ID   ASP23_YEAST             Reviewed;         362 AA.
AC   P0CX78; D6VYF3; P11163; Q12268; Q6Q5K8; Q6Q5K9;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=L-asparaginase 2-3;
DE            EC=3.5.1.1;
DE   AltName: Full=L-asparaginase II;
DE   AltName: Full=L-asparagine amidohydrolase II;
DE            Short=ASP II;
DE   Flags: Precursor;
GN   Name=ASP3-3; OrderedLocusNames=YLR158C; ORFNames=L9632.8;
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], PROTEIN SEQUENCE OF 26-41 AND 56-71, AND
RP   VARIANT 26-GLU--ALA-55 DEL.
RX   PubMed=3042786; DOI=10.1016/s0021-9258(18)37878-5;
RA   Kim K.-W., Kamerud J.Q., Livingston D.M., Roon R.J.;
RT   "Asparaginase II of Saccharomyces cerevisiae. Characterization of the ASP3
RT   gene.";
RL   J. Biol. Chem. 263:11948-11953(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=342521; DOI=10.1016/s0021-9258(17)38144-9;
RA   Dunlop P.C., Meyer G.M., Ban D., Roon R.J.;
RT   "Characterization of two forms of asparaginase in Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 253:1297-1304(1978).
RN   [5]
RP   INDUCTION.
RX   PubMed=6995441; DOI=10.1128/jb.143.1.422-426.1980;
RA   Dunlop P.C., Meyer G.M., Roon R.J.;
RT   "Nitrogen catabolite repression of asparaginase II in Saccharomyces
RT   cerevisiae.";
RL   J. Bacteriol. 143:422-426(1980).
RN   [6]
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=6986375; DOI=10.1016/s0021-9258(19)86066-0;
RA   Dunlop P.C., Meyer G.M., Roon R.J.;
RT   "Reactions of asparaginase II of Saccharomyces cerevisiae. A mechanistic
RT   analysis of hydrolysis and hydroxylaminolysis.";
RL   J. Biol. Chem. 255:1542-1546(1980).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.27 mM for L-asparagine {ECO:0000269|PubMed:342521,
CC         ECO:0000269|PubMed:6986375};
CC         KM=0.27 mM for D-asparagine {ECO:0000269|PubMed:342521,
CC         ECO:0000269|PubMed:6986375};
CC         KM=0.27 mM for N-acetyl-L-asparagine {ECO:0000269|PubMed:342521,
CC         ECO:0000269|PubMed:6986375};
CC         KM=0.07 mM for N-carbamyl-L-asparagine {ECO:0000269|PubMed:342521,
CC         ECO:0000269|PubMed:6986375};
CC         KM=0.06 mM for N-isoleucyl-L-asparagine {ECO:0000269|PubMed:342521,
CC         ECO:0000269|PubMed:6986375};
CC         KM=0.06 mM for N-glycyl-L-asparagine {ECO:0000269|PubMed:342521,
CC         ECO:0000269|PubMed:6986375};
CC         KM=0.06 mM for N-valyl-L-asparagine {ECO:0000269|PubMed:342521,
CC         ECO:0000269|PubMed:6986375};
CC         KM=0.2 mM for N-methionyl-L-asparagine {ECO:0000269|PubMed:342521,
CC         ECO:0000269|PubMed:6986375};
CC         KM=0.4 mM for N-glycyl-D-asparagine {ECO:0000269|PubMed:342521,
CC         ECO:0000269|PubMed:6986375};
CC         Vmax=42 umol/min/mg enzyme for L-asparagine
CC         {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
CC         Vmax=60 umol/min/mg enzyme for D-asparagine
CC         {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
CC         Vmax=167 umol/min/mg enzyme for N-acetyl-L-asparagine
CC         {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
CC         Vmax=79 umol/min/mg enzyme for N-carbamyl-L-asparagine
CC         {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
CC         Vmax=67 umol/min/mg enzyme for N-isoleucyl-L-asparagine
CC         {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
CC         Vmax=135 umol/min/mg enzyme for N-glycyl-L-asparagine
CC         {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
CC         Vmax=56 umol/min/mg enzyme for N-valyl-L-asparagine
CC         {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
CC         Vmax=92 umol/min/mg enzyme for N-methionyl-L-asparagine
CC         {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
CC         Vmax=8 umol/min/mg enzyme for N-glycyl-D-asparagine
CC         {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
CC         Note=Does not act on isoasparagine, L-aspartate diamide, beta-alanine
CC         amide and L-glutamine.;
CC       pH dependence:
CC         Optimum pH is 6.8. Active from pH 5.5 to pH 7.5. Stable from pH 3.5
CC         to pH 10.5. {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
CC   -!- SUBCELLULAR LOCATION: Secreted. Periplasm.
