ID   NAGS_TALMQ              Reviewed;         724 AA.
AC   B6QS64;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, 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=PMAA_048850;
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
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; DS995904; EEA21082.1; -; Genomic_DNA.
DR   RefSeq; XP_002152082.1; XM_002152046.1.
DR   AlphaFoldDB; B6QS64; -.
DR   STRING; 441960.B6QS64; -.
DR   EnsemblFungi; EEA21082; EEA21082; PMAA_048850.
DR   GeneID; 7029629; -.
DR   KEGG; tmf:PMAA_048850; -.
DR   VEuPathDB; FungiDB:PMAA_048850; -.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   OrthoDB; 769117at2759; -.
DR   PhylomeDB; B6QS64; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001294; 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..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..724
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372571"
FT   DOMAIN          542..713
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          37..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   724 AA;  80307 MW;  3B264AA1B7D249C2 CRC64;
     MSLQSSRVLL HRKHDWSTCR NLPARWWSHP RSYHQESQHA DRKPASASAS AWTEPLSKSH
     SRSSGRQRAR EKMADKEFFL SLLTSATTKR EAKAYLSRFP SVKKTKLPMT PKKEAAVELQ
     PPKEIEKPGV NLGSFYGPTR SVLQTPVFRQ GSTPEIETAI NLDEALHVAL VKLTDAQSLD
     DETIHGVALT LSQLTRLGMA SCVVVDPGPV KDATTWRKAA AEQADRLSAA IDACDGGKAR
     RLDSVLVRNK DGEVPKVISR QVLLRPLRKN HIVVVTPVAY SEQTCKASSV ASNDVMIALT
     RELAGLERKH DPDEDPRVTA ENFAALQKEI SVDRLIVLDP VGGIPAFKGP QRAHVFVNME
     QEFRGIETEL QEAMASLEGY VDPGTESDLS AAAMKSNPIS KFVATEVTRM PTRPQHKPLP
     VNGGVMNSAI KEHVENLRLL QQTLTLLPPS SSGIITTPTD VANSARPQQD ILSVSQVGTR
     SSKNLLIHNL LTDKPAYSSS LPSERLGRTT PSIVQSTFLK RGMPLTILPD PRITPWSPNS
     PDSRHLTLDD PRIDLSRLVH LIEDSFNRKL DVQDYLNRVN GRLAGLIIAG EYEGGAILTW
     ETPPSIPESE RNNPENLPRL VPYLDKFAVL KRSQGAGGVA DIVFNAMVRT CLPQGVCWRS
     RMDNPVNKWY FERSRGTWKL DGSNWAMFWT TPGVPEEDSL RFKDYEAVCR SIQPSWADKK
     AVDD