Q6CEE1 (NAGS_YARLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Amino-acid acetyltransferase, mitochondrial
EC=2.3.1.1

Alternative name(s):
Arginine-requiring protein 2
Glutamate N-acetyltransferase
N-acetylglutamate synthase
Short name=AGS
Short name=NAGS

Gene names

Name:	ARG2
Ordered Locus Names:	YALI0B16390g

Organism

Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) [Reference proteome]

Taxonomic identifier

284591 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia › Yarrowia lipolytica

Protein attributes

Sequence length	608 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	N-acetylglutamate synthase involved in arginine biosynthesis By similarity.
Catalytic activity	Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the acetyltransferase family. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acetyl-CoA:L-glutamate N-acetyltransferase 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
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 608		Amino-acid acetyltransferase, mitochondrial		PRO_0000372583
Regions
	Domain	402 – 593	192	N-acetyltransferase
	Compositional bias	478 – 488	11	Poly-Ala

Sequences

	Sequence		Length	Mass (Da)
	Q6CEE1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 5609EFE173123BDE	FASTA	608	67,106
	10 20 30 40 50 60 MLRSSRITAG TCVSRGWHSY TTKTPTKTAI PPAAKSSNEA KDLILSVLQS AATKREAKTY 70 80 90 100 110 120 ISRYAPLTGV ELQKKKEGLV QRLLGVGKEQ DNKEIENLTG HAPEGLLGDS EGTLRVAIIK 130 140 150 160 170 180 IRDIKSIEDD LIAQMGETIA RLSRLGVSPI VVVDAGKARN DFLKLDNKPF RHYQKLILQK 190 200 210 220 230 240 VFKISDAIDA ASPDVGARPI EGLFSMNKKG LRLAMPQMLM HPLSHGKVPV LAPLAYDDVT 250 260 270 280 290 300 SEEKLVMADD VVHFLTQKLA EVPANILSVE KIIFVDPLGG IPSVERSGAH VFVNLKQELS 310 320 330 340 350 360 DIAAELHMGF IPPAQREVHL ANLKAMHKAL KFLPPTASGL ITTPAVAAIP SVGRNPIIYN 370 380 390 400 410 420 VLTDRPVISP SLPVELKKTP TLETTLLREG MPVITLKSDK GLNLITEHEK GNIDLDRLWH 430 440 450 460 470 480 LIEDSFGRRI DKQHYLNRVN GKIAGIIIAG DYEGAAIITW EDIDPVKAQE DRDAADRAAA 490 500 510 520 530 540 EAAAAYAAGI PLPSPPLYQK LGDAVPLNPN QVAYLDKFAV LKRSQGSSSV ADVVFKGMVM 550 560 570 580 590 600 SQFPNELLWR SRKNNPVNKW YFDRSKGSFK IPGSEWCMFW TGRKTREQYL ERFVDICTRI EPSLREEL

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382128 Genomic DNA. Translation: CAG83224.1.
RefSeq	XP_500971.1. XM_500971.1.
3D structure databases
ProteinModelPortal	Q6CEE1.
ModBase	Search...
Protein-protein interaction databases
STRING	4952.Q6CEE1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2907516.
KEGG	yli:YALI0B16390g.
Phylogenomic databases
eggNOG	COG5630.
HOGENOM	HOG000111164.
KO	K00618.
OMA	AAIITWE.
OrthoDB	EOG4X6GJ3.
Enzyme and pathway databases
UniPathway	UPA00068; UER00106.
Family and domain databases
InterPro	IPR006855. DUF619. IPR011190. GlcNAc_Synth_fun. [Graphical view]
Pfam	PF04768. DUF619. 1 hit. [Graphical view]
PIRSF	PIRSF007892. NAGS_fungal. 1 hit.
PROSITE	PS51186. GNAT. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAGS_YARLI

Accession

Primary (citable) accession number: Q6CEE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program