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L-asparaginase 2-1 (EC 3.5.1.1) (L-asparaginase II) (L-asparagine amidohydrolase II) (ASP II)

 ASP21_YEAST             Reviewed;         362 AA.
P0CZ17; D6VYF3; P11163; Q12268; Q6Q5K8; Q6Q5K9;
28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
25-OCT-2017, entry version 40.
RecName: Full=L-asparaginase 2-1;
EC=3.5.1.1;
AltName: Full=L-asparaginase II;
AltName: Full=L-asparagine amidohydrolase II;
Short=ASP II;
Flags: Precursor;
Name=ASP3-1; OrderedLocusNames=YLR155C; ORFNames=L9632.6;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-41 AND
56-71, AND VARIANT 26-GLU--ALA-55 DEL.
PubMed=3042786;
Kim K.-W., Kamerud J.Q., Livingston D.M., Roon R.J.;
"Asparaginase II of Saccharomyces cerevisiae. Characterization of the
ASP3 gene.";
J. Biol. Chem. 263:11948-11953(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=342521;
Dunlop P.C., Meyer G.M., Ban D., Roon R.J.;
"Characterization of two forms of asparaginase in Saccharomyces
cerevisiae.";
J. Biol. Chem. 253:1297-1304(1978).
[6]
INDUCTION.
PubMed=6995441;
Dunlop P.C., Meyer G.M., Roon R.J.;
"Nitrogen catabolite repression of asparaginase II in Saccharomyces
cerevisiae.";
J. Bacteriol. 143:422-426(1980).
[7]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=6986375;
Dunlop P.C., Meyer G.M., Roon R.J.;
"Reactions of asparaginase II of Saccharomyces cerevisiae. A
mechanistic analysis of hydrolysis and hydroxylaminolysis.";
J. Biol. Chem. 255:1542-1546(1980).
-!- CATALYTIC ACTIVITY: L-asparagine + H(2)O = L-aspartate + NH(3).
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.27 mM for L-asparagine {ECO:0000269|PubMed:342521,
ECO:0000269|PubMed:6986375};
KM=0.27 mM for D-asparagine {ECO:0000269|PubMed:342521,
ECO:0000269|PubMed:6986375};
KM=0.27 mM for N-acetyl-L-asparagine {ECO:0000269|PubMed:342521,
ECO:0000269|PubMed:6986375};
KM=0.07 mM for N-carbamyl-L-asparagine
{ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
KM=0.06 mM for N-isoleucyl-L-asparagine
{ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
KM=0.06 mM for N-glycyl-L-asparagine {ECO:0000269|PubMed:342521,
ECO:0000269|PubMed:6986375};
KM=0.06 mM for N-valyl-L-asparagine {ECO:0000269|PubMed:342521,
ECO:0000269|PubMed:6986375};
KM=0.2 mM for N-methionyl-L-asparagine
{ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
KM=0.4 mM for N-glycyl-D-asparagine {ECO:0000269|PubMed:342521,
ECO:0000269|PubMed:6986375};
Vmax=42 umol/min/mg enzyme for L-asparagine
{ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
Vmax=60 umol/min/mg enzyme for D-asparagine
{ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
Vmax=167 umol/min/mg enzyme for N-acetyl-L-asparagine
{ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
Vmax=79 umol/min/mg enzyme for N-carbamyl-L-asparagine
{ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
Vmax=67 umol/min/mg enzyme for N-isoleucyl-L-asparagine
{ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
Vmax=135 umol/min/mg enzyme for N-glycyl-L-asparagine
{ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
Vmax=56 umol/min/mg enzyme for N-valyl-L-asparagine
{ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
Vmax=92 umol/min/mg enzyme for N-methionyl-L-asparagine
{ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
Vmax=8 umol/min/mg enzyme for N-glycyl-D-asparagine
{ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375};
Note=Does not act on isoasparagine, L-aspartate diamide, beta-
alanine amide and L-glutamine.;
pH dependence:
Optimum pH is 6.8. Active from pH 5.5 to pH 7.5. Stable from pH
3.5 to pH 10.5. {ECO:0000269|PubMed:342521,
ECO:0000269|PubMed:6986375};
-!- SUBCELLULAR LOCATION: Secreted. Periplasm.
-!- INDUCTION: Subject to nitrogen catabolite repression (NCR). Not
found in cells grown on rich nitrogen sources like ammonia,
glutamine or glutamate, but is found in cells that have been
subjected to nitrogen starvation or have been grown on a poor
nitrogen source such as proline. {ECO:0000269|PubMed:6995441}.
