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Reviewed, UniProtKB/Swiss-Prot Q8U4E6 (ASGX_PYRFU)

Last modified November 3, 2009. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative L-asparaginase
    EC=3.5.1.1
Alternative name(s):
    L-asparagine amidohydrolase
Cleaved into the following 2 chains:
    1- Recommended name:
            Putative L-asparaginase subunit alpha
    2- Recommended name:
            Putative L-asparaginase subunit beta
Gene names
Ordered Locus Names: PF0142
OrganismPyrococcus furiosus [Complete proteome] [HAMAP]
Taxonomic identifier2261 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

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

Post-translational modification

Autocleaved. Generates the alpha and beta subunits. The N-terminal residue of the beta subunit is thought to be responsible for the nucleophile hydrolase activity Potential.

Sequence similarities

Belongs to the Ntn-hydrolase family.

Ontologies

Keywords
   Molecular functionHydrolase
Protease
   PTMAutocatalytic cleavage
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionasparaginase activity

Inferred from electronic annotation. Source: EC

peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 175175Putative L-asparaginase subunit alpha
PRO_0000184580
Chain176 – 306131Putative L-asparaginase subunit beta
PRO_0000329017

Sites

Active site1761Nucleophile By similarity
Site175 – 1762Cleavage; by autolysis Potential

Sequences

Sequence LengthMass (Da)Tools
Q8U4E6-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 68410D8FE6DE9EE2

FASTA30632,855
        10         20         30         40         50         60 
MVAIIVHGGA GTIRKEERIP KIIEGVREAV LTGWRELKKG SALDAVEEAV KVLEDNPLFN 

        70         80         90        100        110        120 
AGTGSVLTLD GKVEMDAAIM RGKTLDAGAV AGIWGVKNPI SVARKVMEKT DHVLLIGEGA 

       130        140        150        160        170        180 
VKFARLMGFP EYDPTTEERR KQWEELRKKL LETGEIRHWK KLSELIKEYP EVLRSTVGAV 

       190        200        210        220        230        240 
AFDGEEIVAG TSTGGVFLKM FGRVGDTPII GAGTYANEVA GASCTGLGEV AIKLSLAKTA 

       250        260        270        280        290        300 
TDFVRLGLDA QAASEAAIRL ATKYFGPDTM GIIMVDSNGN VGFAKNTKHM SYAFMKEGMK 


EPEAGV 

« Hide

References

[1]"The complete sequence of the Pyrococcus furiosus genome."
Weiss R.B., Dunn D.M., Robb F.T., Brown J.R.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

AE009950 Genomic DNA. Translation: AAL80266.1.
RefSeqNP_577871.1.

3D structure databases

HSSPHSSP built from PDB template 9GAF based on UniProtKB Q47898.
ModBaseSearch...

Protein family/group databases

MEROPST02.002.

Genome annotation databases

GeneID1467974.
GenomeReviewsGene locus PF0142 in contig AE009950_GR.
KEGGpfu:PF0142.
NMPDRfig|186497.1.peg.145.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8U4E6.
OMAMVAIIVH.

Enzyme and pathway databases

BRENDA3.5.1.1. 321.

Family and domain databases

InterProIPR000246. Peptidase_T2.
[Graphical view]
PANTHERPTHR10188. Peptidase_T2. 1 hit.
PfamPF01112. Asparaginase_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASGX_PYRFU
AccessionPrimary (citable) accession number: Q8U4E6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: June 1, 2002
Last modified: November 3, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents