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P00805 (ASPG2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference 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. Ref.13

Subunit structure

Homotetramer. Ref.8 Ref.9 Ref.12 Ref.13 Ref.14

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Region80 – 812Substrate binding
Region111 – 1122Substrate binding

Sites

Active site341O-isoaspartyl threonine intermediate Ref.7 Ref.9 Ref.13

Amino acid modifications

Disulfide bond99 ↔ 127 Ref.12 Ref.13

Experimental info

Mutagenesis341T → A: Loss of enzyme activity. Ref.9 Ref.10 Ref.11
Mutagenesis1111T → S: Reduced enzyme activity. Ref.10 Ref.11 Ref.13
Mutagenesis1111T → V: Loss of enzyme activity. Ref.10 Ref.11 Ref.13
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 [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] [Europe PMC] [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] [Europe PMC] [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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE THR-34, MUTAGENESIS OF THR-34, SUBUNIT.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ASPARTIC ACID, DISULFIDE BOND, SUBUNIT.
[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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT VAL-111, ACTIVE SITE, MUTAGENESIS OF THR-111, CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BOND.
[14]"Structural comparison of Escherichia coli L-asparaginase in two monoclinic space groups."
Sanches M., Barbosa J.A., de Oliveira R.T., Abrahao Neto J., Polikarpov I.
Acta Crystallogr. D 59:416-422(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 23-348 IN COMPLEXES WITH ASPARTIC ACID, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_417432.1. NC_000913.3.
YP_491156.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP00805.
SMRP00805. Positions 23-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9110N.
IntActP00805. 7 interactions.
STRING511145.b2957.

Protein family/group databases

Allergome8365. Esc c Asparaginase.

Proteomic databases

PaxDbP00805.
PRIDEP00805.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75994; AAC75994; b2957.
BAE77020; BAE77020; BAE77020.
GeneID12930249.
947454.
KEGGecj:Y75_p2887.
eco:b2957.
PATRIC32121326. VBIEscCol129921_3051.

Organism-specific databases

EchoBASEEB0044.
EcoGeneEG10046. ansB.

Phylogenomic databases

eggNOGCOG0252.
HOGENOMHOG000044165.
KOK01424.
OMAIDDKAYG.
OrthoDBEOG6VTK47.
PhylomeDBP00805.
ProtClustDBPRK11096.

Enzyme and pathway databases

BioCycEcoCyc:ANSB-MONOMER.
ECOL316407:JW2924-MONOMER.
MetaCyc:ANSB-MONOMER.
SABIO-RKP00805.

Gene expression databases

GenevestigatorP00805.

Family and domain databases

Gene3D3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProIPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_AS1.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view]
PfamPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFPIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSPR00139. ASNGLNASE.
SMARTSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMSSF53774. SSF53774. 1 hit.
TIGRFAMsTIGR00520. asnASE_II. 1 hit.
PROSITEPS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00805.
PROP00805.

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: April 16, 2014
This is version 145 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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