CC   -!- INDUCTION: Subject to nitrogen catabolite repression (NCR). Not found
CC       in cells grown on rich nitrogen sources like ammonia, glutamine or
CC       glutamate, but is found in cells that have been subjected to nitrogen
CC       starvation or have been grown on a poor nitrogen source such as
CC       proline. {ECO:0000269|PubMed:6995441}.
CC   -!- MISCELLANEOUS: Yeast contains 2 L-asparaginase isoenzymes: cytoplasmic
CC       L-asparaginase I, and cell wall L-asparaginase II.
CC   -!- MISCELLANEOUS: There are 4 copies for L-asparaginase 2 in yeast. The 4
CC       identical copies ASP3-1, ASP3-2, ASP3-3 and ASP3-4 are arranged in
CC       tandem repeats located near a ribosomal DNA cluster.
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U51921; AAB67482.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09478.1; -; Genomic_DNA.
DR   PIR; S68471; S68471.
DR   RefSeq; NP_013256.1; NM_001182042.1.
DR   RefSeq; NP_013258.1; NM_001182044.1.
DR   RefSeq; NP_013259.1; NM_001182045.1.
DR   RefSeq; NP_013261.1; NM_001182047.1.
DR   AlphaFoldDB; P0CX78; -.
DR   SMR; P0CX78; -.
DR   BioGRID; 31426; 2.
DR   BioGRID; 31428; 39.
DR   BioGRID; 31431; 61.
DR   BioGRID; 31433; 31.
DR   GlyCosmos; P0CX78; 3 sites, No reported glycans.
DR   GlyGen; P0CX78; 3 sites.
DR   EnsemblFungi; YLR155C_mRNA; YLR155C; YLR155C.
DR   EnsemblFungi; YLR157C_mRNA; YLR157C; YLR157C.
DR   EnsemblFungi; YLR158C_mRNA; YLR158C; YLR158C.
DR   EnsemblFungi; YLR160C_mRNA; YLR160C; YLR160C.
DR   GeneID; 850850; -.
DR   GeneID; 850852; -.
DR   GeneID; 850855; -.
DR   GeneID; 850857; -.
DR   KEGG; sce:YLR155C; -.
DR   KEGG; sce:YLR157C; -.
DR   KEGG; sce:YLR158C; -.
DR   KEGG; sce:YLR160C; -.
DR   AGR; SGD:S000004148; -.
DR   SGD; S000004148; ASP3-3.
DR   VEuPathDB; FungiDB:YLR155C; -.
DR   VEuPathDB; FungiDB:YLR157C; -.
DR   VEuPathDB; FungiDB:YLR158C; -.
DR   VEuPathDB; FungiDB:YLR160C; -.
DR   HOGENOM; CLU_019134_1_1_1; -.
DR   InParanoid; P0CX78; -.
DR   OrthoDB; 1421816at2759; -.
DR   BioCyc; YEAST:YLR158C-MONOMER; -.
DR   PRO; PR:P0CX78; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P0CX78; Protein.
DR   ExpressionAtlas; P0CX78; baseline and differential.
DR   GO; GO:0030287; C:cell wall-bounded periplasmic space; IDA:SGD.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IDA:SGD.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IDA:SGD.
DR   CDD; cd08964; L-asparaginase_II; 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   Direct protein sequencing; Glycoprotein; Hydrolase; Periplasm;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:3042786"
FT   CHAIN           26..362
FT                   /note="L-asparaginase 2-3"
FT                   /id="PRO_0000410442"
FT   DOMAIN          33..359
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   ACT_SITE        43
FT                   /note="O-isoaspartyl threonine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT                   ECO:0000255|PROSITE-ProRule:PRU10100"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122..123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         26..55
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:3042786"
SQ   SEQUENCE   362 AA;  38687 MW;  1DE5DC8692BF0461 CRC64;
     MRSLNTLLLS LFVAMSSGAP LLKIREEKNS SLPSIKIFGT GGTIASKGST SATTAGYSVG
     LTVNDLIEAV PSLAEKANLD YLQVSNVGSN SLNYTHLIPL YHGISEALAS DDYAGAVVTH
     GTDTMEETAF FLDLTINSEK PVCIAGAMRP ATATSADGPM NLYQAVSIAA SEKSLGRGTM
     ITLNDRIASG FWTTKMNANS LDTFRADEQG YLGYFSNDDV EFYYPPVKPN GWQFFDISNL
     TDPSEIPEVI ILYSYQGLNP ELIVKAVKDL GAKGIVLAGS GAGSWTATGS IVNEQLYEEY
     GIPIVHSRRT ADGTVPPDDA PEYAIGSGYL NPQKSRILLQ LCLYSGYGMD QIRSVFSGVY
     GG
//