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Protein

L-asparaginase

Gene

ansB

Organism
Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei36 – 361O-isoaspartyl threonine intermediatePROSITE-ProRule annotation2 Publications
Binding sitei83 – 831Substrate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.5.1.1. 2141.

Names & Taxonomyi

Protein namesi
Recommended name:
L-asparaginase (EC:3.5.1.1)
Short name:
L-ASNase
Alternative name(s):
L-asparagine amidohydrolase
Gene namesi
Name:ansB
Synonyms:asn
OrganismiDickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Taxonomic identifieri556 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Pathology & Biotechi

Pharmaceutical usei

Available under the name Erwinase (Beaufour Ipsen). Used as an antineoplastic in chemotherapy. Reduces the quantity of asparagine available to cancer cells.

Protein family/group databases

Allergomei8366. Erw ch Asparaginase.

Chemistry

ChEMBLiCHEMBL1075190.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 348327L-asparaginasePRO_0000002358Add
BLAST

Interactioni

Subunit structurei

Homotetramer.3 Publications

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 359Combined sources
Helixi36 – 383Combined sources
Beta strandi42 – 454Combined sources
Beta strandi48 – 503Combined sources
Beta strandi51 – 533Combined sources
Helixi57 – 637Combined sources
Helixi65 – 695Combined sources
Beta strandi72 – 8110Combined sources
Helixi83 – 853Combined sources
Helixi88 – 10215Combined sources
Beta strandi109 – 1135Combined sources
Turni116 – 1183Combined sources
Helixi119 – 12911Combined sources
Beta strandi136 – 1394Combined sources
Helixi152 – 16413Combined sources
Helixi166 – 1683Combined sources
Beta strandi174 – 1774Combined sources
Beta strandi180 – 1834Combined sources
Turni184 – 1863Combined sources
Beta strandi191 – 1933Combined sources
Turni201 – 2033Combined sources
Beta strandi206 – 2105Combined sources
Beta strandi213 – 2164Combined sources
Beta strandi218 – 2225Combined sources
Helixi225 – 2273Combined sources
Beta strandi241 – 2455Combined sources
Helixi253 – 2608Combined sources
Beta strandi264 – 2718Combined sources
Turni272 – 2743Combined sources
Helixi278 – 28912Combined sources
Beta strandi293 – 30311Combined sources
Beta strandi311 – 3155Combined sources
Helixi321 – 33111Combined sources
Turni332 – 3343Combined sources
Helixi338 – 34710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HFJX-ray2.40A/C22-348[»]
1HFKX-ray2.17A/C22-348[»]
1HFWX-ray1.80A/B/C/D22-348[»]
1HG0X-ray1.90A/B/C/D22-348[»]
1HG1X-ray1.80A/B/C/D22-348[»]
1JSLX-ray1.70A/B/C/D22-348[»]
1JSRX-ray1.70A/B/C/D22-348[»]
1O7JX-ray1.00A/B/C/D22-348[»]
5F52X-ray1.63A/B/C/D23-348[»]
5HW0X-ray1.70A/B/C/D23-348[»]
ProteinModelPortaliP06608.
SMRiP06608. Positions 22-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06608.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 348323Asparaginase/glutaminasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni116 – 1172Substrate binding

Sequence similaritiesi

Belongs to the asparaginase 1 family.Curated
Contains 1 asparaginase/glutaminase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

