ECOLI:ASPG2

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	ansB
Protein Name(s)	L-asparaginase 2 L-asparaginase II L-ASNase II L-asparagine amidohydrolase II
External Links
UniProt	P00805
EMBL	M34277 M34234 U28377 U00096 AP009048
PIR	A35132
RefSeq	NP_417432.1 YP_491156.1
PDB	1HO3 1IHD 1JAZ 1JJA 1NNS 3ECA 4ECA
PDBsum	1HO3 1IHD 1JAZ 1JJA 1NNS 3ECA 4ECA
ProteinModelPortal	P00805
SMR	P00805
DIP	DIP-9110N
IntAct	P00805
STRING	511145.b2957
Allergome	8365
PaxDb	P00805
PRIDE	P00805
EnsemblBacteria	AAC75994 BAE77020
GeneID	12930249 947454
KEGG	ecj:Y75_p2887 eco:b2957
PATRIC	32121326
EchoBASE	EB0044
EcoGene	EG10046
eggNOG	COG0252
HOGENOM	HOG000044165
InParanoid	P00805
KO	K01424
OMA	FQSPNFG
OrthoDB	EOG6VTK47
PhylomeDB	P00805
BioCyc	EcoCyc:ANSB-MONOMER ECOL316407:JW2924-MONOMER MetaCyc:ANSB-MONOMER
SABIO-RK	P00805
EvolutionaryTrace	P00805
PRO	PR:P00805
Proteomes	UP000000318 UP000000625
Genevestigator	P00805
GO	GO:0005829 GO:0030288 GO:0004067 GO:0042802 GO:0006528
Gene3D	3.40.50.1170 3.40.50.40
InterPro	IPR004550 IPR006034 IPR020827 IPR027475 IPR027473 IPR027474
Pfam	PF00710
PIRSF	PIRSF001220
PRINTS	PR00139
SMART	SM00870
SUPFAM	SSF53774
TIGRFAMs	TIGR00520
PROSITE	PS00144 PS00917 PS51732

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
part_of	GO:0042597	periplasmic space	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10046 PANTHER:PTN000194668 SGD:S000004145 SGD:S000004147 SGD:S000004148 SGD:S000004150	C	Seeded From UniProt	complete
involved_in	GO:0006530	asparagine catabolic process	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000194668 SGD:S000002729 SGD:S000004145 SGD:S000004147 SGD:S000004148 SGD:S000004150	P	Seeded From UniProt	complete
enables	GO:0004067	asparaginase activity	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10046 PANTHER:PTN000194668 SGD:S000002729 SGD:S000004145 SGD:S000004147 SGD:S000004148 SGD:S000004150	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25040257^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00805	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16858726^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00805	F	Seeded From UniProt	complete
involved_in	GO:0051289	protein homotetramerization	PMID:8434007^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	PMID:4962587^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	PMID:24140104^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	PMID:15911532^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004067	asparaginase activity	PMID:1821783^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004067	asparaginase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004550	F	Seeded From UniProt	complete
involved_in	GO:0006520	cellular amino acid metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020827	P	Seeded From UniProt	complete
involved_in	GO:0006528	asparagine metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004550	P	Seeded From UniProt	complete
enables	GO:0004067	asparaginase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.5.1.1	F	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
part_of	GO:0042597	periplasmic space	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0574 UniProtKB-SubCell:SL-0200	C	Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Borek, D et al. (2014) Crystal structure of active site mutant of antileukemic L-asparaginase reveals conserved zinc-binding site. FEBS J. 281 4097-111 PubMed GONUTS page
↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
↑ Swain, AL et al. (1993) Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy. Proc. Natl. Acad. Sci. U.S.A. 90 1474-8 PubMed GONUTS page
↑ Cedar, H & Schwartz, JH (1967) Localization of the two-L-asparaginases in anaerobically grown Escherichia coli. J. Biol. Chem. 242 3753-5 PubMed GONUTS page
↑ Han, MJ et al. (2014) Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains. J. Biosci. Bioeng. 117 437-42 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
↑ Harms, E et al. () Construction of expression systems for Escherichia coli asparaginase II and two-step purification of the recombinant enzyme from periplasmic extracts. Protein Expr. Purif. 2 144-50 PubMed GONUTS page

[PMID:21873635-1] 1.0 ^1.1 ^1.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:25040257-2] Borek, D et al. (2014) Crystal structure of active site mutant of antileukemic L-asparaginase reveals conserved zinc-binding site. FEBS J. 281 4097-111 PubMed GONUTS page

[PMID:16858726-3] Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page

[PMID:8434007-4] Swain, AL et al. (1993) Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy. Proc. Natl. Acad. Sci. U.S.A. 90 1474-8 PubMed GONUTS page

[PMID:4962587-5] Cedar, H & Schwartz, JH (1967) Localization of the two-L-asparaginases in anaerobically grown Escherichia coli. J. Biol. Chem. 242 3753-5 PubMed GONUTS page

[PMID:24140104-6] Han, MJ et al. (2014) Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains. J. Biosci. Bioeng. 117 437-42 PubMed GONUTS page

[PMID:15911532-7] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:1821783-8] Harms, E et al. () Construction of expression systems for Escherichia coli asparaginase II and two-step purification of the recombinant enzyme from periplasmic extracts. Protein Expr. Purif. 2 144-50 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

ECOLI:ASPG2

Contents

Annotations

Notes

References

a

b

e

g

h

i

o

p

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools