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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)DescriptionActionsGraphical viewLength
Active sitei36O-isoaspartyl threonine intermediatePROSITE-ProRule annotation2 Publications1
Binding sitei83Substrate1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesPectobacteriaceaeDickeya

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 databases

ChEMBLiCHEMBL1075190.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Add BLAST21
ChainiPRO_000000235822 – 348L-asparaginaseAdd BLAST327

Proteomic databases

PRIDEiP06608.

Interactioni

Subunit structurei

Homotetramer.3 Publications

Structurei

Secondary structure

1348
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 35Combined sources9
Helixi36 – 38Combined sources3
Beta strandi42 – 45Combined sources4
Beta strandi48 – 50Combined sources3
Beta strandi51 – 54Combined sources4
Helixi57 – 63Combined sources7
Helixi65 – 69Combined sources5
Beta strandi72 – 81Combined sources10
Helixi83 – 85Combined sources3
Helixi88 – 102Combined sources15
Beta strandi109 – 113Combined sources5
Turni116 – 118Combined sources3
Helixi119 – 129Combined sources11
Beta strandi136 – 139Combined sources4
Helixi152 – 164Combined sources13
Helixi166 – 168Combined sources3
Beta strandi174 – 177Combined sources4
Beta strandi180 – 183Combined sources4
Turni184 – 186Combined sources3
Beta strandi191 – 193Combined sources3
Turni201 – 203Combined sources3
Beta strandi206 – 210Combined sources5
Beta strandi213 – 216Combined sources4
Beta strandi218 – 222Combined sources5
Helixi225 – 227Combined sources3
Beta strandi241 – 245Combined sources5
Helixi253 – 260Combined sources8
Beta strandi264 – 271Combined sources8
Turni272 – 274Combined sources3
Helixi278 – 289Combined sources12
Beta strandi293 – 303Combined sources11
Beta strandi311 – 315Combined sources5
Helixi321 – 331Combined sources11
Turni332 – 334Combined sources3
Helixi338 – 347Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5I3ZX-ray2.05A/B/C/D23-348[»]
5I48X-ray1.50A/B/C/D23-348[»]
5I4BX-ray1.60A/B/C23-348[»]
ProteinModelPortaliP06608.
SMRiP06608.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06608.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 348Asparaginase/glutaminasePROSITE-ProRule annotationAdd BLAST323

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni116 – 117Substrate binding2

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)DescriptionActionsGraphical viewLength
Natural varianti177L → I in strain: NCPPB 1125. 1
Natural varianti199K → R in strain: NCPPB 1125. 1
Natural varianti288M → L in strain: NCPPB 1125. 1
Natural varianti295I → M in strain: NCPPB 1125. 1

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
PDB 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[»]
5I3ZX-ray2.05A/B/C/D23-348[»]
5I48X-ray1.50A/B/C/D23-348[»]
5I4BX-ray1.60A/B/C23-348[»]
ProteinModelPortaliP06608.
SMRiP06608.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL1075190.

Protein family/group databases

Allergomei8366. Erw ch Asparaginase.

Proteomic databases

PRIDEiP06608.

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...

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: November 2, 2016
This is version 97 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.