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O57971 (ASGX_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Putative L-asparaginase

EC=3.5.1.1
Alternative name(s):
L-asparagine amidohydrolase
Gene names
Ordered Locus Names:PH0232
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length305 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)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 174174Putative L-asparaginase subunit alpha
PRO_0000184581
Chain175 – 305131Putative L-asparaginase subunit beta
PRO_0000329018

Sites

Active site1751Nucleophile By similarity
Site174 – 1752Cleavage; by autolysis Potential

Sequences

Sequence LengthMass (Da)Tools
O57971 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: C5391CAB69D48E03

FASTA30532,543
        10         20         30         40         50         60 
MVAIIVHGGA GTIKKEERIP KVIEGVKEAV IVGWKELRKG SALDAVEEAI KVLEDNPIFN 

        70         80         90        100        110        120 
AGTGSVLTID GKVEMDAAIM RGKTLEAGAV AGIWGVKNPI SVARKVMEKT DHVLLVGEGA 

       130        140        150        160        170        180 
VKFARLMGFP EYNPITEERI EQWKELKEKL MKGEIKYWKK LGELIKEYPE VLRSTVGAVA 

       190        200        210        220        230        240 
FDGEEIVAGT STGGVFLKMF GRVGDTPIIG AGTYANEVAG ASCTGLGEVA IRLALAKTAT 

       250        260        270        280        290        300 
DFVRLGMDAQ AASNAAISLA TKYFGKDTMG IIMVDAAGNV GFAKNTKHMS YAYMKDGMEE 


PEAGV 

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References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000001 Genomic DNA. Translation: BAA29304.1.
PIRA71247.
RefSeqNP_142228.1. NC_000961.1.

3D structure databases

ProteinModelPortalO57971.
ModBaseSearch...

Protein family/group databases

MEROPST02.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000001542; EBPYRP00000001542; EBPYRG00000001542.
GeneID1444122.
GenomeReviewsGene locus PH0232 in contig BA000001_GR.
KEGGpho:PH0232.
NMPDRfig|70601.1.peg.222.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000022719.
HOGENOMHBG735787.
OMAWAVKWTS.
PhylomeDBO57971.
ProtClustDBCLSK253204.

Enzyme and pathway databases

BioCycPHOR70601:PH0232-MONOMER.

Family and domain databases

InterProIPR000246. Peptidase_T2.
[Graphical view]
KOK13051.
PANTHERPTHR10188. Peptidase_T2. 1 hit.
PfamPF01112. Asparaginase_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASGX_PYRHO
AccessionPrimary (citable) accession number: O57971
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: December 14, 2011
This is version 63 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