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Reviewed, UniProtKB/Swiss-Prot P00805 (ASPG2_ECOLI)

Last modified November 3, 2009. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    L-asparaginase 2
    EC=3.5.1.1
Alternative name(s):
    L-asparaginase II
      Short name=L-ASNase II
    L-asparagine amidohydrolase II
    INN=Colaspase
Gene names
Name: ansB
Ordered Locus Names: b2957, JW2924
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homotetramer. Ref.8

Subcellular location

Periplasm.

Induction

By cAMP and anaerobiosis.

Pharmaceutical use

Available under the names Crastinin (Bayer), Elspar (Merck), Kidrolase (Rhone-Poulenc) and Leunase (Kyowa). Also available as a PEG-conjugated form (Pegaspargase) under the name Oncaspar (Enzon). Used as an antineoplastic in chemotherapy. Reduces the quantity of asparagine available to cancer cells.

Miscellaneous

E.coli contains two L-asparaginase isoenzymes: L-asparaginase I, a low-affinity enzyme located in the cytoplasm, and L-asparaginase II, a high-affinity secreted enzyme.

Sequence similarities

Belongs to the asparaginase 1 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.115 µM for L-asparagine

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Gene Ontology (GO)
   Biological processasparagine metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol

Inferred from direct assay. Source: UniProtKB

periplasmic space

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

Signal peptide1 – 2222 Ref.5
Chain23 – 348326L-asparaginase 2
PRO_0000002356

Sites

Active site341 Ref.7 Ref.9
Active site1111 By similarity
Active site1121 By similarity
Active site1841 By similarity
Binding site1411Substrate

Amino acid modifications

Disulfide bond99 ↔ 127 Ref.12

Experimental info

Mutagenesis341T → A: Almost no activity. Ref.10 Ref.11
Sequence conflict491V → A AA sequence Ref.5
Sequence conflict861N → D AA sequence Ref.5
Sequence conflict1321Missing AA sequence Ref.5
Sequence conflict1561Missing AA sequence Ref.5
Sequence conflict1711Missing AA sequence Ref.5
Sequence conflict2061N → D AA sequence Ref.5
Sequence conflict2681N → D AA sequence Ref.5
Sequence conflict2741S → T AA sequence Ref.5
Sequence conflict2851T → D AA sequence Ref.5
Sequence conflict2901Missing AA sequence Ref.5
Sequence conflict3301Missing AA sequence Ref.5

Secondary structure

.............................................................. 348
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00805-1 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 2076987C0E8B2F99

FASTA34836,851
        10         20         30         40         50         60 
MEFFKKTALA ALVMGFSGAA LALPNITILA TGGTIAGGGD SATKSNYTVG KVGVENLVNA 

        70         80         90        100        110        120 
VPQLKDIANV KGEQVVNIGS QDMNDNVWLT LAKKINTDCD KTDGFVITHG TDTMEETAYF 

       130        140        150        160        170        180 
LDLTVKCDKP VVMVGAMRPS TSMSADGPFN LYNAVVTAAD KASANRGVLV VMNDTVLDGR 

       190        200        210        220        230        240 
DVTKTNTTDV ATFKSVNYGP LGYIHNGKID YQRTPARKHT SDTPFDVSKL NELPKVGIVY 

       250        260        270        280        290        300 
NYANASDLPA KALVDAGYDG IVSAGVGNGN LYKSVFDTLA TAAKTGTAVV RSSRVPTGAT 

