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P00805

- ASPG2_ECOLI

UniProt

P00805 - ASPG2_ECOLI

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Protein
L-asparaginase 2
Gene
ansB, b2957, JW2924
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-asparagine + H2O = L-aspartate + NH3.1 Publication

Kineticsi

  1. KM=0.115 µM for L-asparagine

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei34 – 341O-isoaspartyl threonine intermediate3 Publications

GO - Molecular functioni

  1. asparaginase activity Source: EcoCyc

GO - Biological processi

  1. asparagine metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ansB
Ordered Locus Names:b2957, JW2924
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10046. ansB.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Pharmaceutical usei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341T → A: Loss of enzyme activity. 3 Publications
Mutagenesisi111 – 1111T → S: Reduced enzyme activity. 3 Publications
Mutagenesisi111 – 1111T → V: Loss of enzyme activity. 3 Publications

Protein family/group databases

Allergomei8365. Esc c Asparaginase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 Publication
Add
BLAST
Chaini23 – 348326L-asparaginase 2
PRO_0000002356Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi99 ↔ 1272 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP00805.
PRIDEiP00805.

Expressioni

Inductioni

By cAMP and anaerobiosis.

Gene expression databases

GenevestigatoriP00805.

Interactioni

Subunit structurei

Homotetramer.5 Publications

Protein-protein interaction databases

DIPiDIP-9110N.
IntActiP00805. 7 interactions.
STRINGi511145.b2957.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 339
Helixi34 – 363
Beta strandi42 – 443
Beta strandi48 – 503
Helixi54 – 596
Helixi62 – 665
Beta strandi69 – 7810
Helixi80 – 823
Helixi85 – 9814
Helixi99 – 1013
Beta strandi103 – 1086
Beta strandi111 – 1133
Helixi114 – 12411
Beta strandi131 – 1344
Helixi147 – 15913
Helixi161 – 1633
Beta strandi168 – 1725
Beta strandi175 – 1784
Turni179 – 1813
Beta strandi182 – 1843
Beta strandi186 – 1883
Beta strandi193 – 1953
Turni196 – 1983
Beta strandi201 – 2055
Beta strandi208 – 2114
Helixi220 – 2223
Beta strandi236 – 2405
Helixi248 – 2558
Beta strandi259 – 2668
Turni267 – 2693
Helixi273 – 28412
Beta strandi288 – 29811
Beta strandi302 – 3065
Helixi308 – 3114
Beta strandi313 – 3153
Helixi321 – 33111
Turni332 – 3343
Helixi338 – 3458

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP00805.
SMRiP00805. Positions 23-348.

Miscellaneous databases

EvolutionaryTraceiP00805.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni80 – 812Substrate binding
Regioni111 – 1122Substrate binding

Sequence similaritiesi

Belongs to the asparaginase 1 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0252.
HOGENOMiHOG000044165.
KOiK01424.
OMAiADISGEQ.
OrthoDBiEOG6VTK47.
PhylomeDBiP00805.

Family and domain databases

Gene3Di3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProiIPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_AS1.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view]
PfamiPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFiPIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSiPR00139. ASNGLNASE.
SMARTiSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMiSSF53774. SSF53774. 1 hit.
TIGRFAMsiTIGR00520. asnASE_II. 1 hit.
PROSITEiPS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00805-1 [UniParc]FASTAAdd to Basket

