HNT1_YEAST
ID HNT1_YEAST Reviewed; 158 AA.
AC Q04344; D6VRM5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Adenosine 5'-monophosphoramidase HNT1 {ECO:0000303|PubMed:11805111};
DE EC=3.-.-.- {ECO:0000269|PubMed:11805111};
DE AltName: Full=Histidine triad nucleotide-binding protein HNT1 {ECO:0000303|PubMed:11805111};
DE Short=HINT {ECO:0000303|PubMed:11805111};
DE AltName: Full=Hit family protein 1 {ECO:0000303|PubMed:10958787};
GN Name=HNT1 {ECO:0000303|PubMed:10958787};
GN Synonyms=HIT1 {ECO:0000303|PubMed:1472710}; OrderedLocusNames=YDL125C;
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].
RX PubMed=1860879; DOI=10.1083/jcb.114.3.443;
RA Froehlich K.-U., Fries H.W., Ruediger M., Erdmann R., Botstein D.,
RA Mecke D.;
RT "Yeast cell cycle protein CDC48p shows full-length homology to the
RT mammalian protein VCP and is a member of a protein family involved in
RT secretion, peroxisome formation, and gene expression.";
RL J. Cell Biol. 114:443-453(1991).
RN [2]
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 [3]
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 [4]
RP IDENTIFICATION, AND SIMILARITY TO OTHER MEMBERS OF THE HIT FAMILY.
RX PubMed=1472710; DOI=10.3109/10425179209034013;
RA Seraphin B.;
RT "The HIT protein family: a new family of proteins present in prokaryotes,
RT yeast and mammals.";
RL DNA Seq. 3:177-179(1992).
RN [5]
RP FUNCTION, AND INTERACTION WITH KIN28.
RX PubMed=10958787; DOI=10.1074/jbc.c000505200;
RA Korsisaari N., Makela T.P.;
RT "Interactions of Cdk7 and Kin28 with Hint/PKCI-1 and Hnt1 histidine triad
RT proteins.";
RL J. Biol. Chem. 275:34837-34840(2000).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP ACTIVE SITE, AND MUTAGENESIS OF HIS-116.
RX PubMed=11805111; DOI=10.1074/jbc.m111480200;
RA Bieganowski P., Garrison P.N., Hodawadekar S.C., Faye G., Barnes L.D.,
RA Brenner C.;
RT "Adenosine monophosphoramidase activity of Hint and Hnt1 supports function
RT of Kin28, Ccl1, and Tfb3.";
RL J. Biol. Chem. 277:10852-10860(2002).
RN [7]
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 [8]
RP INDUCTION.
RX PubMed=22842922; DOI=10.1038/ncb2549;
RA Tkach J.M., Yimit A., Lee A.Y., Riffle M., Costanzo M., Jaschob D.,
RA Hendry J.A., Ou J., Moffat J., Boone C., Davis T.N., Nislow C., Brown G.W.;
RT "Dissecting DNA damage response pathways by analysing protein localization
RT and abundance changes during DNA replication stress.";
RL Nat. Cell Biol. 14:966-976(2012).
RN [9]
RP INDUCTION.
RX PubMed=32475637; DOI=10.1016/j.bbrc.2020.04.104;
RA Matsuki Y., Saito T., Nakano Y., Hashimoto S., Matsuo Y., Inada T.;
RT "Crucial role of leaky initiation of uORF3 in the downregulation of HNT1 by
RT ER stress.";
RL Biochem. Biophys. Res. Commun. 528:186-192(2020).
RN [10]
RP INDUCTION.
RX PubMed=31692084; DOI=10.1111/mmi.14416;
RA Tatip S., Taggart J., Wang Y., MacDiarmid C.W., Eide D.J.;
RT "Changes in transcription start sites of Zap1-regulated genes during zinc
RT deficiency: Implications for HNT1 gene regulation.";
RL Mol. Microbiol. 113:285-296(2020).
RN [11]
RP INDUCTION.
RX PubMed=33184379; DOI=10.1038/s41598-020-76239-3;
RA Matsuki Y., Matsuo Y., Nakano Y., Iwasaki S., Yoko H., Udagawa T., Li S.,
RA Saeki Y., Yoshihisa T., Tanaka K., Ingolia N.T., Inada T.;
RT "Ribosomal protein S7 ubiquitination during ER stress in yeast is
RT associated with selective mRNA translation and stress outcome.";
RL Sci. Rep. 10:19669-19669(2020).
