ID   NAGS_PICPA              Reviewed;         590 AA.
AC   Q595W7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 43.
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;
OS   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15789348; DOI=10.1002/yea.1202;
RA   Nett J.H., Hodel N., Rausch S., Wildt S.;
RT   "Cloning and disruption of the Pichia pastoris ARG1, ARG2, ARG3, HIS1,
RT   HIS2, HIS5, HIS6 genes and their use as auxotrophic markers.";
RL   Yeast 22:295-304(2005).
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; AY532166; AAT07967.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q595W7; -.
DR   UniPathway; UPA00068; UER00106.
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; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..590
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372574"
FT   DOMAIN          427..587
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   590 AA;  67515 MW;  19DA6080BCD25A9D CRC64;
     MLSIKDFTSN LTRHARNTEE KRNMVLTILN STATKREVRN YLKKYPLLKD VDIYSKGQMD
     RSSVSKRNKY SSMIDNLMLK HSTNNENNKI EDFHLNRPRS DLISKSKLEI KLTDTLRIAI
     VKIRQFRDID PTALKGIAFT LYKLIKLGVS PIVLLDTDKE VQALNGESDA MVQKSIANYH
     QQALSFINII EKCFHKYEDD NELSARAIRG LFEQKFDEDR FSMTLPELLL IPISQGIVPV
     VYPVGYMDKG SKNVFLSSEA VLQCLATDLK SLNDRHRLDH DKENLFTIEK YIFIDPLGGI
     PSLERYKSAH VYINLLQEYE DIVSELYIGF LKTGERDQHL KNLNLLQKLL QVTTDASGIV
     TTPQIAMLNQ TDRFTNPIIY NVLTDRPTIS SSLPVDLKKT PLLNTSIIRR GVPVEVYVDE
     SSDKSGLCLD SLLKRGALDL EKLKNVIDLS FRKDLNMKKY LARVKNNVAA ILIAGDYEGV
     IIVTWEVTDE EKPQKIAYLD KFAVSPKAQG STGVADVLFK SLLSNFENEL FWRSRSNNPV
     NKWYFERSKG SLTVTGTNWK CFYTGKNYPS LDRMKGYFNI CERIQPSWNG