XANCP:AOTC

Species (Taxon ID)	Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 /LMG 568). (190485)
Gene Name(s)	argF'
Protein Name(s)	N-acetylornithine carbamoyltransferase AOTCase
External Links
UniProt	Q8P8J2
EMBL	AE008922
RefSeq	NP_637604.1
PDB	3KZC 3KZK 3KZM 3KZN 3KZO 3L02 3L04 3L05 3L06 3M4J 3M4N 3M5C 3M5D
PDBsum	3KZC 3KZK 3KZM 3KZN 3KZO 3L02 3L04 3L05 3L06 3M4J 3M4N 3M5C 3M5D
ProteinModelPortal	Q8P8J2
SMR	Q8P8J2
STRING	190485.XCC2249
EnsemblBacteria	AAM41528
GeneID	998828
KEGG	xcc:XCC2249
PATRIC	24075403
eggNOG	COG0078
HOGENOM	HOG000022686
KO	K09065
OMA	METIVHP
OrthoDB	EOG6G4VSH
BioCyc	MetaCyc:MONOMER-12073 XCAM190485:GIXZ-2247-MONOMER
UniPathway	UPA00068
EvolutionaryTrace	Q8P8J2
Proteomes	UP000001010
GO	GO:0005737 GO:0016597 GO:0004070 GO:0043857 GO:0006207 GO:0006526
Gene3D	3.40.50.1370
InterPro	IPR006132 IPR006130 IPR002082 IPR006131
Pfam	PF00185 PF02729
PRINTS	PR00100 PR00101
SUPFAM	SSF53671

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0043857	N-acetylornithine carbamoyltransferase activity	PMID:16585758	ECO:0000314			F		Table 1: Purified ArgF′ enzyme from Xanthomonas catalyzed the AOTCase reaction which forms N-acetylcitrulline from N-acetylornithine and carbamyl phosphate. Figure 4: LC-MS analysis of enzymatically synthesized N-acetylcitrulline. The enzymatic product of the X. campestris AOTCase reaction has the same mass ion and retention time as chemically synthesized N-acetylcitrulline.	complete CACAO 4547
enables	GO:0043857	N-acetylornithine carbamoyltransferase activity	PMID:16585758	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0042450	arginine biosynthetic process via ornithine		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000150424 PomBase:SPAC4G9.10	P		Seeded From UniProt	complete
involved_in	GO:0019240	citrulline biosynthetic process		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000150424 RGD:3236 UniProtKB:P00480	P		Seeded From UniProt	complete
enables	GO:0004585	ornithine carbamoyltransferase activity		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10067 EcoGene:EG10069 PANTHER:PTN000150424 PomBase:SPAC4G9.10 RGD:3236 SGD:S000003624 UniProtKB:P00480 UniProtKB:P08308 UniProtKB:P9WIT9 UniProtKB:Q9YHY9	F		Seeded From UniProt	complete
enables	GO:0004070	aspartate carbamoyltransferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002082	F		Seeded From UniProt	complete
involved_in	GO:0006207	'de novo' pyrimidine nucleobase biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002082	P		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:IPR006130 InterPro:IPR006131 InterPro:IPR006132 InterPro:IPR036901	P		Seeded From UniProt	complete
enables	GO:0016597	amino acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006130 InterPro:IPR006131 InterPro:IPR036901	F		Seeded From UniProt	complete
enables	GO:0016743	carboxyl- or carbamoyltransferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006130 InterPro:IPR006131 InterPro:IPR006132 InterPro:IPR036901	F		Seeded From UniProt	complete
enables	GO:0043857	N-acetylornithine carbamoyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.1.3.9	F		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:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	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
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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