HNT2_YEAST
ID HNT2_YEAST Reviewed; 206 AA.
AC P49775; D6VST4; Q6TQU2; Q6TQU3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase;
DE EC=3.6.1.29;
DE AltName: Full=AP3A hydrolase;
DE Short=AP3Aase;
DE AltName: Full=Diadenosine 5',5'''-P1,P3-triphosphate hydrolase;
DE AltName: Full=Dinucleosidetriphosphatase;
DE AltName: Full=Hit family protein 2;
GN Name=HNT2; Synonyms=APH1; OrderedLocusNames=YDR305C; ORFNames=D9740.15;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-72 AND 172-206.
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Kennedy M.C., Dietrich F.S.;
RT "Verification of 3' and 5' ends of S.cerevisiae transcripts.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1653209; DOI=10.1128/jb.173.17.5275-5279.1991;
RA Brevet A., Chen J., Fromant M., Blanquet S., Plateau P.;
RT "Isolation and characterization of a dinucleoside triphosphatase from
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 173:5275-5279(1991).
RN [5]
RP FUNCTION.
RX PubMed=9573184; DOI=10.1128/jb.180.9.2345-2349.1998;
RA Chen J., Brevet A., Blanquet S., Plateau P.;
RT "Control of 5',5'-dinucleoside triphosphate catabolism by APH1, a
RT Saccharomyces cerevisiae analog of human FHIT.";
RL J. Bacteriol. 180:2345-2349(1998).
RN [6]
RP FUNCTION, ACTIVE SITE, AND MUTAGENESIS OF HIS-98.
RX PubMed=12028594; DOI=10.1186/1471-2199-3-7;
RA Rubio-Texeira M., Varnum J.M., Bieganowski P., Brenner C.;
RT "Control of dinucleoside polyphosphates by the FHIT-homologous HNT2 gene,
RT adenine biosynthesis and heat shock in Saccharomyces cerevisiae.";
RL BMC Mol. Biol. 3:7-7(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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 [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
CC -!- FUNCTION: Cleaves A-5'-PPP-5'A to yield AMP and ADP. Can cleave all
CC dinucleoside polyphosphates, provided the phosphate chain contains at
CC least 3 phosphates and that 1 of the 2 bases composing the nucleotide
CC is a purine. Is most effective on dinucleoside triphosphates.
CC Negatively regulates intracellular dinucleoside polyphosphate levels,
CC which elevate following heat shock. {ECO:0000269|PubMed:12028594,
CC ECO:0000269|PubMed:9573184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2
CC H(+); Xref=Rhea:RHEA:13893, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58529, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=3.6.1.29;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Divalent metal cations. Mn(2+) is the preferred ion.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.3 uM for P(1)-P(3)-bis(5'-adenosyl) triphosphate
CC {ECO:0000269|PubMed:1653209};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion
CC {ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 1920 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64741.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA12144.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U28374; AAB64741.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY389296; AAQ97228.1; -; mRNA.
DR EMBL; AY389295; AAQ97227.1; -; mRNA.
DR EMBL; BK006938; DAA12144.1; ALT_INIT; Genomic_DNA.
DR PIR; S61191; S61191.
DR RefSeq; NP_010591.1; NM_001180613.1.
DR AlphaFoldDB; P49775; -.
DR SMR; P49775; -.
DR BioGRID; 32357; 81.
DR DIP; DIP-4620N; -.
DR IntAct; P49775; 1.
DR MINT; P49775; -.
DR STRING; 4932.YDR305C; -.
DR MaxQB; P49775; -.
DR PaxDb; P49775; -.
DR PRIDE; P49775; -.
DR GeneID; 851899; -.
DR KEGG; sce:YDR305C; -.
DR SGD; S000002713; HNT2.
DR eggNOG; KOG3379; Eukaryota.
DR HOGENOM; CLU_056776_7_2_1; -.
DR BioCyc; YEAST:G3O-29864-MON; -.
DR SABIO-RK; P49775; -.
DR PRO; PR:P49775; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P49775; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IDA:SGD.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:SGD.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009164; P:nucleoside catabolic process; IMP:SGD.
DR CDD; cd01275; FHIT; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR039383; FHIT.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR Pfam; PF01230; HIT; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Mitochondrion; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..206
FT /note="Bis(5'-adenosyl)-triphosphatase"
FT /id="PRO_0000109801"
FT DOMAIN 3..115
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT REGION 143..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 96..100
FT /note="Histidine triad motif"
FT COMPBIAS 144..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000269|PubMed:12028594"
FT MUTAGEN 98
FT /note="H->A,D: Fails to reduce intracellular dinucleoside
FT polyphosphate levels."
FT /evidence="ECO:0000269|PubMed:12028594"
SQ SEQUENCE 206 AA; 23542 MW; 4143F7371805B378 CRC64;
MNKPIYFSKF LVTEQVFYKS KYTYALVNLK PIVPGHVLIV PLRTTVLNLS DLTMPESQDY
FKTLQLIHRF IKWQYKADSI NVAIQDGPEA GQSVPHLHTH IIPRYKINNV GDLIYDKLDH
WDGNGTLTDW QGRRDEYLGV GGRQARKNNS TSATVDGDEL SQGPNVLKPD SQRKVRALTE
MKKEAEDLQA RLEEFVSSDP GLTQWL
