ID   NAGS_PENRW              Reviewed;         769 AA.
AC   B6H6F3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=Pc15g00060;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(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; AM920430; CAP82892.1; -; Genomic_DNA.
DR   RefSeq; XP_002560234.1; XM_002560188.1.
DR   AlphaFoldDB; B6H6F3; -.
DR   SMR; B6H6F3; -.
DR   STRING; 1108849.XP_002560234.1; -.
DR   EnsemblFungi; CAP82892; CAP82892; PCH_Pc15g00060.
DR   GeneID; 8306317; -.
DR   KEGG; pcs:Pc15g00060; -.
DR   VEuPathDB; FungiDB:PCH_Pc15g00060; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   OMA; WAMFWTT; -.
DR   OrthoDB; 769117at2759; -.
DR   BioCyc; PCHR:PC15G00060-MON; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000000724; Contig Pc00c15.
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   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
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           ?..769
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372570"
FT   DOMAIN          590..759
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          150..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   769 AA;  84488 MW;  CAF98CFC8A971520 CRC64;
     MEVPVDFPIS WPCCDTLHAV DPLISLYGVS QKRDEECTHI LNASYQSWYP QAVSYNRGSM
     DASYYFSFSL PWNLPSYIQY LVRPNDPIAV RPTQVLNVRA QQIAEFSGSS ESQDRLGHRA
     KEKLLDREFF LSLLSSASTK REAKSYLARL KASPAKSGQE PTESPKESIS ASLPSGVNLG
     SFYGASRAVY DSPVFRQDTT PTPRAQDIPE RLHLALIKIT TPQLLDNSVI NGVAKTLSQL
     VRLGMACCVV VDPGKTDGHA GRQTAIEQAN RISAAVDEQP DSRSFRLDSA LSISERGSGL
     PTVLSRKVLL SALQDGHVVL VPPIAYTEEN PRAVTVSAND AALALTKEFA GLSFNPDPDE
     DPAVTAERIR NLQREVSLDR VIVLDALGGI PAFKGPQSSH VFINMEQEFD QIKDELSQVR
     NSVSSKQGTS EATYSTLESN PFSKFVNREL VLPEKPTAPP SPGAEVMEEV LDGHLENLRL
     AQQALAMLPS ASSGIITSPQ EVSYSARSPQ QAASDLSAVG TRRQRNPLIH HLLTDKPLLS
     SSLPPGRRGA FNGSGSNQFN PVTSHTTFVK RGMPLTILPN PYTKPWRAQM QPRLGLNDPT
     IDLPRLVTLI EDSFDRKLDV QNYLERVNSR IAGVIVAGEY EGGAILTWET PPGVPDDGSE
     ASAARMVPYL DKFAVLKRSQ GAGGVADVVF NAMVRTCFPN GVCWRSRMDN PVNKWYFERS
     SGTWKLAGSN WAMFWTTPGL VEDTQRFQDY EAVCRSIQPS WADKKNVID