L-asparaginase 2-1 precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P0CZ17 (ASP21_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 13. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	ASP3-1
Ordered Locus Names:	YLR155C
ORF Names:	L9632.6

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	362 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.6
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. K_M=0.27 mM for L-asparagine Ref.5 Ref.7 K_M=0.27 mM for D-asparagine K_M=0.27 mM for N-acetyl-L-asparagine K_M=0.07 mM for N-carbamyl-L-asparagine K_M=0.06 mM for N-isoleucyl-L-asparagine K_M=0.06 mM for N-glycyl-L-asparagine K_M=0.06 mM for N-valyl-L-asparagine K_M=0.2 mM for N-methionyl-L-asparagine K_M=0.4 mM for N-glycyl-D-asparagine V_max=42 µmol/min/mg enzyme for L-asparagine V_max=60 µmol/min/mg enzyme for D-asparagine V_max=167 µmol/min/mg enzyme for N-acetyl-L-asparagine V_max=79 µmol/min/mg enzyme for N-carbamyl-L-asparagine V_max=67 µmol/min/mg enzyme for N-isoleucyl-L-asparagine V_max=135 µmol/min/mg enzyme for N-glycyl-L-asparagine V_max=56 µmol/min/mg enzyme for N-valyl-L-asparagine V_max=92 µmol/min/mg enzyme for N-methionyl-L-asparagine V_max=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 caution	The sequence AAA34438.1 differs from that shown. Reason: Frameshift at position 243.

Ontologies

Keywords
Cellular component	Periplasm Secreted
Domain	Signal
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	asparagine catabolic process Inferred from direct assay Ref.1. Source: SGD cellular response to nitrogen starvation Inferred from direct assay Ref.1. Source: SGD
Cellular_component	cell wall-bounded periplasmic space Inferred from direct assay PubMed 238936. Source: SGD endoplasmic reticulum Inferred from direct assay PubMed 11914276. Source: SGD extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear envelope Inferred from direct assay PubMed 11914276. Source: SGD
Molecular_function	asparaginase activity Inferred from direct assay PubMed 238936. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

Ref.1

Chain

26 – 362

337

L-asparaginase 2-1

PRO_0000002362

Regions

Region

122 – 123

Substrate binding By similarity

Sites

Active site

O-isoaspartyl threonine intermediate By similarity

Binding site

Substrate By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

239

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

26 – 55

Missing.

Experimental info

Sequence conflict

S → P in AAS56283. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P0CZ17 [UniParc].

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

362

38,687

        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' referencesShow '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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." 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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	S68471.
RefSeq	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
ProteinModelPortal	P0CZ17.
SMR	P0CZ17. Positions 32-343.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR155C; YLR155C; YLR155C. YLR157C; YLR157C; YLR157C. YLR158C; YLR158C; YLR158C. YLR160C; YLR160C; YLR160C.
GeneID	850850. 850852. 850855. 850857.
KEGG	sce:YLR155C. sce:YLR157C. sce:YLR158C. sce:YLR160C.
Organism-specific databases
CYGD	YLR155c.
SGD	S000004145. ASP3-1.
Phylogenomic databases
GeneTree	ENSGT00510000050435.
KO	K01424.
Gene expression databases
ArrayExpress	P0CZ17.
GermOnline	YLR155C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004550. AsnASE_II. IPR006034. Asparaginase/glutaminase. IPR020827. Asparaginase/glutaminase_CS. [Graphical view]
Pfam	PF00710. Asparaginase. 1 hit. [Graphical view]
PIRSF	PIRSF001220. L-ASNase_gatD. 1 hit.
PRINTS	PR00139. ASNGLNASE.
SMART	SM00870. Asparaginase. 1 hit. [Graphical view]
SUPFAM	SSF53774. Asp/Glutamnse. 1 hit.
TIGRFAMs	TIGR00520. asnASE_II. 1 hit.
PROSITE	PS00144. ASN_GLN_ASE_1. 1 hit. PS00917. ASN_GLN_ASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967149.

Entry information

Entry name

ASP21_YEAST

Accession

Primary (citable) accession number: P0CZ17
Secondary accession number(s): D6VYF3

Q6Q5K9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 28, 2011
Last sequence update:	June 28, 2011
Last modified:	May 1, 2013
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XII

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents