ASPG1_YEAST
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 03-AUG-2022, entry version 180.
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].
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;
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=H2O + L-asparagine = 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; 43.
DR DIP; DIP-4030N; -.
DR IntAct; P38986; 18.
DR MINT; P38986; -.
DR STRING; 4932.YDR321W; -.
DR iPTMnet; P38986; -.
DR MaxQB; P38986; -.
DR PaxDb; P38986; -.
DR PRIDE; P38986; -.
DR EnsemblFungi; YDR321W_mRNA; YDR321W; YDR321W.
DR GeneID; 851920; -.
DR KEGG; sce:YDR321W; -.
DR SGD; S000002729; ASP1.
DR VEuPathDB; FungiDB:YDR321W; -.
DR eggNOG; KOG0503; Eukaryota.
DR HOGENOM; CLU_019134_1_1_1; -.
DR InParanoid; P38986; -.
DR OMA; RKNHTSR; -.
DR BioCyc; YEAST:YDR321W-MON; -.
DR BRENDA; 3.5.1.1; 984.
DR SABIO-RK; P38986; -.
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:asparagine catabolic process; IMP:SGD.
DR CDD; cd08964; L-asparaginase_II; 1.
DR Gene3D; 3.40.50.1170; -; 1.
DR Gene3D; 3.40.50.40; -; 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 Pfam; PF00710; Asparaginase; 1.
DR Pfam; PF17763; Asparaginase_C; 1.
DR PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR PRINTS; PR00139; ASNGLNASE.
DR SMART; SM00870; Asparaginase; 1.
DR SUPFAM; SSF53774; SSF53774; 1.
DR TIGRFAMs; TIGR00520; asnASE_II; 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."
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
