ID   NAGS_PODAN              Reviewed;         674 AA.
AC   B2B2C5; A0A090CPZ0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 60.
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; OrderedLocusNames=Pa_6_3620; ORFNames=PODANS_6_3620;
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
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; CU638744; CAP71260.1; -; Genomic_DNA.
DR   EMBL; FO904941; CDP30660.1; -; Genomic_DNA.
DR   RefSeq; XP_001910126.1; XM_001910091.1.
DR   AlphaFoldDB; B2B2C5; -.
DR   SMR; B2B2C5; -.
DR   STRING; 5145.XP_001910126.1; -.
DR   EnsemblFungi; CAP71260; CAP71260; PODANS_6_3620.
DR   GeneID; 6194495; -.
DR   KEGG; pan:PODANSg7163; -.
DR   VEuPathDB; FungiDB:PODANS_6_3620; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001197; Chromosome 6.
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; IPR006855; Vertebrate-like_GNAT_dom.
DR   Pfam; PF04768; NAT; 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..50
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           51..674
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372576"
FT   DOMAIN          497..665
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          33..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   674 AA;  73657 MW;  859C2FB2DC29CA8C CRC64;
     MPLVAAMLTR SNGAWKKATS VVQASICRDQ QRPNHTTITS VTSVSQRRHF SSAENGAKPS
     RSHPSAAEAK QKRESDREFL ISVLESSATK RDAKAYLQTY GSSKAKAVPK ESPASTALVS
     DKAIPEAKDV SFFVQGSVPV ESLEADEVPR VAIVKLREPQ TWDDTLLGGV AKTLTRLRDL
     GLRSVIVLEC SAEKSSVLDW KDVVTQQTDR LQKAIQKYGT PGAELVDGGI WKRSTTPPSA
     SSLGHTKLSV GFGEAFTAPL RHGHILVVPS RAVVEETLEH TAADANEVIF ALAKYFAGLQ
     VNAGQNQTRT AVVDRVIIID PFGGIPARNL GDGARVFINL EEQFNSIKAT LSAAEPQDNG
     SPIPGISGNP KASHIENLEL VKNILAILPS TASAVITSPI EAANLQSNQA YDIRRDAEEA
     MAGEVKTRRW QNPIIHNLLT DRPIYSASLP IGRIKSTTNG TYQRSSRMPT TTLAKKGLPV
     TIFPDTRTRS WQPPKPGTPR LKLTDTCVDL PRLIHLINDS FGRKLDAEHY LNRVQDSLAG
     IIIAGEYEGG AILTWERPFG LDEETAYNSG RLVPYLDKFA VLKKSQGAGG VADIVFNAMV
     RDCFPNGVCW RSRKDNPVNK WYFERSRGVR KLPGSNWAMF WTTPEAAVKD QVMEDYEDVC
     RGVVPSWADS KAAD