 440..455
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 458..477
FT /evidence="ECO:0007829|PDB:3RM5"
FT TURN 478..481
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 490..497
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 501..518
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 523..525
FT /evidence="ECO:0007829|PDB:3RM5"
FT HELIX 526..548
FT /evidence="ECO:0007829|PDB:3RM5"
SQ SEQUENCE 551 AA; 61269 MW; D57D1C6B693EE401 CRC64;
MTYSTVSINT PPPYLTLACN EKLPTVLSIA GTDPSGGAGI EADVKTITAH RCYAMTCITA
LNAQTPVKVY SINNTPKEVV FQTLESNLKD MKCNVIKTGM LTAAAIEVLH EKLLQLGENR
PKLVVDPVLV ATSGSSLAGK DIVSLITEKV APFADILTPN IPECYKLLGE ERKVNGLQDI
FQIAKDLAKI TKCSNILVKG GHIPWNDEKE KYITDVLFLG AEQKFIIFKG NFVNTTHTHG
TGCTLASAIA SNLARGYSLP QSVYGGIEYV QNAVAIGCDV TKETVKDNGP INHVYAVEIP
LEKMLSDECF TASDVIPKKP LKSAADKIPG GNFYEYLINH PKVKPHWDSY INHEFVKKVA
DGTLERKKFQ FFIEQDYAYL VDYARVHCIA GSKAPCLEDM EKELVIVGGV RTEMGQHEKR
LKEVFGVKDP DYFQKIKRGP ALRAYSRYFN DVSRRGNWQE LVASLTPCLM GYGEALTKMK
GKVTAPEGSV YHEWCETYAS SWYREAMDEG EKLLNHILET YPPEQLDTLV TIYAEVCELE
TNFWTAALEY E
