ECOLI:ASSY

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	argG
Protein Name(s)	Argininosuccinate synthase Citrulline--aspartate ligase
External Links
UniProt	P0A6E4
EMBL	M35236 U18997 U00096 AP009048
PIR	G65107
RefSeq	NP_417640.1 WP_000207680.1
PDB	1K92 1K97 1KP2 1KP3
PDBsum	1K92 1K97 1KP2 1KP3
ProteinModelPortal	P0A6E4
SMR	P0A6E4
DIP	DIP-35842N
IntAct	P0A6E4
STRING	511145.b3172
DrugBank	DB00536
SWISS-2DPAGE	P0A6E4
PaxDb	P0A6E4
PRIDE	P0A6E4
EnsemblBacteria	AAC76205 BAE77217
GeneID	947590
KEGG	eco:b3172
PATRIC	32121762
EchoBASE	EB0066
EcoGene	EG10068
eggNOG	COG0137
HOGENOM	HOG000230094
InParanoid	P0A6E4
KO	K01940
OMA	MRNLDIA
OrthoDB	EOG6K9QCV
PhylomeDB	P0A6E4
BioCyc	EcoCyc:ARGSUCCINSYN-MONOMER ECOL316407:JW3140-MONOMER
UniPathway	UPA00068
EvolutionaryTrace	P0A6E4
PRO	PR:P0A6E4
Proteomes	UP000000318 UP000000625
GO	GO:0005737 GO:0005829 GO:0004055 GO:0005524 GO:0006526 GO:0000053 GO:0000050
Gene3D	1.10.287.400 3.40.50.620 3.90.1260.10
HAMAP	MF_00581
InterPro	IPR023437 IPR001518 IPR018223 IPR024074 IPR024073 IPR014729
Pfam	PF00764
TIGRFAMs	TIGR00032
PROSITE	PS00564 PS00565

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0006526	arginine biosynthetic process	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000172504 PomBase:SPBC428.05c RGD:2163 SGD:S000005419 UniProtKB:A0A1D8PRR5 UniProtKB:P00966	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000172504 RGD:2163	C	Seeded From UniProt	complete
enables	GO:0004055	argininosuccinate synthase activity	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000172504 PomBase:SPBC428.05c RGD:2163 SGD:S000005419 UniProtKB:P00966	F	Seeded From UniProt	complete
involved_in	GO:0000053	argininosuccinate metabolic process	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000172504 RGD:2163 UniProtKB:P00966	P	Seeded From UniProt	complete
involved_in	GO:0000050	urea cycle	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000172504 RGD:2163 UniProtKB:P00966	P	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11738042^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6E4	F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004055	argininosuccinate synthase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001518 InterPro:IPR018223 InterPro:IPR023434 InterPro:IPR023437 InterPro:IPR024074	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001518 InterPro:IPR018223	F	Seeded From UniProt	complete
involved_in	GO:0006526	arginine biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001518 InterPro:IPR018223	P	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR024073	F	Seeded From UniProt	complete
enables	GO:0004055	argininosuccinate synthase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:6.3.4.5	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000101700	C	Seeded From UniProt	complete
enables	GO:0004055	argininosuccinate synthase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000101700	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000101700	F	Seeded From UniProt	complete
involved_in	GO:0006526	arginine biosynthetic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000101700	P	Seeded From UniProt	complete
involved_in	GO:0006526	arginine biosynthetic process	GO_REF:0000037 GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0055 UniPathway:UPA00068	P	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
involved_in	GO:0008652	cellular amino acid biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0028	P	Seeded From UniProt	complete
enables	GO:0016874	ligase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0436	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Lemke, CT & Howell, PL (2001) The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis. Structure 9 1153-64 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 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

[PMID:21873635-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 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:11738042-2] Lemke, CT & Howell, PL (2001) The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis. Structure 9 1153-64 PubMed GONUTS page

[PMID:18304323-3] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:15911532-4] 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

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ECOLI:ASSY

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