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P50286 (ASPG_WOLSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Synonyms:ansB
Ordered Locus Names:WS0660
OrganismWolinella succinogenes [Complete proteome] [HAMAP]
Taxonomic identifier844 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeWolinella

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the asparaginase 1 family.

Sequence caution

The sequence CAE09790.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processasparagine 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 – 330330L-asparaginase
PRO_0000171086

Regions

Region93 – 942Substrate binding By similarity

Sites

Active site141O-isoaspartyl threonine intermediate Probable

Experimental info

Sequence conflict1211S → P in CAA61503. Ref.1
Sequence conflict1211S → P in CAA58658. Ref.1

Secondary structure

.......................................................... 330
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50286 [UniParc].

Last modified September 26, 2003. Version 2.
Checksum: B706B41958E924CE

FASTA33034,856
        10         20         30         40         50         60 
MAKPQVTILA TGGTIAGSGE SSVKSSYSAG AVTVDKLLAA VPAINDLATI KGEQISSIGS 

        70         80         90        100        110        120 
QEMTGKVWLK LAKRVNELLA QKETEAVIIT HGTDTMEETA FFLNLTVKSQ KPVVLVGAMR 

       130        140        150        160        170        180 
SGSSMSADGP MNLYNAVNVA INKASTNKGV VIVMNDEIHA AREATKLNTT AVNAFASPNT 

       190        200        210        220        230        240 
GKIGTVYYGK VEYFTQSVRP HTLASEFDIS KIEELPRVDI LYAHPDDTDV LVNAALQAGA 

       250        260        270        280        290        300 
KGIIHAGMGN GNPFPLTQNA LEKAAKSGVV VARSSRVGSG STTQEAEVDD KKLGFVATES 

       310        320        330 
LNPQKARVLL MLALTKTSDR EAIQKIFSTY 

« Hide

References

« Hide 'large scale' references
[1]"Crystal structure and amino acid sequence of Wolinella succinogenes L-asparaginase."
Lubkowski J., Palm G.J., Gilliland G.L., Derst C., Roehm K.H., Wlodawer A.
Eur. J. Biochem. 241:201-207(1996) [PubMed: 8898907] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[2]"Complete genome sequence and analysis of Wolinella succinogenes."
Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., Meyer F., Lederer H., Schuster S.C.
Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003) [PubMed: 14500908] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSMZ 1740.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89215 Genomic DNA. Translation: CAA61503.1.
X83689 Genomic DNA. Translation: CAA58658.1.
BX571658 Genomic DNA. Translation: CAE09790.1. Different initiation.
PIRS74205.
RefSeqNP_906890.1. NC_005090.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WSAX-ray2.20A/B1-330[»]
ProteinModelPortalP50286.
SMRP50286. Positions 3-330.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2555338.
GenomeReviewsGene locus WS0660 in contig BX571656_GR.
KEGGwsu:WS0660.
NMPDRfig|273121.1.peg.617.
PATRIC24038396. VBIWolSuc63014_0628.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG497495.
ProtClustDBCLSK922838.

Enzyme and pathway databases

BioCycWSUC273121:WS0660-MONOMER.

Family and domain databases

InterProIPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_CS.
[Graphical view]
KOK01424.
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.
TIGRFAMsTIGR00520. AsnASE_II. 1 hit.
PROSITEPS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASPG_WOLSU
AccessionPrimary (citable) accession number: P50286
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 26, 2003
Last modified: January 25, 2012
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families