ASP24_YEAST
ID ASP24_YEAST Reviewed; 362 AA.
AC P0CX79; D6VYF3; P11163; Q12268; Q6Q5K8; Q6Q5K9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=L-asparaginase 2-4;
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=ASP3-4; OrderedLocusNames=YLR160C; ORFNames=L9632.9;
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}.
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DR EMBL; U51921; AAB67484.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09481.1; -; 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; P0CX79; -.
DR SMR; P0CX79; -.
DR BioGRID; 31428; 39.
DR BioGRID; 31431; 61.
DR BioGRID; 31433; 31.
DR IntAct; P0CX79; 1.
DR MINT; P0CX79; -.
DR PRIDE; P0CX79; -.
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 SGD; S000004150; ASP3-4.
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; P0CX79; -.
DR BioCyc; YEAST:YLR160C-MON; -.
DR PRO; PR:P0CX79; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P0CX79; protein.
DR ExpressionAtlas; P0CX79; baseline and differential.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
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; 3.40.50.1170; -; 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 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 2-4"
FT /id="PRO_0000410443"
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