CC -!- FUNCTION: Hydrolyzes adenosine 5'-monophosphoramidate substrates such
CC as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl
CC lysine methyl ester and AMP-NH2 (PubMed:11805111). Plays a role in the
CC regulation of kinase KIN28 function (PubMed:10958787). Essential for
CC growth on galactose media at elevated temperatures (PubMed:11805111).
CC {ECO:0000269|PubMed:10958787, ECO:0000269|PubMed:11805111}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphoramidate + H2O = AMP + NH4(+);
CC Xref=Rhea:RHEA:67916, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57890, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:11805111};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67917;
CC Evidence={ECO:0000269|PubMed:11805111};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11805111};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=870 nM for adenosine 5'-monophosphoramidate
CC {ECO:0000269|PubMed:11805111};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with KIN28
CC (PubMed:10958787). {ECO:0000250|UniProtKB:Q59WG0,
CC ECO:0000269|PubMed:10958787}.
CC -!- INDUCTION: Expression is increased in response to DNA replication
CC stress (PubMed:22842922). Expression is regulated by ZAP1 during zinc-
CC deficiency via changes in transcription start sites (PubMed:31692084).
CC Expression is also down-regulated during unfolded protein response
CC (UPR) (PubMed:32475637, PubMed:33184379). {ECO:0000269|PubMed:22842922,
CC ECO:0000269|PubMed:31692084, ECO:0000269|PubMed:32475637,
CC ECO:0000269|PubMed:33184379}.
CC -!- MISCELLANEOUS: Present with 5410 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-15 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X56956; CAA40275.1; -; Genomic_DNA.
DR EMBL; Z74173; CAA98693.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11735.1; -; Genomic_DNA.
DR PIR; B39977; B39977.
DR RefSeq; NP_010158.1; NM_001180184.1.
DR AlphaFoldDB; Q04344; -.
DR SMR; Q04344; -.
DR BioGRID; 31938; 81.
DR DIP; DIP-2760N; -.
DR IntAct; Q04344; 4.
DR MINT; Q04344; -.
DR STRING; 4932.YDL125C; -.
DR iPTMnet; Q04344; -.
DR MaxQB; Q04344; -.
DR PaxDb; Q04344; -.
DR PRIDE; Q04344; -.
DR EnsemblFungi; YDL125C_mRNA; YDL125C; YDL125C.
DR GeneID; 851432; -.
DR KEGG; sce:YDL125C; -.
DR SGD; S000002283; HNT1.
DR VEuPathDB; FungiDB:YDL125C; -.
DR eggNOG; KOG3275; Eukaryota.
DR HOGENOM; CLU_056776_3_0_1; -.
DR InParanoid; Q04344; -.
DR OMA; SDCLFCK; -.
DR BioCyc; YEAST:G3O-29524-MON; -.
DR PRO; PR:Q04344; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04344; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; IDA:SGD.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IDA:SGD.
DR GO; GO:0010043; P:response to zinc ion; IMP:SGD.
DR CDD; cd01277; HINT_subgroup; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR039384; HINT.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR001310; Histidine_triad_HIT.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR46648; PTHR46648; 1.
DR Pfam; PF01230; HIT; 1.
DR PRINTS; PR00332; HISTRIAD.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Nucleotide-binding; Reference proteome.
FT CHAIN 1..158
FT /note="Adenosine 5'-monophosphoramidase HNT1"
FT /id="PRO_0000109800"
FT DOMAIN 26..129
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT MOTIF 114..118
FT /note="Histidine triad motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT ACT_SITE 116
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000269|PubMed:11805111"
FT BINDING 51..52
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 103
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 109..111
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 116..118
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT MUTAGEN 116
FT /note="H->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:11805111"
SQ SEQUENCE 158 AA; 17680 MW; 55BCD6CFCF666954 CRC64;
MEPLISAPYL TTTKMSAPAT LDAACIFCKI IKSEIPSFKL IETKYSYAFL DIQPTAEGHA
LIIPKYHGAK LHDIPDEFLT DAMPIAKRLA KAMKLDTYNV LQNNGKIAHQ EVDHVHFHLI
PKRDEKSGLI VGWPAQETDF DKLGKLHKEL LAKLEGSD
