Reviewed, UniProtKB/Swiss-Prot P0A962 (ASPG1_ECOLI)

Names and origin

Protein names

Recommended name:
    L-asparaginase 1
    EC=3.5.1.1
Alternative name(s):
    L-asparaginase I
      Short name=L-ASNase I
    L-asparagine amidohydrolase I

Gene names

Name:	ansA
Ordered Locus Names:	b1767, JW1756

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-asparagine + H2O = L-aspartate + NH3.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
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=3.5 mM for L-asparagine

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	amino acid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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

Chain

1 – 338

338

L-asparaginase 1

PRO_0000171079

Sites

Active site

14

1

By similarity

Active site

91

1

By similarity

Active site

92

1

By similarity

Active site

163

1

By similarity

Secondary structure

1

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338

Helix Strand Turn

Details...

Beta strand

5 – 13

9

Helix

14 – 16

3

Helix

30 – 35

6

Helix

39 – 42

4

Beta strand

48 – 58

11

Helix

60 – 62

3

Helix

65 – 78

14

Helix

79 – 81

3

Beta strand

83 – 88

6

Helix

94 – 104

11

Beta strand

112 – 115

4

Helix

128 – 141

14

Beta strand

145 – 151

7

Beta strand

154 – 157

4

Helix

158 – 160

3

Beta strand

168 – 170

3

Beta strand

180 – 189

10

Beta strand

212 – 216

5

Helix

224 – 229

6

Beta strand

231 – 233

3

Beta strand

235 – 242

8

Turn

243 – 245

3

Helix

251 – 262

12

Beta strand

266 – 275

10

Helix

288 – 291

4

Helix

302 – 314

13

Helix

319 – 326

8

Beta strand

330 – 334

5

Sequences

	Sequence		Length	Mass (Da)
	P0A962-1 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 75D97E6D10E9F8DA	FASTA	338	37,127
	10 20 30 40 50 60 MQKKSIYVAY TGGTIGMQRS EQGYIPVSGH LQRQLALMPE FHRPEMPDFT IHEYTPLMDS 70 80 90 100 110 120 SDMTPEDWQH IAEDIKAHYD DYDGFVILHG TDTMAYTASA LSFMLENLGK PVIVTGSQIP 130 140 150 160 170 180 LAELRSDGQI NLLNALYVAA NYPINEVTLF FNNRLYRGNR TTKAHADGFD AFASPNLPPL 190 200 210 220 230 240 LEAGIHIRRL NTPPAPHGEG ELIVHPITPQ PIGVVTIYPG ISADVVRNFL RQPVKALILR 250 260 270 280 290 300 SYGVGNAPQN KAFLQELQEA SDRGIVVVNL TQCMSGKVNM GGYATGNALA HAGVIGGADM 310 320 330 TVEATLTKLH YLLSQELDTE TIRKAMSQNL RGELTPDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression in Escherichia coli K-12 of the L-asparaginase I-encoding ansA gene and its flanking regions." Jerlstroem P.G., Bezjak D.A., Jennings M.P., Beacham I.R. Gene 78:37-46(1989) [PubMed: 2670682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M26934 Genomic DNA. Translation: AAA23446.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74837.1.
AP009048 Genomic DNA. Translation: BAA15558.1.

PIR

XDEC1. G64936.

RefSeq

AP_002386.1.
NP_416281.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HIM	X-ray	1.82	A/B/C/D	1-338	[»]
2P2D	X-ray	1.89	A/B/C/D	1-338	[»]
2P2N	X-ray	1.90	A/B/C/D	1-338	[»]

ModBase

Search...

Genome annotation databases

GeneID

946278.

GenomeReviews

Gene locus JW1756 in contig AP009048_GR.
Gene locus b1767 in contig U00096_GR.

KEGG

ecj:JW1756.
eco:b1767.

Organism-specific databases

EchoBASE

EB0043.

EcoGene

EG10045. ansA.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A962.

OMA

P0A962. ISGHDMT.

Enzyme and pathway databases

BioCyc

EcoCyc:ANSA-MON.
MetaCyc:ANSA-MON.

Family and domain databases

InterPro

IPR006033. AsnASEI.
IPR006034. Asp/Glutamnse.
[Graphical view]

PANTHER

PTHR11707. Asp/Glutamnse. 1 hit.

Pfam

PF00710. Asparaginase. 1 hit.
[Graphical view]

PRINTS

PR00139. ASNGLNASE.

ProDom

PD003221. Asp/Glutamnse. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00519. asnASE_I. 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

ASPG1_ECOLI

Accession

Primary (citable) accession number: P0A962
Secondary accession number(s): P18840

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)