NAGS_YARLI
ID NAGS_YARLI Reviewed; 608 AA.
AC Q6CEE1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=YALI0B16390g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382128; CAG83224.1; -; Genomic_DNA.
DR RefSeq; XP_500971.1; XM_500971.1.
DR AlphaFoldDB; Q6CEE1; -.
DR STRING; 4952.CAG83224; -.
DR EnsemblFungi; CAG83224; CAG83224; YALI0_B16390g.
DR GeneID; 2907516; -.
DR KEGG; yli:YALI0B16390g; -.
DR VEuPathDB; FungiDB:YALI0_B16390g; -.
DR HOGENOM; CLU_013088_0_0_1; -.
DR InParanoid; Q6CEE1; -.
DR OMA; WAMFWTT; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000001300; Chromosome B.
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 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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..608
FT /note="Amino-acid acetyltransferase, mitochondrial"
FT /id="PRO_0000372583"
FT DOMAIN 402..604
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 608 AA; 67106 MW; 5609EFE173123BDE CRC64;
MLRSSRITAG TCVSRGWHSY TTKTPTKTAI PPAAKSSNEA KDLILSVLQS AATKREAKTY
ISRYAPLTGV ELQKKKEGLV QRLLGVGKEQ DNKEIENLTG HAPEGLLGDS EGTLRVAIIK
IRDIKSIEDD LIAQMGETIA RLSRLGVSPI VVVDAGKARN DFLKLDNKPF RHYQKLILQK
VFKISDAIDA ASPDVGARPI EGLFSMNKKG LRLAMPQMLM HPLSHGKVPV LAPLAYDDVT
SEEKLVMADD VVHFLTQKLA EVPANILSVE KIIFVDPLGG IPSVERSGAH VFVNLKQELS
DIAAELHMGF IPPAQREVHL ANLKAMHKAL KFLPPTASGL ITTPAVAAIP SVGRNPIIYN
VLTDRPVISP SLPVELKKTP TLETTLLREG MPVITLKSDK GLNLITEHEK GNIDLDRLWH
LIEDSFGRRI DKQHYLNRVN GKIAGIIIAG DYEGAAIITW EDIDPVKAQE DRDAADRAAA
EAAAAYAAGI PLPSPPLYQK LGDAVPLNPN QVAYLDKFAV LKRSQGSSSV ADVVFKGMVM
SQFPNELLWR SRKNNPVNKW YFDRSKGSFK IPGSEWCMFW TGRKTREQYL ERFVDICTRI
EPSLREEL