ID   NAGS_TALSN              Reviewed;         690 AA.
AC   B8M3T8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 54.
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=TSTA_038860;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962654; EED20681.1; -; Genomic_DNA.
DR   RefSeq; XP_002481115.1; XM_002481070.1.
DR   AlphaFoldDB; B8M3T8; -.
DR   STRING; 441959.B8M3T8; -.
DR   EnsemblFungi; EED20681; EED20681; TSTA_038860.
DR   GeneID; 8107928; -.
DR   VEuPathDB; FungiDB:TSTA_038860; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; B8M3T8; -.
DR   OMA; WAMFWTT; -.
DR   OrthoDB; 769117at2759; -.
DR   PhylomeDB; B8M3T8; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001745; 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   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           ?..690
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372581"
FT   DOMAIN          508..679
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          62..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   690 AA;  75915 MW;  FD18FD7ADA6A1D2F CRC64;
     MTGLVGENFR RDGGVIPATI TKNLNKSSGR QRAREKMADK EFFLSLLSSA ATKRDAKAYL
     SRFPSVKKPK PPIPRQNQGA VETQSGKENE KPGVNLGSFY GATRSVLETP VFRQGPAPET
     ETAHAIGLDE ALHVALVKLA NAQSLDDETI QGVALTLAQL TRLGMASCVV VDPGPMQDET
     TWRKAAAEQA DRLSAAIDAC DGGKARRLDS VLVKNKDRDL PKIISRQVLL RPLRNNHIVV
     VTPVAYSEET CKASSVPSSD AMLALTRELA GLERKHDPDE DPRVTAEIFA ALQKEVAVDR
     LIVLDSVGGI PAFKGPQQSH VFVNMEQEFK DIEAELHEAM ASIERFVDPS AESDITEAAT
     KSNPISKFVA TEVTPLSTGQ QKPLIEANGG LMTSTLKGHI ENLRLLQQTL TLLPPSSSAI
     ITTPRDVANS ARPHQDVLSV SQVGTRRQKN PLIHNLLTDK PVYSSSLPSE RRGQTAPSIA
     PSTFLKRGMP LTILPDPRIT PWSPNSPDGH HLTLDDPRID LPRLVHLIED SFNRKLDVQD
     YLSRVNGRLA GLIIAGEYEG GAILTWETPP DIPEQDRHKP ENISRLVPYL DKFAVLKRSQ
     GAGGVADIVF NAMVRTCLPG GVCWRSRMDN PVNKWYFERS RGTWKLNGSN WAMFWTTPRV
     PEEDPLKFRD YEAVCRSIQP SWADKKAVVD