P06608 (ASPG_ERWCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-asparaginase
Short name=L-ASNase
EC=3.5.1.1

Alternative name(s):
L-asparagine amidohydrolase

Gene names

Name:	ansB
Synonyms:	asn

Organism

Erwinia chrysanthemi

Taxonomic identifier

556 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-asparagine + H2O = L-aspartate + NH3.
Subunit structure	Homotetramer. Ref.4 Ref.7
Pharmaceutical use	Available under the name Erwinase (Beaufour Ipsen). Used as an antineoplastic in chemotherapy. Reduces the quantity of asparagine available to cancer cells.
Miscellaneous	The sequence of strain NCPPB 1066 is shown.
Sequence similarities	Belongs to the asparaginase 1 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Hydrolase
Technical term	3D-structure Pharmaceutical
Gene Ontology (GO)
Biological process	asparagine metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	asparaginase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Chain

22 – 348

327

L-asparaginase

PRO_0000002358

Regions

Region

116 – 117

2

Substrate binding

Sites

Active site

36

1

O-isoaspartyl threonine intermediate Ref.4 Ref.6

Binding site

83

1

Substrate

Natural variations

Natural variant

177

1

L → I in strain: NCPPB 1125.

Natural variant

199

1

K → R in strain: NCPPB 1125.

Natural variant

288

1

M → L in strain: NCPPB 1125.

Natural variant

295

1

I → M in strain: NCPPB 1125.

Secondary structure

1

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348

Helix Strand Turn

Details...

Beta strand

27 – 35

9

Helix

36 – 38

3

Helix

57 – 63

7

Helix

65 – 69

5

Beta strand

72 – 81

10

Helix

83 – 85

3

Helix

88 – 102

15

Beta strand

109 – 113

5

Helix

119 – 129

11

Beta strand

136 – 139

4

Helix

152 – 164

13

Helix

166 – 168

3

Beta strand

174 – 177

4

Beta strand

180 – 183

4

Turn

184 – 186

3

Beta strand

191 – 193

3

Turn

201 – 203

3

Beta strand

206 – 210

5

Beta strand

213 – 216

4

Beta strand

218 – 222

5

Helix

225 – 227

3

Beta strand

241 – 245

5

Helix

253 – 260

8

Beta strand

264 – 271

8

Turn

272 – 274

3

Helix

278 – 289

12

Beta strand

293 – 303

11

Beta strand

311 – 315

5

Helix

321 – 331

11

Turn

332 – 334

3

Helix

338 – 347

10

Sequences

	Sequence		Length	Mass (Da)
	P06608 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: C6A4C188E569D9A6	FASTA	348	37,575
	10 20 30 40 50 60 MERWFKSLFV LVLFFVFTAS AADKLPNIVI LATGGTIAGS AATGTQTTGY KAGALGVDTL 70 80 90 100 110 120 INAVPEVKKL ANVKGEQFSN MASENMTGDV VLKLSQRVNE LLARDDVDGV VITHGTDTVE 130 140 150 160 170 180 ESAYFLHLTV KSDKPVVFVA AMRPATAISA DGPMNLLEAV RVAGDKQSRG RGVMVVLNDR 190 200 210 220 230 240 IGSARYITKT NASTLDTFKA NEEGYLGVII GNRIYYQNRI DKLHTTRSVF DVRGLTSLPK 250 260 270 280 290 300 VDILYGYQDD PEYLYDAAIQ HGVKGIVYAG MGAGSVSVRG IAGMRKAMEK GVVVIRSTRT 310 320 330 340 GNGIVPPDEE LPGLVSDSLN PAHARILLML ALTRTSDPKV IQEYFHTY

References

[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: 3026924] [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: 3194219] [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: 3379033] [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: 8348975] [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: 11341830] [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: 11755201] [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: 12499544] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 22-348, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X14777 Genomic DNA. Translation: CAA32884.1.
X12746 Genomic DNA. Translation: CAA31239.1.

PIR

A26054.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HFJ	X-ray	2.40	A/C	22-348	[»]
1HFK	X-ray	2.17	A/C	22-348	[»]
1HFW	X-ray	1.80	A/B/C/D	22-348	[»]
1HG0	X-ray	1.90	A/B/C/D	22-348	[»]
1HG1	X-ray	1.80	A/B/C/D	22-348	[»]
1JSL	X-ray	1.70	A/B/C/D	22-348	[»]
1JSR	X-ray	1.70	A/B/C/D	22-348	[»]
1O7J	X-ray	1.00	A/B/C/D	22-348	[»]

ProteinModelPortal

P06608.

SMR

P06608. Positions 22-348.

ModBase

Search...

Protein family/group databases

Allergome

8366. Erw ch Asparaginase.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_CS.
[Graphical view]

PANTHER

PTHR11707. Asp/Glutamnse. 1 hit.

Pfam

PF00710. Asparaginase. 1 hit.
[Graphical view]

PIRSF

PIRSF001220. L-ASNase_gatD. 1 hit.

PRINTS

PR00139. ASNGLNASE.

SMART

SM00870. Asparaginase. 1 hit.
[Graphical view]

SUPFAM

SSF53774. Asp/Glutamnse. 1 hit.

TIGRFAMs

TIGR00520. AsnASE_II. 1 hit.

PROSITE

PS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ASPG_ERWCH

Accession

Primary (citable) accession number: P06608

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	July 27, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program