TNR3_SCHPO
ID TNR3_SCHPO Reviewed; 569 AA.
AC P41888;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Thiamine pyrophosphokinase;
DE Short=TPK;
DE Short=Thiamine kinase;
DE EC=2.7.6.2 {ECO:0000269|PubMed:7499352};
GN Name=tnr3; ORFNames=SPAC6F12.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=972 / ATCC 24843;
RX PubMed=7499352; DOI=10.1074/jbc.270.47.28457;
RA Fankhauser H., Zurlinden A., Schweingruber A.-M., Edenharter E.,
RA Schweingruber M.E.;
RT "Schizosaccharomyces pombe thiamine pyrophosphokinase is encoded by gene
RT tnr3 and is a regulator of thiamine metabolism, phosphate metabolism,
RT mating, and growth.";
RL J. Biol. Chem. 270:28457-28462(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION.
RX PubMed=1551569; DOI=10.1093/genetics/130.3.445;
RA Schweingruber A.-M., Fankhauser H., Dlugonski J., Steinmann-Loss C.,
RA Schweingruber M.E.;
RT "Isolation and characterization of regulatory mutants from
RT Schizosaccharomyces pombe involved in thiamine-regulated gene expression.";
RL Genetics 130:445-449(1992).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Involved in the regulation of thiamine metabolism, phosphate
CC metabolism, mating and cell growth. {ECO:0000269|PubMed:1551569,
CC ECO:0000269|PubMed:7499352}.
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:7499352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11577;
CC Evidence={ECO:0000269|PubMed:7499352};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 uM for thiamine {ECO:0000269|PubMed:7499352};
CC KM=1.9 mM for ATP {ECO:0000269|PubMed:7499352};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:7499352};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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DR EMBL; X84417; CAA59135.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11089.1; -; Genomic_DNA.
DR PIR; S52350; S52350.
DR RefSeq; NP_593291.1; NM_001018721.2.
DR AlphaFoldDB; P41888; -.
DR SMR; P41888; -.
DR BioGRID; 279468; 17.
DR STRING; 4896.SPAC6F12.05c.1; -.
DR iPTMnet; P41888; -.
DR MaxQB; P41888; -.
DR PaxDb; P41888; -.
DR PRIDE; P41888; -.
DR EnsemblFungi; SPAC6F12.05c.1; SPAC6F12.05c.1:pep; SPAC6F12.05c.
DR GeneID; 2543032; -.
DR KEGG; spo:SPAC6F12.05c; -.
DR PomBase; SPAC6F12.05c; tnr3.
DR VEuPathDB; FungiDB:SPAC6F12.05c; -.
DR eggNOG; KOG3153; Eukaryota.
DR eggNOG; KOG4313; Eukaryota.
DR HOGENOM; CLU_479095_0_0_1; -.
DR InParanoid; P41888; -.
DR OMA; PELQYVF; -.
DR PhylomeDB; P41888; -.
DR BRENDA; 2.7.6.2; 5613.
DR PRO; PR:P41888; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0044715; F:8-oxo-dGDP phosphatase activity; IDA:PomBase.
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:PomBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IMP:PomBase.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006772; P:thiamine metabolic process; IMP:PomBase.
DR GO; GO:0036172; P:thiamine salvage; EXP:PomBase.
DR CDD; cd07995; TPK; 1.
DR Gene3D; 3.40.50.10240; -; 1.
DR InterPro; IPR031804; DUF4743.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR006282; Thi_PPkinase.
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; PF15916; DUF4743; 1.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF04265; TPK_B1_binding; 1.
DR Pfam; PF04263; TPK_catalytic; 1.
DR SMART; SM00983; TPK_B1_binding; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR SUPFAM; SSF63862; SSF63862; 1.
DR SUPFAM; SSF63999; SSF63999; 1.
DR TIGRFAMs; TIGR01378; thi_PPkinase; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..569
FT /note="Thiamine pyrophosphokinase"
FT /id="PRO_0000072610"
FT DOMAIN 136..276
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
SQ SEQUENCE 569 AA; 64236 MW; 5118042478DF00FC CRC64;
MAMSSITSAK QLNAEELLDE CDSFNGEFVP GTIPFRANGA AIGYVTPLVL EILIKADNFK
FNWVYVPGEY IEINASTFEK RTDILAKVLE HWRHNNTFGI ADQWRNELYT VYGKSKKPVL
AVERGGFWLF GFLSTGVHCT MYIPATKEHP LRIWVPRRSP TKQTWPNYLD NSVAGGIAHG
DSVIGTMIKE FSEEANLDVS SMNLIPCGTV SYIKMEKRHW IQPELQYVFD LPVDDLVIPR
INDGEVAGFS LLPLNQVLHE LELKSFKPNC ALVLLDFLIR HGIITPQHPQ YLQTLERIHR
PLPVPVGKYE RGDSFEDTSK KAETCVPAKP QKATHQLAPC KAWLRDYDTD QKFAVLLLNQ
PIDIPDDRFR TLWKRASIRV CADGGANQLR NYDSSLKPDY VVGDFDSLTD ETKAYYKEMG
VNIVFDPCQN TTDFMKCHKI IKEHGIDTIF VLCGMGGRVD HAIGNLNHLF WAASISEKNE
VFLLTELNVS TLLQPGINHV DCHDNIGLHC GLLPVGQSVY VKKTSGLEWN IEDRICQFGG
LVSSCNVVTK ATVTIEVNNF IVWTMETRL
