NAGS_YEAS1
ID NAGS_YEAS1 Reviewed; 574 AA.
AC B3LQ40;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 49.
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=SCRG_03599;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- ACTIVITY REGULATION: Feedback inhibition by L-arginine. {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4.
CC -!- SUBUNIT: Interacts with the acetylglutamate kinase chain of AGR5,6.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; CH408050; EDV12693.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LQ40; -.
DR SMR; B3LQ40; -.
DR PRIDE; B3LQ40; -.
DR EnsemblFungi; EDV12693; EDV12693; SCRG_03599.
DR HOGENOM; CLU_013088_0_0_1; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000008335; 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; Transferase;
KW Transit peptide.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 14..574
FT /note="Amino-acid acetyltransferase, mitochondrial"
FT /id="PRO_0000372584"
FT DOMAIN 392..560
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 574 AA; 65610 MW; 167456A4900B7D59 CRC64;
MWRRIFAHEL KYDQPNASSK NLILSVLNTT ATKREAKDYL SKYTNDSGQH NHCLFFIRDL
HKVAPAILSQ FSSVIKRLGM LGLRPMFVIP PSPTHVNIQA ELLDSIVTEA DLKPLHLKEG
LTKSRTGLYH SVFSQESRFF DIGNSNFIPI VKPYVYNEET ASEFMTKDVV KFMDCLCQGN
IPHIDKFFIL NNAGGIPSGE RNDNAHVFIN LSQELEHLSS SLSHNISTLT KREPRSQNLL
HRMEVYVKKD EISSLECEYH DHLENLLLMD KVLSNLAATA TGLITTVKAA ALSSDRKNPL
VYNLLTDRSL ISSSLPRFKK KDGEIDSPAN MFDDHAWYEL PSQQVNAAPS NSDAVLVTTV
LKKGVHIKTY DYKTLTQFNS IGLPKKFHVP EKGAKPSSNS PKLDINKFKS IIDQSFKRSL
DLHDYIKRIN GKIATIIVIG DYEGIAILTY EGSEENSFVY LDKFAVLPHL KGSLGISDII
FNLMFKKFPN EILWRSRKDN VVNKWYFQRS VAVLDLSIDL DPEHCDEKQS QFKLFYYGNP
QYAKRALRDK KRLREFMRSV RDIKPSWENE KNIS