P40360 (NAGS_YEAST) 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:	YJL071W
ORF Names:	HRB574, J1091

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	574 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	N-acetylglutamate synthase involved in arginine biosynthesis. Ref.5 Ref.7
Catalytic activity	Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.
Enzyme regulation	Feedback inhibition by L-arginine. Ref.6
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subunit structure	Interacts with the acetylglutamate kinase chain of AGR5,6. Ref.7
Subcellular location	Mitochondrion Ref.5 Ref.8.
Miscellaneous	Present with 112 molecules/cell in log phase SD medium.
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 Traceable author statement Ref.7. Source: SGD ornithine biosynthetic process Inferred from mutant phenotype Ref.7. Source: SGD
Cellular_component	mitochondrial matrix Inferred from direct assay Ref.5. Source: SGD
Molecular_function	acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from direct assay Ref.7. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 13	13	Mitochondrion
	Chain	14 – 574	561	Amino-acid acetyltransferase, mitochondrial		PRO_0000203054
Regions
	Domain	395 – 567	173	N-acetyltransferase

Sequences

	Sequence		Length	Mass (Da)
	P40360 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 167456A4900B7D59	FASTA	574	65,610
	10 20 30 40 50 60 MWRRIFAHEL KYDQPNASSK NLILSVLNTT ATKREAKDYL SKYTNDSGQH NHCLFFIRDL 70 80 90 100 110 120 HKVAPAILSQ FSSVIKRLGM LGLRPMFVIP PSPTHVNIQA ELLDSIVTEA DLKPLHLKEG 130 140 150 160 170 180 LTKSRTGLYH SVFSQESRFF DIGNSNFIPI VKPYVYNEET ASEFMTKDVV KFMDCLCQGN 190 200 210 220 230 240 IPHIDKFFIL NNAGGIPSGE RNDNAHVFIN LSQELEHLSS SLSHNISTLT KREPRSQNLL 250 260 270 280 290 300 HRMEVYVKKD EISSLECEYH DHLENLLLMD KVLSNLAATA TGLITTVKAA ALSSDRKNPL 310 320 330 340 350 360 VYNLLTDRSL ISSSLPRFKK KDGEIDSPAN MFDDHAWYEL PSQQVNAAPS NSDAVLVTTV 370 380 390 400 410 420 LKKGVHIKTY DYKTLTQFNS IGLPKKFHVP EKGAKPSSNS PKLDINKFKS IIDQSFKRSL 430 440 450 460 470 480 DLHDYIKRIN GKIATIIVIG DYEGIAILTY EGSEENSFVY LDKFAVLPHL KGSLGISDII 490 500 510 520 530 540 FNLMFKKFPN EILWRSRKDN VVNKWYFQRS VAVLDLSIDL DPEHCDEKQS QFKLFYYGNP 550 560 570 QYAKRALRDK KRLREFMRSV RDIKPSWENE KNIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Sor F.J. Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Sequence of a 17.1 kb DNA fragment from chromosome X of Saccharomyces cerevisiae includes the mitochondrial ribosomal protein L8." Vandenbol M., Durand P., Dion C., Portetelle D., Hilger F. Yeast 11:57-60(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Arginine metabolism in Saccharomyces cerevisiae: subcellular localization of the enzymes." Jauniaux J.-C., Urrestarazu L.A., Wiame J.-M. J. Bacteriol. 133:1096-1107(1978) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"Regulation of activity and synthesis of N-acetylglutamate synthase from Saccharomyces cerevisiae." Wipe B., Leisinger T. J. Bacteriol. 140:874-880(1979) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[7]	"A new yeast metabolon involving at least the two first enzymes of arginine biosynthesis: acetylglutamate synthase activity requires complex formation with acetylglutamate kinase." Abadjieva A., Pauwels K., Hilven P., Crabeel M. J. Biol. Chem. 276:42869-42880(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ACETYLGLUTAMATE KINASE.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X88851 Genomic DNA. Translation: CAA61310.1. Z34288 Genomic DNA. Translation: CAA84051.1. Z49346 Genomic DNA. Translation: CAA89363.1. BK006943 Genomic DNA. Translation: DAA08728.1.
PIR	S50800.
RefSeq	NP_012464.1. NM_001181504.1.
3D structure databases
ProteinModelPortal	P40360.
SMR	P40360. Positions 402-538.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5679N.
MINT	MINT-572756.
STRING	4932.YJL071W.
Proteomic databases
PaxDb	P40360.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJL071W; YJL071W; YJL071W.
GeneID	853374.
KEGG	sce:YJL071W.
Organism-specific databases
CYGD	YJL071w.
SGD	S000003607. ARG2.
Phylogenomic databases
eggNOG	COG5630.
HOGENOM	HOG000113727.
KO	K00618.
OMA	DYEGIAI.
OrthoDB	EOG4X6GJ3.
Enzyme and pathway databases
UniPathway	UPA00068; UER00106.
Gene expression databases
Genevestigator	P40360.
GermOnline	YJL071W. Saccharomyces cerevisiae.
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...
Other
NextBio	973819.

Entry information

Entry name

NAGS_YEAST

Accession

Primary (citable) accession number: P40360
Secondary accession number(s): D6VWB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program