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Protein

L-asparaginase 2-1

Gene

ASP3-1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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-asparagine2 Publications
  3. KM=0.27 mM for N-acetyl-L-asparagine2 Publications
  4. KM=0.07 mM for N-carbamyl-L-asparagine2 Publications
  5. KM=0.06 mM for N-isoleucyl-L-asparagine2 Publications
  6. KM=0.06 mM for N-glycyl-L-asparagine2 Publications
  7. KM=0.06 mM for N-valyl-L-asparagine2 Publications
  8. KM=0.2 mM for N-methionyl-L-asparagine2 Publications
  9. KM=0.4 mM for N-glycyl-D-asparagine2 Publications
  1. Vmax=42 µmol/min/mg enzyme for L-asparagine2 Publications
  2. Vmax=60 µmol/min/mg enzyme for D-asparagine2 Publications
  3. Vmax=167 µmol/min/mg enzyme for N-acetyl-L-asparagine2 Publications
  4. Vmax=79 µmol/min/mg enzyme for N-carbamyl-L-asparagine2 Publications
  5. Vmax=67 µmol/min/mg enzyme for N-isoleucyl-L-asparagine2 Publications
  6. Vmax=135 µmol/min/mg enzyme for N-glycyl-L-asparagine2 Publications
  7. Vmax=56 µmol/min/mg enzyme for N-valyl-L-asparagine2 Publications
  8. Vmax=92 µmol/min/mg enzyme for N-methionyl-L-asparagine2 Publications
  9. Vmax=8 µmol/min/mg enzyme for N-glycyl-D-asparagine2 Publications

pH dependencei

Optimum pH is 6.8. Active from pH 5.5 to pH 7.5. Stable from pH 3.5 to pH 10.5.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei43O-isoaspartyl threonine intermediatePROSITE-ProRule annotation1
Binding sitei89SubstrateBy similarity1

GO - Molecular functioni

  • asparaginase activity Source: SGD

GO - Biological processi

  • asparagine catabolic process Source: SGD
  • 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
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

SGDiS000004145. ASP3-1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Periplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 251 PublicationAdd BLAST25
ChainiPRO_000000236226 – 362L-asparaginase 2-1Add BLAST337

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi29N-linked (GlcNAc...)Sequence analysis1
Glycosylationi93N-linked (GlcNAc...)Sequence analysis1
Glycosylationi239N-linked (GlcNAc...)Sequence analysis1

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

BioGridi31428. 15 interactors.
31431. 22 interactors.
31433. 17 interactors.
MINTiMINT-509856.

Structurei

3D structure databases

ProteinModelPortaliP0CZ17.
SMRiP0CZ17.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 359Asparaginase/glutaminasePROSITE-ProRule annotationAdd BLAST327

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni122 – 123Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the asparaginase 1 family.Curated
Contains 1 asparaginase/glutaminase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00510000050435.
InParanoidiP0CZ17.
KOiK01424.
OrthoDBiEOG092C3Z6Q.

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.
PS51732. ASN_GLN_ASE_3. 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

        10         20         30         40         50
MRSLNTLLLS LFVAMSSGAP LLKIREEKNS SLPSIKIFGT GGTIASKGST
60 70 80 90 100
SATTAGYSVG LTVNDLIEAV PSLAEKANLD YLQVSNVGSN SLNYTHLIPL
110 120 130 140 150
YHGISEALAS DDYAGAVVTH GTDTMEETAF FLDLTINSEK PVCIAGAMRP
160 170 180 190 200
ATATSADGPM NLYQAVSIAA SEKSLGRGTM ITLNDRIASG FWTTKMNANS
210 220 230 240 250
LDTFRADEQG YLGYFSNDDV EFYYPPVKPN GWQFFDISNL TDPSEIPEVI
260 270 280 290 300
ILYSYQGLNP ELIVKAVKDL GAKGIVLAGS GAGSWTATGS IVNEQLYEEY
310 320 330 340 350
GIPIVHSRRT ADGTVPPDDA PEYAIGSGYL NPQKSRILLQ LCLYSGYGMD
360
QIRSVFSGVY GG
Length:362
Mass (Da):38,687
Last modified:June 28, 2011 - v1
Checksum:i1DE5DC8692BF0461
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti31S → P in AAS56283 (PubMed:17322287).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti26 – 55Missing .1 PublicationAdd BLAST30

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP0CZ17.
SMRiP0CZ17.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31428. 15 interactors.
31431. 22 interactors.
31433. 17 interactors.
MINTiMINT-509856.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

SGDiS000004145. ASP3-1.

Phylogenomic databases

GeneTreeiENSGT00510000050435.
InParanoidiP0CZ17.
KOiK01424.
OrthoDBiEOG092C3Z6Q.

Enzyme and pathway databases

BioCyciYEAST:YLR155C-MONOMER.

Miscellaneous databases

PROiP0CZ17.

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.
PS51732. ASN_GLN_ASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 34 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.