       310        320        330        340 
TQDAEVDDAK YGFVASGTLN PQKARVLLQL ALTQTKDPQQ IQQIFNQY 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins."
Jennings M.P., Beacham I.R.
J. Bacteriol. 172:1491-1498(1990) [PubMed: 2407723] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"L-asparaginase II of Escherichia coli K-12: cloning, mapping and sequencing of the ansB gene."
Bonthron D.T.
Gene 91:101-105(1990) [PubMed: 2144836] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The primary structure of L-asparaginase from Escherichia coli."
Maita T., Matsuda G.
Hoppe-Seyler's Z. Physiol. Chem. 361:105-117(1980) [PubMed: 6766894] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-348.
[6]"Amino acid sequences of the tryptic peptides from carboxymethylated L-asparaginase from Escherichia coli."
Maita T., Morokuma K., Matsuda G.
Hoppe-Seyler's Z. Physiol. Chem. 360:1483-1495(1979) [PubMed: 387570] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[7]"Structure of peptide from active site region of Escherichia coli L-asparaginase."
Peterson R.G., Richards F.F., Handschumacher R.E.
J. Biol. Chem. 252:2072-2076(1977) [PubMed: 321449] [Abstract]
Cited for: ACTIVE SITE.
[8]"Chemical evidence for identical subunits in L-asparaginase from Escherichia coli B."
Greenquist A.C., Wriston J.C. Jr.
Arch. Biochem. Biophys. 152:280-286(1972) [PubMed: 4561256] [Abstract]
Cited for: SUBUNIT.
[9]"A catalytic role for threonine-12 of E. coli asparaginase II as established by site-directed mutagenesis."
Harms E., Wehner A., Aung H.P., Roehm K.H.
FEBS Lett. 285:55-58(1991) [PubMed: 1906013] [Abstract]
Cited for: ACTIVE SITE THR-34.
[10]"Site-specific mutagenesis of Escherichia coli asparaginase II. None of the three histidine residues is required for catalysis."
Wehner A., Harms E., Jennings M.P., Beacham I.R., Derst C., Bast P., Roehm K.H.
Eur. J. Biochem. 208:475-480(1992) [PubMed: 1521538] [Abstract]
Cited for: MUTAGENESIS OF HISTIDINE RESIDUES.
[11]"Probing the role of threonine and serine residues of E. coli asparaginase II by site-specific mutagenesis."
Ders C., Henseling J., Roehm K.H.
Protein Eng. 5:785-789(1992) [PubMed: 1287659] [Abstract]
Cited for: MUTAGENESIS OF THREONINE AND SERINE RESIDUES.
[12]"Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy."
Swain A.L., Jaskolski M., Housset D., Rao J.K.M., Wlodawer A.
Proc. Natl. Acad. Sci. U.S.A. 90:1474-1478(1993) [PubMed: 8434007] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[13]"A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant."
Palm G.J., Lubkowski J., Derst C., Schleper S., Roehm K.H., Wlodawer A.
FEBS Lett. 390:211-216(1996) [PubMed: 8706862] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT VAL-111.
+Additional computationally mapped references.

Cross-references

Sequence databases

M34277 Genomic DNA. Translation: AAA24062.1.
M34234 Genomic DNA. Translation: AAA23445.1.
U28377 Genomic DNA. Translation: AAA69124.1.
U00096 Genomic DNA. Translation: AAC75994.1.
AP009048 Genomic DNA. Translation: BAE77020.1.
PIRXDEC. A35132.
RefSeqAP_003514.1.
NP_417432.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1HO3X-ray2.50A/B23-348[»]
1IHDX-ray2.65A/C23-348[»]
1JAZX-ray2.27A/B23-348[»]
1JJAX-ray2.30A/B/C/D/E/F23-348[»]
1NNSX-ray1.95A/B23-348[»]
3ECAX-ray2.40A/B/C/D23-348[»]
4ECAX-ray2.20A/B/C/D23-348[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:9110N.
STRINGP00805.

Genome annotation databases

GeneID947454.
GenomeReviewsGene locus JW2924 in contig AP009048_GR.
Gene locus b2957 in contig U00096_GR.
KEGGecj:JW2924.
eco:b2957.

Organism-specific databases

EchoBASEEB0044.
EcoGeneEG10046. ansB.
CMRSearch...

Phylogenomic databases

HOGENOMP00805.
OMANFGPLGY.

Enzyme and pathway databases

BioCycEcoCyc:ANSB-MON.
MetaCyc:ANSB-MON.

Gene expression databases

GenevestigatorP00805.

Family and domain databases

InterProIPR004550. AsnASE_II.
IPR006034. Asp/Glutamnse.
[Graphical view]
PANTHERPTHR11707. Asp/Glutamnse. 1 hit.
PfamPF00710. Asparaginase. 1 hit.
[Graphical view]
PRINTSPR00139. ASNGLNASE.
ProDomPD003221. Asp/Glutamnse. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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 nameASPG2_ECOLI
AccessionPrimary (citable) accession number: P00805
Secondary accession number(s): Q2M9N6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: November 3, 2009
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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