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P30363 (ASPG_BACLI) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Short name=L-ASNase
EC=3.5.1.1
Alternative name(s):
L-asparagine amidohydrolase
Gene names
Name:ansA
OrganismBacillus licheniformis
Taxonomic identifier1402 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the asparaginase 1 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processcellular amino acid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionasparaginase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 322322L-asparaginase
PRO_0000171076

Regions

Region89 – 902Substrate binding By similarity

Sites

Active site131O-isoaspartyl threonine intermediate By similarity
Binding site561Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P30363 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 7048BEC52D0B1DFB

FASTA32235,442
        10         20         30         40         50         60 
MNKKVALITT GGTIASRKTE SGRLAAGAIS GPELAEMCSL PEDVQIDVYP AFQLPSMHIT 

        70         80         90        100        110        120 
FQHLLELKQT IERVFQDGGY DGAVVTHGTD TLEETAYFLD LTIEDERPVV VTGSQRAPEQ 

       130        140        150        160        170        180 
QGTDAYTNIR HAVYTACSPD IKGAGTVVVF NERIFNARYV KKVHASNLQG FDVFGFGYLG 

       190        200        210        220        230        240 
IIDNDKVYVY QKLLKRDVHQ LQRPLPAVDI VKCYLDGDGK FIRAAVREGV EGIVLEGVGR 

       250        260        270        280        290        300 
GQVPPNMMAD IEQALNQGVY IVITTSAEEG EVYTTYDYAG SSYDLAKKGV ILGKDYDSKK 

       310        320 
ARMKLAVLLA SYKEGIKDKF CY 

« Hide

References

[1]"Lack of specific hybridization between the lep genes of Salmonella typhimurium and Bacillus licheniformis."
van Dijl J.M., de Jong A., Smith H., Bron S., Venema G.
FEMS Microbiol. Lett. 65:345-351(1991) [PubMed: 1916233] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11497 Genomic DNA. Translation: CAA77574.1.
PIRS18999.

3D structure databases

ProteinModelPortalP30363.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_CS.
[Graphical view]
PANTHERPTHR11707. Asp/Glutamnse. 1 hit.
PfamPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFPIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSPR00139. ASNGLNASE.
SMARTSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMSSF53774. Asp/Glutamnse. 1 hit.
PROSITEPS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASPG_BACLI
AccessionPrimary (citable) accession number: P30363
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: September 21, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families