« Hide

MEFFKKTALA ALVMGFSGAA LALPNITILA TGGTIAGGGD SATKSNYTVG    50
KVGVENLVNA VPQLKDIANV KGEQVVNIGS QDMNDNVWLT LAKKINTDCD 100
KTDGFVITHG TDTMEETAYF LDLTVKCDKP VVMVGAMRPS TSMSADGPFN 150
LYNAVVTAAD KASANRGVLV VMNDTVLDGR DVTKTNTTDV ATFKSVNYGP 200
LGYIHNGKID YQRTPARKHT SDTPFDVSKL NELPKVGIVY NYANASDLPA 250
KALVDAGYDG IVSAGVGNGN LYKSVFDTLA TAAKTGTAVV RSSRVPTGAT 300
TQDAEVDDAK YGFVASGTLN PQKARVLLQL ALTQTKDPQQ IQQIFNQY 348
Length:348
Mass (Da):36,851
Last modified:November 1, 1990 - v2
Checksum:i2076987C0E8B2F99
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491V → A AA sequence 1 Publication
Sequence conflicti86 – 861N → D AA sequence 1 Publication
Sequence conflicti132 – 1321Missing AA sequence 1 Publication
Sequence conflicti156 – 1561Missing AA sequence 1 Publication
Sequence conflicti171 – 1711Missing AA sequence 1 Publication
Sequence conflicti206 – 2061N → D AA sequence 1 Publication
Sequence conflicti268 – 2681N → D AA sequence 1 Publication
Sequence conflicti274 – 2741S → T AA sequence 1 Publication
Sequence conflicti285 – 2851T → D AA sequence 1 Publication
Sequence conflicti290 – 2901Missing AA sequence 1 Publication
Sequence conflicti330 – 3301Missing AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA35132. XDEC.
RefSeqiNP_417432.1. NC_000913.3.
YP_491156.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75994; AAC75994; b2957.
BAE77020; BAE77020; BAE77020.
GeneIDi12930249.
947454.
KEGGiecj:Y75_p2887.
eco:b2957.
PATRICi32121326. VBIEscCol129921_3051.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A35132. XDEC.
RefSeqi NP_417432.1. NC_000913.3.
YP_491156.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HO3 X-ray 2.50 A/B 23-348 [» ]
1IHD X-ray 2.65 A/C 23-348 [» ]
1JAZ X-ray 2.27 A/B 23-348 [» ]
1JJA X-ray 2.30 A/B/C/D/E/F 23-348 [» ]
1NNS X-ray 1.95 A/B 23-348 [» ]
3ECA X-ray 2.40 A/B/C/D 23-348 [» ]
4ECA X-ray 2.20 A/B/C/D 23-348 [» ]
ProteinModelPortali P00805.
SMRi P00805. Positions 23-348.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9110N.
IntActi P00805. 7 interactions.
STRINGi 511145.b2957.

Protein family/group databases

Allergomei 8365. Esc c Asparaginase.

Proteomic databases

PaxDbi P00805.
PRIDEi P00805.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75994 ; AAC75994 ; b2957 .
BAE77020 ; BAE77020 ; BAE77020 .
GeneIDi 12930249.
947454.
KEGGi ecj:Y75_p2887.
eco:b2957.
PATRICi 32121326. VBIEscCol129921_3051.

Organism-specific databases

EchoBASEi EB0044.
EcoGenei EG10046. ansB.

Phylogenomic databases

eggNOGi COG0252.
HOGENOMi HOG000044165.
KOi K01424.
OMAi ADISGEQ.
OrthoDBi EOG6VTK47.
PhylomeDBi P00805.

Enzyme and pathway databases

BioCyci EcoCyc:ANSB-MONOMER.
ECOL316407:JW2924-MONOMER.
MetaCyc:ANSB-MONOMER.
SABIO-RK P00805.

Miscellaneous databases

EvolutionaryTracei P00805.
PROi P00805.

Gene expression databases

Genevestigatori P00805.

Family and domain databases

Gene3Di 3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProi IPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_AS1.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view ]
Pfami PF00710. Asparaginase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSi PR00139. ASNGLNASE.
SMARTi SM00870. Asparaginase. 1 hit.
[Graphical view ]
SUPFAMi SSF53774. SSF53774. 1 hit.
TIGRFAMsi TIGR00520. asnASE_II. 1 hit.
PROSITEi PS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiASPG2_ECOLI
AccessioniPrimary (citable) accession number: P00805
Secondary accession number(s): Q2M9N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: May 14, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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