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.
PS51732. ASN_GLN_ASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P06608-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERWFKSLFV LVLFFVFTAS AADKLPNIVI LATGGTIAGS AATGTQTTGY
60 70 80 90 100
KAGALGVDTL INAVPEVKKL ANVKGEQFSN MASENMTGDV VLKLSQRVNE
110 120 130 140 150
LLARDDVDGV VITHGTDTVE ESAYFLHLTV KSDKPVVFVA AMRPATAISA
160 170 180 190 200
DGPMNLLEAV RVAGDKQSRG RGVMVVLNDR IGSARYITKT NASTLDTFKA
210 220 230 240 250
NEEGYLGVII GNRIYYQNRI DKLHTTRSVF DVRGLTSLPK VDILYGYQDD
260 270 280 290 300
PEYLYDAAIQ HGVKGIVYAG MGAGSVSVRG IAGMRKAMEK GVVVIRSTRT
310 320 330 340
GNGIVPPDEE LPGLVSDSLN PAHARILLML ALTRTSDPKV IQEYFHTY
Length:348
Mass (Da):37,575
Last modified:January 1, 1988 - v1
Checksum:iC6A4C188E569D9A6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti177 – 1771L → I in strain: NCPPB 1125.
Natural varianti199 – 1991K → R in strain: NCPPB 1125.
Natural varianti288 – 2881M → L in strain: NCPPB 1125.
Natural varianti295 – 2951I → M in strain: NCPPB 1125.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14777 Genomic DNA. Translation: CAA32884.1.
X12746 Genomic DNA. Translation: CAA31239.1.
PIRiA26054.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14777 Genomic DNA. Translation: CAA32884.1.
X12746 Genomic DNA. Translation: CAA31239.1.
PIRiA26054.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HFJX-ray2.40A/C22-348[»]
1HFKX-ray2.17A/C22-348[»]
1HFWX-ray1.80A/B/C/D22-348[»]
1HG0X-ray1.90A/B/C/D22-348[»]
1HG1X-ray1.80A/B/C/D22-348[»]
1JSLX-ray1.70A/B/C/D22-348[»]
1JSRX-ray1.70A/B/C/D22-348[»]
1O7JX-ray1.00A/B/C/D22-348[»]
5F52X-ray1.63A/B/C/D23-348[»]
5HW0X-ray1.70A/B/C/D23-348[»]
ProteinModelPortaliP06608.
SMRiP06608. Positions 22-348.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL1075190.

Protein family/group databases

Allergomei8366. Erw ch Asparaginase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.5.1.1. 2141.

Miscellaneous databases

EvolutionaryTraceiP06608.

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.
PS51732. ASN_GLN_ASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of the Erwinia chrysanthemi NCPPB 1066 L-asparaginase gene."
    Minton N.P., Bullman H.M.S., Scawen M.D., Atkinson T., Gilbert H.J.
    Gene 46:25-35(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NCPPB 1066.
  2. "Sequence of L-asparaginase gene from Erwinia chrysanthemi NCPPB 1125."
    Filpula D., Nagle J.W., Pulford S., Anderson D.M.
    Nucleic Acids Res. 16:10385-10385(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NCPPB 1125.
  3. "Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi."
    Tanaka S., Robinson E.A., Appella E., Miller M., Ammon H.L., Roberts J., Weber I.T., Wlodawer A.
    J. Biol. Chem. 263:8583-8591(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  4. "A left-handed crossover involved in amidohydrolase catalysis. Crystal structure of Erwinia chrysanthemi L-asparaginase with bound L-aspartate."
    Miller M.M., Rao J.K.M., Wlodawer A., Gribskov M.R.
    FEBS Lett. 328:275-279(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ASPARTIC ACID, ACTIVE SITE, SUBUNIT.
  5. "Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase."
    Aghaiypour K., Wlodawer A., Lubkowski J.
    Biochemistry 40:5655-5664(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-348 IN COMPLEXES WITH GLUTAMIC ACID; ASPARTIC ACID AND SUCCINIC ACID.
  6. "Do bacterial L-asparaginases utilize a catalytic triad Thr-Tyr-Glu?"
    Aghaiypour K., Wlodawer A., Lubkowski J.
    Biochim. Biophys. Acta 1550:117-128(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-348 IN COMPLEX WITH INHIBITOR 6-DIAZO-5-OXY-NORLEUCINE, ACTIVE SITE.
  7. "Atomic resolution structure of Erwinia chrysanthemi L-asparaginase."
    Lubkowski J., Dauter M., Aghaiypour K., Wlodawer A., Dauter Z.
    Acta Crystallogr. D 59:84-92(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 22-348, SUBUNIT.

Entry informationi

Entry nameiASPG_DICCH
AccessioniPrimary (citable) accession number: P06608
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: July 6, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequence of strain NCPPB 1066 is shown.

Keywords - Technical termi

3D-structure, Pharmaceutical

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.