NAGS_CANAL
ID NAGS_CANAL Reviewed; 580 AA.
AC Q59MB6; A0A1D8PDG4; Q59MA4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Amino-acid acetyltransferase, mitochondrial;
DE EC=2.3.1.1;
DE AltName: Full=Arginine-requiring protein 2;
DE AltName: Full=Glutamate N-acetyltransferase;
DE AltName: Full=N-acetylglutamate synthase;
DE Short=AGS;
DE Short=NAGS;
DE Flags: Precursor;
GN Name=ARG2; OrderedLocusNames=CAALFM_C105020CA;
GN ORFNames=CaO19.56, CaO19.7717;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP INDUCTION.
RX PubMed=17975531; DOI=10.3314/jjmm.48.159;
RA Cho T., Aoyama T., Toyoda M., Nakayama H., Chibana H., Kaminishi H.;
RT "Transcriptional changes in Candida albicans Genes by both farnesol and
RT high cell density at an early stage of morphogenesis in N-acetyl-D-
RT glucosamine medium.";
RL Nippon Ishinkin Gakkai Zasshi 48:159-167(2007).
CC -!- FUNCTION: N-acetylglutamate synthase involved in arginine biosynthesis.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- INDUCTION: Up-regulated in cells treated with farnesol and grown at
CC high cell density in N-acetyl-D-glucosamine medium. Expression is
CC regulated by the general amino acid control response transcription
CC factor GCN4. {ECO:0000269|PubMed:17975531}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26174.1; -; Genomic_DNA.
DR RefSeq; XP_710867.2; XM_705775.2.
DR AlphaFoldDB; Q59MB6; -.
DR STRING; 237561.Q59MB6; -.
DR GeneID; 3647533; -.
DR KEGG; cal:CAALFM_C105020CA; -.
DR CGD; CAL0000184037; ARG2.
DR VEuPathDB; FungiDB:C1_05020C_A; -.
DR eggNOG; KOG2436; Eukaryota.
DR HOGENOM; CLU_013088_0_0_1; -.
DR InParanoid; Q59MB6; -.
DR OrthoDB; 769117at2759; -.
DR UniPathway; UPA00068; UER00106.
DR PRO; PR:Q59MB6; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006592; P:ornithine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR011190; GlcNAc_Synth_fun.
DR InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR Pfam; PF04768; NAT; 1.
DR PIRSF; PIRSF007892; NAGS_fungal; 1.
DR PROSITE; PS51731; GNAT_NAGS; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Amino-acid biosynthesis; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..580
FT /note="Amino-acid acetyltransferase, mitochondrial"
FT /id="PRO_0000372556"
FT DOMAIN 403..560
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 580 AA; 66683 MW; 387726E29CA0C75B CRC64;
MSKLKTLNRQ FISNLETHKV TTDAKRNLIL SILKSTTTKR EAKNYLTKYQ NQFDFNDDLD
FNKSIKIKNE QSSLTNRDSQ RELFINRFLN QSNPFINVYD KEDVKLQKVP LRLAIFKIKF
TKITIKQWKG IAETFKRLIT LGISPIIMLD YDHLPSDSYK NNELYMINQG NKMLNYLGHP
EEESDLKVTL LRSLFTSHKG VPTLDSLESI LIPLYQGIIP IIQPIVYNAD LSKQEFLASD
KLLLGLSSAL IEKRTTDLLS IEKIVMIDPI GGIPSIERHQ TSHVFINLSQ EYSDILSELF
IGHIEPKYRD THVDNLNTMN NVLSYINEKS GNDETTGIIT TPEIMSINID QLNPIIYNVL
TDRAIISSSL PSTTNRTPHL STTIIKKGVE VQIFDVDNYD KDLTMQNLFD DKLVNKEKLI
DLLNDSFGKS LDVGPYLDRI NKNIATVVIV GDYDGAAIIT WEYSKGEKIA YLDKFAIAKK
NQGLPGLADV IFKIILQSHP FELIWRSRKN NPVNKWYFER CCGCMSAPDS QWKIFYTGEV
FDKKIDRFKR KLRHQNGVVD IDRKLQQYSE ICEGITPSFK
