ID   ASPG1_YEAST             Reviewed;         381 AA.
AC   P38986; D6VSV3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   10-JUN-2026, entry version 196.
DE   RecName: Full=L-asparaginase 1;
DE            EC=3.5.1.1;
DE   AltName: Full=L-asparaginase I;
DE   AltName: Full=L-asparagine amidohydrolase I;
DE            Short=ASP I;
GN   Name=ASP1; OrderedLocusNames=YDR321W; ORFNames=D9798.6;
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], AND MUTAGENESIS OF ALA-176.
RC   STRAIN=ATCC 26786 / X2180-1A;
RX   PubMed=8026756; DOI=10.1016/0378-1119(94)90200-3;
RA   Sinclair K., Warner J.P., Bonthron D.T.;
RT   "The ASP1 gene of Saccharomyces cerevisiae, encoding the intracellular
RT   isozyme of L-asparaginase.";
RL   Gene 144:37-43(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867; DOI=10.1038/387s075;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-asparagine + H2O = L-aspartate + NH4(+);
CC         Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC   -!- SUBUNIT: Homomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Expressed constitutively.
CC   -!- MISCELLANEOUS: Yeast contains two L-asparaginase isoenzymes:
CC       cytoplasmic L-asparaginase I, and cell wall L-asparaginase II.
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR   EMBL; Z27406; CAA81794.1; -; Genomic_DNA.
DR   EMBL; U32517; AAB64757.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12163.1; -; Genomic_DNA.
DR   PIR; S48513; S48513.
DR   RefSeq; NP_010607.3; NM_001180629.3.
DR   AlphaFoldDB; P38986; -.
DR   SMR; P38986; -.
DR   BioGRID; 32378; 58.
DR   DIP; DIP-4030N; -.
DR   FunCoup; P38986; 96.
DR   IntAct; P38986; 25.
DR   MINT; P38986; -.
DR   STRING; 4932.YDR321W; -.
DR   iPTMnet; P38986; -.
DR   PaxDb; 4932-YDR321W; -.
DR   PeptideAtlas; P38986; -.
DR   EnsemblFungi; YDR321W_mRNA; YDR321W; YDR321W.
DR   GeneID; 851920; -.
DR   KEGG; sce:YDR321W; -.
DR   AGR; SGD:S000002729; -.
DR   SGD; S000002729; ASP1.
DR   VEuPathDB; FungiDB:YDR321W; -.
DR   eggNOG; KOG0503; Eukaryota.
DR   HOGENOM; CLU_019134_1_1_1; -.
DR   InParanoid; P38986; -.
DR   OMA; RYYMQPL; -.
DR   OrthoDB; 542841at2759; -.
DR   BioCyc; YEAST:YDR321W-MONOMER; -.
DR   BRENDA; 3.5.1.1; 984.
DR   SABIO-RK; P38986; -.
DR   BioGRID-ORCS; 851920; 5 hits in 10 CRISPR screens.
DR   CD-CODE; E03F929F; Stress granule.
DR   PRO; PR:P38986; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P38986; protein.
DR   GO; GO:0005737; C:cytoplasm; IC:SGD.
DR   GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
DR   GO; GO:0004067; F:asparaginase activity; IDA:SGD.
DR   GO; GO:0006530; P:L-asparagine catabolic process; IMP:SGD.
DR   CDD; cd08964; L-asparaginase_II; 1.
DR   FunFam; 3.40.50.1170:FF:000001; L-asparaginase 2; 1.
DR   FunFam; 3.40.50.40:FF:000006; L-asparaginase I; 1.
DR   Gene3D; 3.40.50.40; -; 1.
DR   Gene3D; 3.40.50.1170; L-asparaginase, N-terminal domain; 1.
DR   InterPro; IPR004550; AsnASE_II.
DR   InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR   InterPro; IPR006034; Asparaginase/glutaminase-like.
DR   InterPro; IPR020827; Asparaginase/glutaminase_AS1.
DR   InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR   InterPro; IPR040919; Asparaginase_C.
DR   InterPro; IPR027473; L-asparaginase_C.
DR   InterPro; IPR027474; L-asparaginase_N.
DR   InterPro; IPR037152; L-asparaginase_N_sf.
DR   NCBIfam; TIGR00520; asnASE_II; 1.
DR   PANTHER; PTHR11707:SF28; 60 KDA LYSOPHOSPHOLIPASE; 1.
DR   PANTHER; PTHR11707; L-ASPARAGINASE; 1.
DR   Pfam; PF00710; Asparaginase; 1.
DR   Pfam; PF17763; Asparaginase_C; 1.
DR   PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR   PIRSF; PIRSF500176; L_ASNase; 1.
DR   PRINTS; PR00139; ASNGLNASE.
DR   SMART; SM00870; Asparaginase; 1.
DR   SUPFAM; SSF53774; Glutaminase/Asparaginase; 1.
DR   PROSITE; PS00144; ASN_GLN_ASE_1; 1.
DR   PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR   PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..381
FT                   /note="L-asparaginase 1"
FT                   /id="PRO_0000171091"
FT   DOMAIN          54..378
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   ACT_SITE        64
FT                   /note="O-isoaspartyl threonine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT                   ECO:0000255|PROSITE-ProRule:PRU10100"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         141..142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         350
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         176
FT                   /note="A->V: Almost no activity."
FT                   /evidence="ECO:0000269|PubMed:8026756"
SQ   SEQUENCE   381 AA;  41395 MW;  8204CB7C58B5B75F CRC64;
     MKSDSVEITT ICPDVENSQF VVQSNCPETI PEILKSQNAA VNGSGIACQQ RSLPRIKILG
     TGGTIASKAI DSSQTAGYHV DLTIQDLLDA IPDISKVCDI EYEQLCNVDS KDINEDILYK
     IYKGVSESLQ AFDGIVITHG TDTLSETAFF IESTIDAGDV PIVFVGSMRP STSVSADGPM
     NLYQAICIAS NPKSRGRGVL VSLNDQISSG YYITKTNANS LDSFNVRQGY LGNFVNNEIH
     YYYPPVKPQG CHKFKLRVDG KHFKLPEVCI LYAHQAFPPA IVNLVADKYD GIVLATMGAG
     SLPEEVNETC MKLSLPIVYS KRSMDGMVPI ANVPKKGSKE DNLIASGYLS PEKSRILLQL
     CLAGNYTLEE IKHVFTGVYG G
//