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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: -Experimental evidence at protein leveli

Functioni

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.

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

Keywordsi

Molecular functionHydrolase

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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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...) asparagineSequence analysis1
Glycosylationi93N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi239N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP0CZ17

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, 39 interactors
31431, 61 interactors
31433, 30 interactors
STRINGi4932.YLR160C

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

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00510000050435
InParanoidiP0CZ17
KOiK01424
OMAiTKTYGFH
OrthoDBiEOG092C3Z6Q

Family and domain databases

Gene3Di3.40.50.1170, 1 hit
3.40.50.40, 1 hit
InterProiView protein in InterPro
IPR004550 AsnASE_II
IPR036152 Asp/glu_Ase-like_sf
IPR006034 Asparaginase/glutaminase-like
IPR020827 Asparaginase/glutaminase_AS1
IPR027475 Asparaginase/glutaminase_AS2
IPR027473 L-asparaginase_C
IPR027474 L-asparaginase_N
IPR037152 L-asparaginase_N_sf
PfamiView protein in Pfam
PF00710 Asparaginase, 1 hit
PIRSFiPIRSF001220 L-ASNase_gatD, 1 hit
PRINTSiPR00139 ASNGLNASE
SMARTiView protein in SMART
SM00870 Asparaginase, 1 hit
SUPFAMiSSF53774 SSF53774, 1 hit
TIGRFAMsiTIGR00520 asnASE_II, 1 hit
PROSITEiView protein in PROSITE
PS00144 ASN_GLN_ASE_1, 1 hit
PS00917 ASN_GLN_ASE_2, 1 hit
PS51732 ASN_GLN_ASE_3, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiASP21_YEAST
AccessioniPrimary (citable) accession number: P0CZ17
Secondary accession number(s): D6VYF3
, P11163, Q12268, Q6Q5K8, Q6Q5K9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: March 28, 2018
This is version 43 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health