ID   NAGS_NEUCR              Reviewed;         712 AA.
AC   Q1K8F6; Q12643; V5IQ12;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Amino-acid acetyltransferase, mitochondrial;
DE            EC=2.3.1.1;
DE   AltName: Full=Arginine-requiring protein 14;
DE   AltName: Full=Glutamate N-acetyltransferase;
DE   AltName: Full=N-acetylglutamate synthase;
DE            Short=AGS;
DE            Short=NAGS;
DE   Flags: Precursor;
GN   Name=arg-14; ORFNames=NCU07682;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX   PubMed=8939437; DOI=10.1046/j.1365-2958.1996.1321494.x;
RA   Yu Y.G., Turner G.E., Weiss R.L.;
RT   "Acetylglutamate synthase from Neurospora crassa: structure and regulation
RT   of expression.";
RL   Mol. Microbiol. 22:545-554(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [3]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=2939069; DOI=10.1016/s0021-9258(17)38460-0;
RA   Hinde R.W., Jacobson J.A., Weiss R.L., Davis R.H.;
RT   "N-acetyl-L-glutamate synthase of Neurospora crassa. Characteristics,
RT   localization, regulation, and genetic control.";
RL   J. Biol. Chem. 261:5848-5852(1986).
CC   -!- FUNCTION: N-acetylglutamate synthase involved in arginine biosynthesis.
CC       {ECO:0000269|PubMed:2939069, ECO:0000269|PubMed:8939437}.
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   -!- ACTIVITY REGULATION: Inhibited by arginine.
CC       {ECO:0000269|PubMed:2939069}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.3 nM for glutamate {ECO:0000269|PubMed:2939069};
CC       pH dependence:
CC         Optimum pH is 8.8-9. {ECO:0000269|PubMed:2939069};
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:0000269|PubMed:2939069}.
CC   -!- INDUCTION: By histidine or arginine limitation.
CC       {ECO:0000269|PubMed:8939437}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR   EMBL; L35484; AAC37502.1; -; Genomic_DNA.
DR   EMBL; CM002239; ESA42856.1; -; Genomic_DNA.
DR   RefSeq; XP_011394254.1; XM_011395952.1.
DR   AlphaFoldDB; Q1K8F6; -.
DR   SMR; Q1K8F6; -.
DR   STRING; 5141.EFNCRP00000007999; -.
DR   EnsemblFungi; ESA42856; ESA42856; NCU07682.
DR   GeneID; 3878463; -.
DR   KEGG; ncr:NCU07682; -.
DR   VEuPathDB; FungiDB:NCU07682; -.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; Q1K8F6; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006592; P:ornithine biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Acyltransferase; Amino-acid biosynthesis; Mitochondrion;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..47
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..712
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372569"
FT   DOMAIN          534..702
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          55..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   712 AA;  78280 MW;  C8F6F7494258F1C6 CRC64;
     MFVRTCRSSC NAWTNATSTT QAGSLLPPNA HRSVVLTLSL QACSARTHES LIRSFASTTS
     QSKRQEAEAE EKRQVSPRLG PSAPRSSYPS SAEARQKRDS DREFLISVLE SSATKRDARG
     YLQTFGSSAA LTSAGQKKPS TIGILGVPAS VAGRPAFVQG TEKEISVKRN EAPHVAVVKL
     RAPQAWDDVL LEGVAKTLTR LRDLGLLSVI VLDCDDIKPN QASSWHETVT EQTDRLLRAI
     GQYGFPAAEV VDSGIWKSTE NPQIPSSVPS NPLYVGFGKA FTTPLANGHI LVVPPRAYSD
     ASLQYSKADA NDIVIALTTF FAGLQFGQQS SDYRQLAEKV SDGQSFRKAL VDRVIVIDPL
     GGIPSHRQGH GTQVFINLED EFKNIQDALY EKTQPTSAGT KDAGVSARAT VHLENLRLAK
     STLALLPSNA SVVMTSPAEA ANINVSRRNQ LEAKPDGFAG EVKTRTWRNP LIHNLLTDRP
     IYSSSLPIGR IKPTHQDEEI ALSRMPTTTL AKRGLPVTIF PDPRVNRWQP PQPGVPRLRL
     TDTCIDLPRL VHLINDSFGR KLNVEHYLDR VKDSLAGIII AGEYEGGAIL TWETPFGLDE
     ETAYRKGRLV PYLDKFAVLR KSQGAGGVAD IVFNAMVRDA FPDGVCWRSR KDNPVNKWYF
     ERSRGVLKLP ESNWAMFWTT PEAVSNDQMM RDYEDVCRNI APSWADTTKP AD