ID   NAGS_ASPCL              Reviewed;         718 AA.
AC   A1C6J2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=ACLA_070450;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027045; EAW14013.1; -; Genomic_DNA.
DR   RefSeq; XP_001275439.1; XM_001275438.1.
DR   AlphaFoldDB; A1C6J2; -.
DR   STRING; 5057.CADACLAP00007066; -.
DR   PRIDE; A1C6J2; -.
DR   EnsemblFungi; EAW14013; EAW14013; ACLA_070450.
DR   GeneID; 4707512; -.
DR   KEGG; act:ACLA_070450; -.
DR   VEuPathDB; FungiDB:ACLA_070450; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   OMA; WAMFWTT; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000006701; 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..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..718
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372549"
FT   DOMAIN          539..708
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          97..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   718 AA;  79482 MW;  32780EB3F250E2A2 CRC64;
     MNPNAVWPRT AQSSLKKHQV SLCTCQRRSH YRLRSFSTFA DRKIHQSAGF SSSSKNHDRL
     SHRAREKLLD REFFLSLLSS ASTQREAKSY LARLKAQHQP DLPQKPTSAP ASTAKIPPLP
     SGVNLGSFYG ASRSVYETPV FRQGPTPTPR QDQPERLHLA LVKLSIPQTL DDTIIDGVAK
     TLAQLDRLGL TCCVMIDPGA AEDARLLRTL ATEQADRLAI AIHKQPDSKS LRLDSVLSVD
     PATPHLPKVL SRKALLKPLR DGHTVILTPI AYTEDVPRAV MVSADDAVLA LTRELAGLAT
     FPDPDEDPLT TAERIGRLQK EVSLDRVILL HPLGGIPAFN WRQSSHVFIN MEQEYDDIEN
     ELLQARDVIS AGDANLTASD ILQHPSSVAV SNPLSKFVHK EIVPLPPARS LSPMVPEAQR
     SAVEGHLENL RLSQKALAML PSASSGIITS PIEVANSAKT DQPSDLSVVG TRRQRNPLIH
     NLLTDKPLLS SSLPMSRRGP IISAQGILNP VTSHTTFVKR GMPLTILPNP WVKPWSAQRQ
     PRLRLDDPSI DLPRLVHLIE DSFNRKLDVQ DYLNRVNDRL AGLIIAGEYE GGAILTWELP
     PGVQDDGSAE NSARMVPYLD KFAVLKRSQG AGGVADIVFN AMVRTCFPNG VCWRSRKNNP
     VNKWYFERSL GTWKLSDTNW TMFWTTPGLV EDSQKFRDYE AVCRSIQPSW AEDTGVVD