CAMJE:ARLY

Species (Taxon ID)	Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168). (192222)
Gene Name(s)	argH (ECO:0000255 with HAMAP-Rule:MF_00006)
Protein Name(s)	Argininosuccinate lyase (ECO:0000255 with HAMAP-Rule:MF_00006) ASAL (ECO:0000255 with HAMAP-Rule:MF_00006) Arginosuccinase (ECO:0000255 with HAMAP-Rule:MF_00006)
External Links
UniProt	Q46104
EMBL	M77188 AL111168
PIR	B81367
RefSeq	YP_002344329.1
ProteinModelPortal	Q46104
IntAct	Q46104
STRING	192222.Cj0931c
EnsemblBacteria	CAL35051
GeneID	905111
KEGG	cje:Cj0931c
PATRIC	20058806
eggNOG	COG0165
HOGENOM	HOG000242744
KO	K01755
OMA	ATDFRLW
OrthoDB	EOG6P5ZF8
BioCyc	CJEJ192222:GJTS-899-MONOMER
UniPathway	UPA00068
Proteomes	UP000000799
GO	GO:0005737 GO:0004056 GO:0042450
Gene3D	1.10.275.10
HAMAP	MF_00006
InterPro	IPR029419 IPR009049 IPR024083 IPR020557 IPR000362 IPR022761 IPR008948
PANTHER	PTHR11444 PTHR11444:SF3
Pfam	PF14698 PF00206
PRINTS	PR00149
SUPFAM	SSF48557
TIGRFAMs	TIGR00838
PROSITE	PS00163

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0004056	argininosuccinate lyase activity	PMID:11683360	ECO:0000314			F		E. coli C600 (WT functional argH),E. coli W3678 (no argH gene), C. jejuni TGH9011 (WT functional argH), and transformed E. coli (C. jejuni TGH9011 argH gene) were examined for ASL activity. E. coli C600, which is wild type with respect to the argH gene, showed a specific activity of 1.1 + 0.17 ,umol of arginine per h per mg of protein. C. jejuni TGH9011 showed a specific activity of 1.3 ± 0.32 ,umol of arginine per h per mg of protein. E. coli W3678 did not possess any significant ASL activity compared with extract-free controls. The transformed strain pARGH1-1 had a specific activity of 5.7 ± 1.2 ,imol of arginine per h per mg of protein. This result confirms that the protein derived from the recombinant plasmid possesses argininosuccinate lyase activity activity.	complete CACAO 4555
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008948 InterPro:IPR020557	F		Seeded From UniProt	complete
enables	GO:0004056	argininosuccinate lyase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR009049	F		Seeded From UniProt	complete
involved_in	GO:0042450	arginine biosynthetic process via ornithine	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR009049	P		Seeded From UniProt	complete
enables	GO:0004056	argininosuccinate lyase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:4.3.2.1	F		Seeded From UniProt	complete
enables	GO:0004056	argininosuccinate lyase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000037443	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:UR000037443	C		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:UR000037443	P		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
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:0016829	lyase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0456	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
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References

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