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P0CZ17

- ASP21_YEAST

UniProt

P0CZ17 - ASP21_YEAST

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Protein
L-asparaginase 2-1
Gene
ASP3-1, YLR155C, L9632.6
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Kineticsi

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

  1. KM=0.27 mM for L-asparagine2 Publications
  2. KM=0.27 mM for D-asparagine
  3. KM=0.27 mM for N-acetyl-L-asparagine
  4. KM=0.07 mM for N-carbamyl-L-asparagine
  5. KM=0.06 mM for N-isoleucyl-L-asparagine
  6. KM=0.06 mM for N-glycyl-L-asparagine
  7. KM=0.06 mM for N-valyl-L-asparagine
  8. KM=0.2 mM for N-methionyl-L-asparagine
  9. 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 dependencei

Optimum pH is 6.8. Active from pH 5.5 to pH 7.5. Stable from pH 3.5 to pH 10.5.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei43 – 431O-isoaspartyl threonine intermediate By similarity
Binding sitei89 – 891Substrate By similarity

GO - Molecular functioni

  1. asparaginase activity Source: SGD

GO - Biological processi

  1. asparagine catabolic process Source: SGD
  2. cellular response to nitrogen starvation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciYEAST:YLR155C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
L-asparaginase 2-1 (EC:3.5.1.1)
Alternative name(s):
L-asparaginase II
L-asparagine amidohydrolase II
Short name:
ASP II
Gene namesi
Name:ASP3-1
Ordered Locus Names:YLR155C
ORF Names:L9632.6
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

CYGDiYLR155c.
SGDiS000004145. ASP3-1.

Subcellular locationi

GO - Cellular componenti

  1. cell wall-bounded periplasmic space Source: SGD
  2. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 Publication
Add
BLAST
Chaini26 – 362337L-asparaginase 2-1
PRO_0000002362Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi29 – 291N-linked (GlcNAc...) Reviewed prediction
Glycosylationi93 – 931N-linked (GlcNAc...) Reviewed prediction
Glycosylationi239 – 2391N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Expressioni

Inductioni

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.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi31426. 1 interaction.
31428. 15 interactions.
31431. 22 interactions.
31433. 17 interactions.
MINTiMINT-509856.

Structurei

3D structure databases

ProteinModelPortaliP0CZ17.
SMRiP0CZ17. Positions 32-343.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 1232Substrate binding By similarity

Sequence similaritiesi

Belongs to the asparaginase 1 family.

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00510000050435.
KOiK01424.
OrthoDBiEOG75TMN3.

Family and domain databases

Gene3Di3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProiIPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_AS1.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view]
PfamiPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFiPIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSiPR00139. ASNGLNASE.
SMARTiSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMiSSF53774. SSF53774. 1 hit.
TIGRFAMsiTIGR00520. asnASE_II. 1 hit.
PROSITEiPS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0CZ17-1 [UniParc]FASTAAdd to Basket

« Hide

MRSLNTLLLS LFVAMSSGAP LLKIREEKNS SLPSIKIFGT GGTIASKGST    50
SATTAGYSVG LTVNDLIEAV PSLAEKANLD YLQVSNVGSN SLNYTHLIPL 100
YHGISEALAS DDYAGAVVTH GTDTMEETAF FLDLTINSEK PVCIAGAMRP 150
ATATSADGPM NLYQAVSIAA SEKSLGRGTM ITLNDRIASG FWTTKMNANS 200
LDTFRADEQG YLGYFSNDDV EFYYPPVKPN GWQFFDISNL TDPSEIPEVI 250
ILYSYQGLNP ELIVKAVKDL GAKGIVLAGS GAGSWTATGS IVNEQLYEEY 300
GIPIVHSRRT ADGTVPPDDA PEYAIGSGYL NPQKSRILLQ LCLYSGYGMD 350
QIRSVFSGVY GG 362
Length:362
Mass (Da):38,687
Last modified:June 28, 2011 - v1
Checksum:i1DE5DC8692BF0461
GO

Sequence cautioni

The sequence AAA34438.1 differs from that shown. Reason: Frameshift at position 243.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 5530Missing.
Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311S → P in AAS56283. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03926 Genomic DNA. Translation: AAA34438.1. Frameshift.
U51921 Genomic DNA. Translation: AAB67479.1.
AY557957 Genomic DNA. Translation: AAS56283.1.
BK006945 Genomic DNA. Translation: DAA09469.1.
PIRiS68471.
RefSeqiNP_013256.1. NM_001182042.1.
NP_013258.1. NM_001182044.1.
NP_013259.1. NM_001182045.1.
NP_013261.1. NM_001182047.1.

Genome annotation databases

EnsemblFungiiYLR155C; YLR155C; YLR155C.
YLR157C; YLR157C; YLR157C.
YLR158C; YLR158C; YLR158C.
YLR160C; YLR160C; YLR160C.
GeneIDi850850.
850852.
850855.
850857.
KEGGisce:YLR155C.
sce:YLR157C.
sce:YLR158C.
sce:YLR160C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03926 Genomic DNA. Translation: AAA34438.1 . Frameshift.
U51921 Genomic DNA. Translation: AAB67479.1 .
AY557957 Genomic DNA. Translation: AAS56283.1 .
BK006945 Genomic DNA. Translation: DAA09469.1 .
PIRi S68471.
RefSeqi NP_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

ProteinModelPortali P0CZ17.
SMRi P0CZ17. Positions 32-343.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31426. 1 interaction.
31428. 15 interactions.
31431. 22 interactions.
31433. 17 interactions.
MINTi MINT-509856.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR155C ; YLR155C ; YLR155C .
YLR157C ; YLR157C ; YLR157C .
YLR158C ; YLR158C ; YLR158C .
YLR160C ; YLR160C ; YLR160C .
GeneIDi 850850.
850852.
850855.
850857.
KEGGi sce:YLR155C.
sce:YLR157C.
sce:YLR158C.
sce:YLR160C.

Organism-specific databases

CYGDi YLR155c.
SGDi S000004145. ASP3-1.

Phylogenomic databases

GeneTreei ENSGT00510000050435.
KOi K01424.
OrthoDBi EOG75TMN3.

Enzyme and pathway databases

BioCyci YEAST:YLR155C-MONOMER.

Miscellaneous databases

NextBioi 967149.

Family and domain databases

Gene3Di 3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProi IPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_AS1.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view ]
Pfami PF00710. Asparaginase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSi PR00139. ASNGLNASE.
SMARTi SM00870. Asparaginase. 1 hit.
[Graphical view ]
SUPFAMi SSF53774. SSF53774. 1 hit.
TIGRFAMsi TIGR00520. asnASE_II. 1 hit.
PROSITEi PS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "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.
  6. "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.
  7. "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.

Entry informationi

Entry nameiASP21_YEAST
AccessioniPrimary (citable) accession number: P0CZ17
Secondary accession number(s): D6VYF3
, P11163, Q12268, Q6Q5K8, Q6Q5K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: May 14, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi