ID   NAGS_VANPO              Reviewed;         567 AA.
AC   A7TQL5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=Kpol_1027p10;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480460; EDO15436.1; -; Genomic_DNA.
DR   RefSeq; XP_001643294.1; XM_001643244.1.
DR   AlphaFoldDB; A7TQL5; -.
DR   STRING; 436907.A7TQL5; -.
DR   EnsemblFungi; EDO15436; EDO15436; Kpol_1027p10.
DR   GeneID; 5543517; -.
DR   KEGG; vpo:Kpol_1027p10; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; A7TQL5; -.
DR   OMA; YFQRSVG; -.
DR   OrthoDB; 769117at2759; -.
DR   PhylomeDB; A7TQL5; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000000267; 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   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           ?..567
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372582"
FT   DOMAIN          392..558
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   567 AA;  64850 MW;  6078E768F2C2B80C CRC64;
     MWKHLLSGGL KVEQQNASAK KLILSVLNST ATKREARDYL TKYTRSDDSK QLNHCLLLIR
     HLNSLRQHEI SELTSTVKKL GMLGLRPIFV IPPSRHIAKQ AEILDIITTL AGFRPLQLQN
     SLSQSIDGTY TSILSSQNAI LNNHELEVVP ILKPYVYREK DASEFLTNDF TKFMQNLCKG
     NNTHIDKFFI LNRIGGIPSN ERNENSHVFV NLSQEYDCLK KDLKGQVDLL IERRPRTESL
     LHKLELHLNE DAINTLENQF KEHLQDLEMM NVVLSNLSSS ATGLITTIES AASSSEKKNP
     LIYNILTDRS LISSSLPRFK KIRHTPPSGS RPAKKFHRMT YLEDYQQLDK SSPPDSALVT
     TVFKKGIDIK IFDYPKLTQF NSLSLPVEFR VKDSPQTNPL HKIDLSKLKG LIDRSFKRSL
     NLNHYLHRIN GNIASIIVIG DYDGIAILTN EGPNDNPFVY LDKFAISPEM KGSLCISDII
     FNLMVKKFPK ELLWRSRNDN VVNKWYFQRS VGVLDLSIDL GDGNQTKSNF NLFYYGEPKS
     TNYGFHNLAR LKEYAKHIRD IHPSWDK