-!- MISCELLANEOUS: Yeast contains 2 L-asparaginase isoenzymes:
cytoplasmic L-asparaginase I, and cell wall L-asparaginase II.
-!- MISCELLANEOUS: There are 4 copies for L-asparaginase 2 in yeast.
The 4 identical copies ASP3-1, ASP3-2, ASP3-3 and ASP3-4 are
arranged in tandem repeats located near a ribosomal DNA cluster.
-!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA34438.1; Type=Frameshift; Positions=243; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; J03926; AAA34438.1; ALT_FRAME; Genomic_DNA.
EMBL; U51921; AAB67479.1; -; Genomic_DNA.
EMBL; AY557957; AAS56283.1; -; Genomic_DNA.
EMBL; BK006945; DAA09469.1; -; Genomic_DNA.
PIR; S68471; S68471.
RefSeq; NP_013256.1; NM_001182042.1.
RefSeq; NP_013258.1; NM_001182044.1.
RefSeq; NP_013259.1; NM_001182045.1.
RefSeq; NP_013261.1; NM_001182047.1.
ProteinModelPortal; P0CZ17; -.
SMR; P0CZ17; -.
BioGrid; 31428; 39.
BioGrid; 31431; 61.
BioGrid; 31433; 30.
MINT; MINT-509856; -.
STRING; 4932.YLR160C; -.
EnsemblFungi; YLR155C; YLR155C; YLR155C.
EnsemblFungi; YLR157C; YLR157C; YLR157C.
EnsemblFungi; YLR158C; YLR158C; YLR158C.
EnsemblFungi; YLR160C; YLR160C; YLR160C.
GeneID; 850850; -.
GeneID; 850852; -.
GeneID; 850855; -.
GeneID; 850857; -.
KEGG; sce:YLR155C; -.
KEGG; sce:YLR157C; -.
KEGG; sce:YLR158C; -.
KEGG; sce:YLR160C; -.
SGD; S000004145; ASP3-1.
GeneTree; ENSGT00510000050435; -.
InParanoid; P0CZ17; -.
KO; K01424; -.
OMA; VRKNHTS; -.
OrthoDB; EOG092C3Z6Q; -.
BioCyc; YEAST:YLR155C-MONOMER; -.
PRO; PR:P0CZ17; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0030287; C:cell wall-bounded periplasmic space; IDA:SGD.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004067; F:asparaginase activity; IDA:SGD.
GO; GO:0006530; P:asparagine catabolic process; IDA:SGD.
GO; GO:0006995; P:cellular response to nitrogen starvation; IDA:SGD.
Gene3D; 3.40.50.1170; -; 1.
Gene3D; 3.40.50.40; -; 1.
InterPro; IPR004550; AsnASE_II.
InterPro; IPR036152; Asp/glu_Ase-like_sf.
InterPro; IPR006034; Asparaginase/glutaminase-like.
InterPro; IPR020827; Asparaginase/glutaminase_AS1.
InterPro; IPR027475; Asparaginase/glutaminase_AS2.
InterPro; IPR027473; L-asparaginase_C.
InterPro; IPR027474; L-asparaginase_N.
InterPro; IPR037152; L-asparaginase_N_sf.
Pfam; PF00710; Asparaginase; 1.
PIRSF; PIRSF001220; L-ASNase_gatD; 1.
PRINTS; PR00139; ASNGLNASE.
SMART; SM00870; Asparaginase; 1.
SUPFAM; SSF53774; SSF53774; 1.
TIGRFAMs; TIGR00520; asnASE_II; 1.
PROSITE; PS00144; ASN_GLN_ASE_1; 1.
PROSITE; PS00917; ASN_GLN_ASE_2; 1.
PROSITE; PS51732; ASN_GLN_ASE_3; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Glycoprotein; Hydrolase;
Periplasm; Reference proteome; Secreted; Signal.
SIGNAL 1 25 {ECO:0000269|PubMed:3042786}.
CHAIN 26 362 L-asparaginase 2-1.
/FTId=PRO_0000002362.
DOMAIN 33 359 Asparaginase/glutaminase.
{ECO:0000255|PROSITE-ProRule:PRU01068}.
REGION 122 123 Substrate binding. {ECO:0000250}.
ACT_SITE 43 43 O-isoaspartyl threonine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10099,
ECO:0000255|PROSITE-ProRule:PRU10100}.
BINDING 89 89 Substrate. {ECO:0000250}.
CARBOHYD 29 29 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 26 55 Missing. {ECO:0000269|PubMed:3042786}.
CONFLICT 31 31 S -> P (in Ref. 4; AAS56283).
{ECO:0000305}.
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


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