THI22_YEAST
ID THI22_YEAST Reviewed; 572 AA.
AC Q06490; D6W4C0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Thiamine biosynthesis protein THI22;
DE Flags: Precursor;
GN Name=THI22; OrderedLocusNames=YPR121W;
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, AND SEQUENCE REVISION TO 95.
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, 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: Is not required for thiamine biosynthesis.
CC {ECO:0000269|PubMed:10383756}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- INDUCTION: By absence of thiamine. {ECO:0000269|PubMed:10383756}.
CC -!- SIMILARITY: Belongs to the thiaminase-2 family. {ECO:0000305}.
CC -!- CAUTION: Although highly homologous to the 2 other thiaminase-2 family
CC members THI20 and THI21 in yeast, no hydroxymethylpyrimidine phosphate
CC kinase activity could be demonstrated for this protein. {ECO:0000305}.
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DR EMBL; U40828; AAB68062.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11536.2; -; Genomic_DNA.
DR PIR; S69014; S69014.
DR RefSeq; NP_015446.2; NM_001184218.2.
DR AlphaFoldDB; Q06490; -.
DR SMR; Q06490; -.
DR BioGRID; 36290; 102.
DR DIP; DIP-6441N; -.
DR IntAct; Q06490; 8.
DR MINT; Q06490; -.
DR STRING; 4932.YPR121W; -.
DR PaxDb; Q06490; -.
DR PRIDE; Q06490; -.
DR EnsemblFungi; YPR121W_mRNA; YPR121W; YPR121W.
DR GeneID; 856239; -.
DR KEGG; sce:YPR121W; -.
DR SGD; S000006325; THI22.
DR VEuPathDB; FungiDB:YPR121W; -.
DR eggNOG; KOG2598; Eukaryota.
DR GeneTree; ENSGT00940000176386; -.
DR HOGENOM; CLU_020520_2_1_1; -.
DR InParanoid; Q06490; -.
DR OMA; ADCARNE; -.
DR BioCyc; YEAST:G3O-34260-MON; -.
DR PRO; PR:Q06490; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06490; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IBA:GO_Central.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IBA:GO_Central.
DR GO; GO:0050334; F:thiaminase activity; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEP:SGD.
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 2: Evidence at transcript level;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..572
FT /note="Thiamine biosynthesis protein THI22"
FT /id="PRO_0000034064"
FT CONFLICT 95
FT /note="Q -> H (in Ref. 1; AAB68062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 63298 MW; 7822B23A9546823C CRC64;
MVIILLGLCT LGFPRTAFCP SIMTNSTVSI NTPPPYLTLA CNEKLPTVMS IAGSDSSGGA
GVEADIKTIT AHRCYAMTCV TTLTAQTPVK VYGAQNIPKK MVSQILDANL QDMKCNVIKT
GMLTVDAIEV LHEKLLQLGE NRPKLVIDPV LCAASDSSPT GKDVVSLIIE KISPFADILT
PNISDCFMLL GENREVSKLQ DVLEIAKDLS RITNCSNILV KGGHIPCDDG KEKHITDVLY
LGAEQKFITF KGQFVNTTRT HGAGCTLASA IASNLARGYS LSQSVYGGIE YVQNAIAIGC
DVTKKAVKVG PINHVYAVEI PLEKMLTDEC FTASDAVPKK PIEGSLDKIP GGSFFNYLIN
HPKVKPHWDA YVNHEFVKRV ADGTLERKKF QFFIEQDYLY LIDYVRVCCV TGSKSPTLED
LEKDLVIADC ARNELNEHER RLREEFGVKD PDYLQKIKRG PALRAYCRYL IDISRRGNWQ
EIVVALNPCL MGYVYAVDKV KDKITAAEGS IYSEWCDTCA SSFCYQAVLE GERLMNHILE
TYPPDQLDSL VTIFARGCEL ETNFWTAAME YE
