THI80_YEAST
ID THI80_YEAST Reviewed; 319 AA.
AC P35202; D6W2K1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Thiamine pyrophosphokinase {ECO:0000303|PubMed:8394343};
DE Short=TPK {ECO:0000303|PubMed:8394343};
DE Short=Thiamine kinase {ECO:0000303|PubMed:8394343};
DE EC=2.7.6.2 {ECO:0000269|PubMed:8394343};
GN Name=THI80 {ECO:0000303|PubMed:8394343}; OrderedLocusNames=YOR143C;
GN ORFNames=YOR3373C;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION.
RX PubMed=8394343; DOI=10.1016/s0021-9258(19)85354-1;
RA Nosaka K., Kaneko Y., Nishimura H., Iwashima A.;
RT "Isolation and characterization of a thiamin pyrophosphokinase gene, THI80,
RT from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 268:17440-17447(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [3]
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 [4]
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 [5]
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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=11435118; DOI=10.1016/s0969-2126(01)00615-3;
RA Baker L.-J., Dorocke J.A., Harris R.A., Timm D.E.;
RT "The crystal structure of yeast thiamin pyrophosphokinase.";
RL Structure 9:539-546(2001).
CC -!- FUNCTION: Essential protein, it is the only enzyme in yeast capable of
CC synthesizing thiamine pyrophosphate (TPP).
CC {ECO:0000269|PubMed:8394343}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thiamine = AMP + H(+) + thiamine diphosphate;
CC Xref=Rhea:RHEA:11576, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58937, ChEBI:CHEBI:456215; EC=2.7.6.2;
CC Evidence={ECO:0000269|PubMed:8394343};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine diphosphate from thiamine: step 1/1.
CC {ECO:0000269|PubMed:8394343}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11435118}.
CC -!- INDUCTION: Expression requires the positive regulatory factors THI2 and
CC THI3 (PubMed:8394343). Incompletely repressed by exogenous thiamine
CC pyrophosphokinase (PubMed:8394343). {ECO:0000269|PubMed:8394343}.
CC -!- MISCELLANEOUS: Present with 3320 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the thiamine pyrophosphokinase family.
CC {ECO:0000305}.
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DR EMBL; D14417; BAA03312.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64061.1; -; Genomic_DNA.
DR EMBL; Z75051; CAA99346.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10917.1; -; Genomic_DNA.
DR PIR; A47499; A47499.
DR RefSeq; NP_014786.1; NM_001183562.1.
DR PDB; 1IG0; X-ray; 1.80 A; A/B=1-319.
DR PDBsum; 1IG0; -.
DR AlphaFoldDB; P35202; -.
DR SMR; P35202; -.
DR BioGRID; 34540; 154.
DR DIP; DIP-5324N; -.
DR IntAct; P35202; 5.
DR STRING; 4932.YOR143C; -.
DR iPTMnet; P35202; -.
DR MaxQB; P35202; -.
DR PaxDb; P35202; -.
DR PRIDE; P35202; -.
DR EnsemblFungi; YOR143C_mRNA; YOR143C; YOR143C.
DR GeneID; 854314; -.
DR KEGG; sce:YOR143C; -.
DR SGD; S000005669; THI80.
DR VEuPathDB; FungiDB:YOR143C; -.
DR eggNOG; KOG3153; Eukaryota.
DR GeneTree; ENSGT00390000016016; -.
DR HOGENOM; CLU_044237_0_0_1; -.
DR InParanoid; P35202; -.
DR OMA; RPTMRHS; -.
DR BioCyc; MetaCyc:YOR143C-MON; -.
DR BioCyc; YEAST:YOR143C-MON; -.
DR Reactome; R-SCE-196819; Vitamin B1 (thiamin) metabolism.
DR UniPathway; UPA00060; UER00597.
DR EvolutionaryTrace; P35202; -.
DR PRO; PR:P35202; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P35202; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030975; F:thiamine binding; IEA:InterPro.
DR GO; GO:0004788; F:thiamine diphosphokinase activity; IDA:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IMP:SGD.
DR CDD; cd07995; TPK; 1.
DR Gene3D; 3.40.50.10240; -; 1.
DR InterPro; IPR016966; Thiamin_pyrophosphokinase_euk.
DR InterPro; IPR007373; Thiamin_PyroPKinase_B1-bd.
DR InterPro; IPR036371; TPK_B1-bd_sf.
DR InterPro; IPR007371; TPK_catalytic.
DR InterPro; IPR036759; TPK_catalytic_sf.
DR Pfam; PF04265; TPK_B1_binding; 1.
DR Pfam; PF04263; TPK_catalytic; 1.
DR PIRSF; PIRSF031057; Thiamin_pyrophosphokinase; 1.
DR SMART; SM00983; TPK_B1_binding; 1.
DR SUPFAM; SSF63862; SSF63862; 1.
DR SUPFAM; SSF63999; SSF63999; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..319
FT /note="Thiamine pyrophosphokinase"
FT /id="PRO_0000072513"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:1IG0"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1IG0"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 184..195
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 196..212
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 260..278
FT /evidence="ECO:0007829|PDB:1IG0"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 292..302
FT /evidence="ECO:0007829|PDB:1IG0"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:1IG0"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:1IG0"
SQ SEQUENCE 319 AA; 36616 MW; B82609E195D4D53F CRC64;
MSEECIENPE RIKIGTDLIN IRNKMNLKEL IHPNEDENST LLILNQKIDI PRPLFYKIWK
LHDLKVCADG AANRLYDYLD DDETLRIKYL PNYIIGDLDS LSEKVYKYYR KNKVTIIKQT
TQYSTDFTKC VNLISLHFNS PEFRSLISNK DNLQSNHGIE LEKGIHTLYN TMTESLVFSK
VTPISLLALG GIGGRFDQTV HSITQLYTLS ENASYFKLCY MTPTDLIFLI KKNGTLIEYD
PQFRNTCIGN CGLLPIGEAT LVKETRGLKW DVKNWPTSVV TGRVSSSNRF VGDNCCFIDT
KDDIILNVEI FVDKLIDFL
