Q59MB6 (NAGS_CANAL) 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
ORF Names:	CaO19.56, CaO19.7717

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	580 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

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.
Induction	Up-regulated in cells treated with farnesol and grown at high cell density in N-acetyl-D-glucosamine medium. Expression is regulated by the general amino acid control response transcription factor GCN4. Ref.2
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
Gene Ontology (GO)
Biological process	cellular amino acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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	? – 580		Amino-acid acetyltransferase, mitochondrial		PRO_0000372556
Regions
	Domain	402 – 567	166	N-acetyltransferase
Natural variations
	Natural variant	421	1	E → D in allele: CaO19.7717.
	Natural variant	434	1	C → G in allele: CaO19.7717.
	Natural variant	552	1	P → L in allele: CaO19.7717.

Sequences

	Sequence		Length	Mass (Da)
	Q59MB6 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 1BA49DB9937A4A24	FASTA	580	66,740
	10 20 30 40 50 60 MSKLKTLNRQ FISNLETHKV TTDAKRNLIL SILKSTTTKR EAKNYLTKYQ NQFDFNDDLD 70 80 90 100 110 120 FNKSIKIKNE QSSLTNRDSQ RELFINRFLN QSNPFINVYD KEDVKLQKVP LRLAIFKIKF 130 140 150 160 170 180 TKITIKQWKG IAETFKRLIT LGISPIIMLD YDHLPSDSYK NNELYMINQG NKMLNYLGHP 190 200 210 220 230 240 EEESDLKVTL LRSLFTSHKG VPTLDSLESI LIPLYQGIIP IIQPIVYNAD LSKQEFLASD 250 260 270 280 290 300 KLLLGLSSAL IEKRTNDLLS IEKIVMIDPI GGIPSIERHQ TSHVFINLSQ EYSDILSELF 310 320 330 340 350 360 IGHIEPKYRD THVDNLNTMN NVLSYINEKS GNDETTGIIT TPEIMSINID QLNPIIYNVL 370 380 390 400 410 420 TDRAIISSSL PSTTNRTPHL STTIIKKGVE VQIFDVDNYD KDLTMQNLFD DKLVNKEKLI 430 440 450 460 470 480 ELLNDSFGKS LDVCPYLDRI NKNIATVVIV GDYDGAAIIT WEYSKGEKIA YLDKFAIAKK 490 500 510 520 530 540 NQGLPGLADV IFKIILQSHP FELIWRSRKN NPVNKWYFER CCGCMSAPDS QWKIFYTGEV 550 560 570 580 FDKKIDRFKR KPRHQNGVVD IDRKLQQYSE ICEGITPSFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314 / ATCC MYA-2876.
[2]	"Transcriptional changes in Candida albicans Genes by both farnesol and high cell density at an early stage of morphogenesis in N-acetyl-D-glucosamine medium." Cho T., Aoyama T., Toyoda M., Nakayama H., Chibana H., Kaminishi H. Nippon Ishinkin Gakkai Zasshi 48:159-167(2007) [PubMed: 17975531] [Abstract] Cited for: INDUCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACQ01000231 Genomic DNA. Translation: EAK91624.1. AACQ01000232 Genomic DNA. Translation: EAK91611.1.
RefSeq	XP_710855.1. XM_705763.1. XP_710867.1. XM_705775.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q59MB6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3647533. 3647545.
KEGG	cal:CaO19.56. cal:CaO19.7717.
Organism-specific databases
CGD	CAL0000606. ARG2.
Phylogenomic databases
PhylomeDB	Q59MB6.
Family and domain databases
InterPro	IPR006855. DUF619. IPR011190. GlcNAc_Synth_fun. [Graphical view]
KO	K00618.
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_CANAL

Accession

Primary (citable) accession number: Q59MB6
Secondary accession number(s): Q59MA4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	April 26, 2005
Last modified:	January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program