NTPPA_YEAST
ID NTPPA_YEAST Reviewed; 232 AA.
AC Q99210; D6W2H0;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=dTTP/UTP pyrophosphatase {ECO:0000305};
DE Short=dTTPase/UTPase {ECO:0000305};
DE EC=3.6.1.9 {ECO:0000269|PubMed:24210219};
DE AltName: Full=Maf-like protein YOR111W;
DE AltName: Full=Nucleoside triphosphate pyrophosphatase {ECO:0000303|PubMed:24210219};
DE AltName: Full=Nucleotide pyrophosphatase {ECO:0000303|PubMed:24210219};
DE Short=Nucleotide PPase {ECO:0000305};
GN OrderedLocusNames=YOR111W; ORFNames=O3237, YOR3237W;
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 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
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 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 [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).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVE SITE, AND MUTAGENESIS OF SER-25; THR-26; ARG-29; ARG-30; TYR-66;
RP LYS-74; GLN-76; ASN-77; ASP-103; THR-104; GLU-115; LYS-116; GLU-188;
RP PHE-193; LYS-194 AND GLN-196.
RX PubMed=24210219; DOI=10.1016/j.chembiol.2013.09.011;
RA Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X.,
RA Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N.,
RA Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G.,
RA Yakunin A.F.;
RT "Biochemical and structural studies of conserved Maf proteins revealed
RT nucleotide pyrophosphatases with a preference for modified nucleotides.";
RL Chem. Biol. 20:1386-1398(2013).
CC -!- FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP
CC and UTP. Can also hydrolyze the modified nucleotides 5-methyl-UTP
CC (m(5)UTP) and pseudo-UTP. Has weak activity with CTP (PubMed:24210219).
CC May have a dual role in cell division arrest and in preventing the
CC incorporation of modified nucleotides into cellular nucleic acids
CC (PubMed:24210219). {ECO:0000269|PubMed:24210219}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTTP + H2O = diphosphate + dTMP + H(+); Xref=Rhea:RHEA:28534,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; EC=3.6.1.9;
CC Evidence={ECO:0000269|PubMed:24210219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UTP = diphosphate + H(+) + UMP; Xref=Rhea:RHEA:29395,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; EC=3.6.1.9;
CC Evidence={ECO:0000269|PubMed:24210219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + TTP = 5-methyl-UMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:58736, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:63527, ChEBI:CHEBI:142797;
CC Evidence={ECO:0000269|PubMed:24210219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + psi-UTP = diphosphate + H(+) + psi-UMP;
CC Xref=Rhea:RHEA:58740, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58380, ChEBI:CHEBI:142798;
CC Evidence={ECO:0000269|PubMed:24210219};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:24210219};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=47.4 uM for dTTP {ECO:0000269|PubMed:24210219};
CC KM=29.7 uM for UTP {ECO:0000269|PubMed:24210219};
CC KM=72.0 uM for CTP {ECO:0000269|PubMed:24210219};
CC KM=13.0 uM for m(5)UTP {ECO:0000269|PubMed:24210219};
CC KM=20 uM for pseudo-UTP {ECO:0000269|PubMed:24210219};
CC Note=kcat is 5.7 sec(-1) with dTTP as substrate. kcat is 2.6 sec(-1)
CC with UTP as substrate. kcat is 1.2 sec(-1) with CTP as substrate.
CC kcat is 2.2 sec(-1) with m(5)UTP as substrate. kcat is 5.3 sec(-1)
CC with pseudo-UTP as substrate. {ECO:0000269|PubMed:24210219};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1940 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Maf family. YhdE subfamily.
CC {ECO:0000305|PubMed:24210219}.
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DR EMBL; X94335; CAA64031.1; -; Genomic_DNA.
DR EMBL; X90518; CAA62105.1; -; Genomic_DNA.
DR EMBL; Z75019; CAA99309.1; -; Genomic_DNA.
DR EMBL; AY692705; AAT92724.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10886.1; -; Genomic_DNA.
DR PIR; S60984; S60984.
DR RefSeq; NP_014754.3; NM_001183530.3.
DR AlphaFoldDB; Q99210; -.
DR SMR; Q99210; -.
DR BioGRID; 34507; 20.
DR DIP; DIP-1305N; -.
DR IntAct; Q99210; 7.
DR MINT; Q99210; -.
DR STRING; 4932.YOR111W; -.
DR MaxQB; Q99210; -.
DR PaxDb; Q99210; -.
DR PRIDE; Q99210; -.
DR EnsemblFungi; YOR111W_mRNA; YOR111W; YOR111W.
DR GeneID; 854278; -.
DR KEGG; sce:YOR111W; -.
DR SGD; S000005637; YOR111W.
DR VEuPathDB; FungiDB:YOR111W; -.
DR eggNOG; KOG1509; Eukaryota.
DR GeneTree; ENSGT00940000168021; -.
DR HOGENOM; CLU_040416_0_2_1; -.
DR InParanoid; Q99210; -.
DR OMA; RIDGDFY; -.
DR BioCyc; YEAST:G3O-33640-MON; -.
DR PRO; PR:Q99210; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q99210; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036218; F:dTTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central.
DR GO; GO:0036221; F:UTP diphosphatase activity; IEA:RHEA.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00555; Maf; 1.
DR Gene3D; 3.90.950.10; -; 1.
DR HAMAP; MF_00528; Maf; 1.
DR InterPro; IPR029001; ITPase-like_fam.
DR InterPro; IPR003697; Maf-like.
DR PANTHER; PTHR43213; PTHR43213; 1.
DR Pfam; PF02545; Maf; 1.
DR PIRSF; PIRSF006305; Maf; 1.
DR SUPFAM; SSF52972; SSF52972; 1.
DR TIGRFAMs; TIGR00172; maf; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleotide metabolism; Reference proteome.
FT CHAIN 1..232
FT /note="dTTP/UTP pyrophosphatase"
FT /id="PRO_0000123091"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:24210219"
FT SITE 29
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000305|PubMed:24210219"
FT SITE 104
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000305|PubMed:24210219"
FT SITE 196
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000305|PubMed:24210219"
FT MUTAGEN 25
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 26
FT /note="T->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 29
FT /note="R->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 30
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 66
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 74
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 76
FT /note="Q->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 77
FT /note="N->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 103
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 104
FT /note="T->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 115
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 116
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 188
FT /note="E->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 193
FT /note="F->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 194
FT /note="K->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 196
FT /note="Q->A,E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
SQ SEQUENCE 232 AA; 26477 MW; C0A83ED2AE20BE13 CRC64;
MSGNSQLPPD VIGFICSKYD IILASTSPRR YEILHDIMGI TDLKTMVSTF EENLDKMNYS
TDPIGYVCDT SWHKAQNIIE ILTDYEDENP NEIDKPKLII CADTIIIDKS GRIYEKPKTK
EVQKKFLMKF CYEDDEPVNV VTAVTLIKWY GRENFELVPF RDETKVYFDN KIPLRILEEY
VESGDGLEVG GGFKIQGQGA ILIEKIEGDY YNVVGLPLNK TFKGLYAEAN SI
