ID   NAGS_ASPTN              Reviewed;         691 AA.
AC   Q0CY06;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 66.
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; ORFNames=ATEG_01428;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR   EMBL; CH476595; EAU38185.1; -; Genomic_DNA.
DR   RefSeq; XP_001208793.1; XM_001208793.1.
DR   AlphaFoldDB; Q0CY06; -.
DR   STRING; 341663.Q0CY06; -.
DR   EnsemblFungi; EAU38185; EAU38185; ATEG_01428.
DR   GeneID; 4315748; -.
DR   VEuPathDB; FungiDB:ATEG_01428; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   OMA; WAMFWTT; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Mitochondrion;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..691
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372554"
FT   DOMAIN          512..681
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   691 AA;  75672 MW;  8EE5243DAE26E33B CRC64;
     MSSTSLAWPR TAKSSLLQSA DFSSTSKGYD RLGRRAREKL LDREFFLSLL NSASTKREAK
     SYLARLKAQH SPKPQVKEPE KESKDDAPQP LPSGVNLGSF YGASRSVYDS PVFRHDSTPT
     PHREISEERL HLSLVKLTTP QLLDDYIIDG VAKTLSQLNR LGMASCVVVD PGAGDHPNAL
     RKIAAEQADR LSNAIDALPD SKSAHLDSVL SLSSTDPDTP TVMSRKALLS PMRDGHIVVV
     APIAYTDDVR AVVVPADNAV LALTKELAGL ATRPDPDEDP WVTAQRIGDL QREVSLDRVI
     LLDPLGGIPA FSGPQTSHVF INMEQEFDDI EQELLRVRES AASSNQPSAS SLLDGDASSI
     ADSNPISKFV NHDVVPVPPE QEAVLPGLRL EERAVDGHLE NLSLSQKVLA MLPSASSGII
     TSPLEVANSA MAPQTTPSGL AVGTRRQRNP LIHNLLTDKP LLSSSLPLSR RAAINGRRGS
     LTAPSSHTTF VKRGMPLTLV PNPRVQTWTA QNRPRMSLDD PSIDLPRLVH LIEDSFNRKL
     DVQDYLNRIH DRLAGLIIAG EYEGGAILTW ELPPGVEDDG SPASEARMVP YLDKFAVLKR
     SQGAGGVADI VFNAMVRSCF PNGVCWRSRK DNPVNKWYFE RSEGTWKLAD TNWTMFWTTP
     NLPDDLQRFQ DYEAVCRSIQ PSWADDTGVV D