Reviewed, UniProtKB/Swiss-Prot P0A963 (ASPG1_ECO57)

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:	Z2801, ECs2474

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	L-asparagine + H2O = L-aspartate + NH3.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular 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_0000171080
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

Sequences

	Sequence		Length	Mass (Da)
	P0A963-1 [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

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG56754.1. BA000007 Genomic DNA. Translation: BAB35897.1.
PIR	B90938.
RefSeq	NP_288201.1. NP_310501.1.
3D structure databases
SMR	P0A963. Positions 2-337.
ModBase	Search...
Genome annotation databases
GeneID	916909. 961739.
GenomeReviews	Gene locus Z2801 in contig AE005174_GR. Gene locus ECs2474 in contig BA000007_GR.
KEGG	ece:Z2801. ecs:ECs2474.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG497495.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS2474-MONOMER.
Family and domain databases
InterPro	IPR006033. AsnASEI. IPR006034. Asparaginase/glutaminase. IPR020827. Asparaginase/glutaminase_CS. [Graphical view]
PANTHER	PTHR11707. Asp/Glutamnse. 1 hit.
Pfam	PF00710. Asparaginase. 1 hit. [Graphical view]
PRINTS	PR00139. ASNGLNASE.
SMART	SM00870. Asparaginase. 1 hit. [Graphical view]
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_ECO57

Accession

Primary (citable) accession number: P0A963
Secondary accession number(s): P18840

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	February 9, 2010
This is version 33 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)