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P0CX79 (ASP24_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-asparaginase 2-4

EC=3.5.1.1
Alternative name(s):
L-asparaginase II
L-asparagine amidohydrolase II
Short name=ASP II
Gene names
Name:ASP3-4
Ordered Locus Names:YLR160C
ORF Names:L9632.9
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-asparagine + H2O = L-aspartate + NH3.

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. Ref.5

Miscellaneous

Yeast contains 2 L-asparaginase isoenzymes: cytoplasmic L-asparaginase I, and cell wall L-asparaginase II.

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.

Sequence similarities

Belongs to the asparaginase 1 family.

Biophysicochemical properties

Kinetic parameters:

Does not act on isoasparagine, L-aspartate diamide, beta-alanine amide and L-glutamine.

KM=0.27 mM for L-asparagine Ref.4 Ref.6

KM=0.27 mM for D-asparagine

KM=0.27 mM for N-acetyl-L-asparagine

KM=0.07 mM for N-carbamyl-L-asparagine

KM=0.06 mM for N-isoleucyl-L-asparagine

KM=0.06 mM for N-glycyl-L-asparagine

KM=0.06 mM for N-valyl-L-asparagine

KM=0.2 mM for N-methionyl-L-asparagine

KM=0.4 mM for N-glycyl-D-asparagine

Vmax=42 µmol/min/mg enzyme for L-asparagine

Vmax=60 µmol/min/mg enzyme for D-asparagine

Vmax=167 µmol/min/mg enzyme for N-acetyl-L-asparagine

Vmax=79 µmol/min/mg enzyme for N-carbamyl-L-asparagine

Vmax=67 µmol/min/mg enzyme for N-isoleucyl-L-asparagine

Vmax=135 µmol/min/mg enzyme for N-glycyl-L-asparagine

Vmax=56 µmol/min/mg enzyme for N-valyl-L-asparagine

Vmax=92 µmol/min/mg enzyme for N-methionyl-L-asparagine

Vmax=8 µmol/min/mg enzyme for N-glycyl-D-asparagine

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.1
Chain26 – 362337L-asparaginase 2-4
PRO_0000410443

Regions

Region122 – 1232Substrate binding By similarity

Sites

Active site431O-isoaspartyl threonine intermediate By similarity
Binding site891Substrate By similarity

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential

Natural variations

Natural variant26 – 5530Missing.

Sequences

Sequence LengthMass (Da)Tools
P0CX79 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 1DE5DC8692BF0461

FASTA36238,687
        10         20         30         40         50         60 
MRSLNTLLLS LFVAMSSGAP LLKIREEKNS SLPSIKIFGT GGTIASKGST SATTAGYSVG 

        70         80         90        100        110        120 
LTVNDLIEAV PSLAEKANLD YLQVSNVGSN SLNYTHLIPL YHGISEALAS DDYAGAVVTH 

       130        140        150        160        170        180 
GTDTMEETAF FLDLTINSEK PVCIAGAMRP ATATSADGPM NLYQAVSIAA SEKSLGRGTM 

       190        200        210        220        230        240 
ITLNDRIASG FWTTKMNANS LDTFRADEQG YLGYFSNDDV EFYYPPVKPN GWQFFDISNL 

       250        260        270        280        290        300 
TDPSEIPEVI ILYSYQGLNP ELIVKAVKDL GAKGIVLAGS GAGSWTATGS IVNEQLYEEY 

       310        320        330        340        350        360 
GIPIVHSRRT ADGTVPPDDA PEYAIGSGYL NPQKSRILLQ LCLYSGYGMD QIRSVFSGVY 


GG 

« Hide

References

« Hide 'large scale' references
[1]"Asparaginase II of Saccharomyces cerevisiae. Characterization of the ASP3 gene."
Kim K.-W., Kamerud J.Q., Livingston D.M., Roon R.J.
J. Biol. Chem. 263:11948-11953(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-41 AND 56-71, VARIANT 26-GLU--ALA-55 DEL.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
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. expand/collapse author list , 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.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
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.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Characterization of two forms of asparaginase in Saccharomyces cerevisiae."
Dunlop P.C., Meyer G.M., Ban D., Roon R.J.
J. Biol. Chem. 253:1297-1304(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[5]"Nitrogen catabolite repression of asparaginase II in Saccharomyces cerevisiae."
Dunlop P.C., Meyer G.M., Roon R.J.
J. Bacteriol. 143:422-426(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[6]"Reactions of asparaginase II of Saccharomyces cerevisiae. A mechanistic analysis of hydrolysis and hydroxylaminolysis."
Dunlop P.C., Meyer G.M., Roon R.J.
J. Biol. Chem. 255:1542-1546(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U51921 Genomic DNA. Translation: AAB67484.1.
BK006945 Genomic DNA. Translation: DAA09481.1.
PIRS68471.
RefSeqNP_013256.1. NM_001182042.1.
NP_013258.1. NM_001182044.1.
NP_013259.1. NM_001182045.1.
NP_013261.1. NM_001182047.1.

3D structure databases

ProteinModelPortalP0CX79.
SMRP0CX79. Positions 32-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31426. 1 interaction.
31428. 15 interactions.
31431. 22 interactions.
31433. 17 interactions.
IntActP0CX79. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR155C; YLR155C; YLR155C.
YLR157C; YLR157C; YLR157C.
YLR158C; YLR158C; YLR158C.
YLR160C; YLR160C; YLR160C.
GeneID850850.
850852.
850855.
850857.
KEGGsce:YLR155C.
sce:YLR157C.
sce:YLR158C.
sce:YLR160C.

Organism-specific databases

CYGDYLR160c.
SGDS000004150. ASP3-4.

Phylogenomic databases

KOK01424.
OrthoDBEOG75TMN3.

Enzyme and pathway databases

BioCycYEAST:YLR160C-MONOMER.

Family and domain databases

Gene3D3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProIPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_AS1.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view]
PfamPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFPIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSPR00139. ASNGLNASE.
SMARTSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMSSF53774. SSF53774. 1 hit.
TIGRFAMsTIGR00520. asnASE_II. 1 hit.
PROSITEPS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967149.

Entry information

Entry nameASP24_YEAST
AccessionPrimary (citable) accession number: P0CX79
Secondary accession number(s): D6VYF3 expand/collapse secondary AC list , P11163, Q12268, Q6Q5K8, Q6Q5K9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: May 14, 2014
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families