NAGS_ASPNC
ID NAGS_ASPNC Reviewed; 726 AA.
AC A2QGF0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=An03g02930;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(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; AM270051; CAK44592.1; -; Genomic_DNA.
DR RefSeq; XP_001390189.1; XM_001390152.1.
DR AlphaFoldDB; A2QGF0; -.
DR SMR; A2QGF0; -.
DR PaxDb; A2QGF0; -.
DR EnsemblFungi; CAK44592; CAK44592; An03g02930.
DR GeneID; 4980283; -.
DR KEGG; ang:ANI_1_1218034; -.
DR VEuPathDB; FungiDB:An03g02930; -.
DR HOGENOM; CLU_013088_0_0_1; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000006706; Chromosome 6R.
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..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 45..726
FT /note="Amino-acid acetyltransferase, mitochondrial"
FT /id="PRO_5000219763"
FT DOMAIN 547..716
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 78172 MW; 22C58DDD375FBA40 CRC64;
MSSRTLVGLR STTSTHLQRS GVAAAAAVSS SSTSSSGSAP RRCLSSASGR QVQQSAEFSS
SSKSWDRLGR RAKEKLLDRE FFLSLLNSAS TKREAKSYLA RLKAQHQGTP PLKPAAKQPG
VAEAAAPVSS GASSTSFYGA SRSVYDSPVF RHDSTPTPPL QDVSERLHLA LVKITTPQLL
DDSTVNGVAK TLSQLNRLGM ACCVVVDPGT AGDSNQLRRI AAEQADRIST AVDAQPDSKS
AHIDSVLSVS ALNPEAPKVL SRKLLLGPLR DGHIVVLAPI AYTEDVPRAV TVSASDAILA
LTKELAGLAT NPDPDEDPIR TAQRIAGLQE EVSLDRVILL DPLGGIPAFS GPQTSHVFIN
MEQEFDDIEN ELLRVWQSAA SAKNNLPEEG LPSIADSNPL SKFADTEVVP VPPSQKAYSS
DLTLGTSMVE GHINNLRLSQ AALAMLPSAS SSIITSPLEV ANSAQSPGGA SPDVSAVGTR
RQRNPLIHNL LTDKPLLSSS LPLSRRAALN GRRDSIATQP SHTTFVKRGM PLTIIPNPWL
SPWTAKDRPR LGLDDPSIDL PRLVHLIEDS FNRKLDVQDY LNRVNGRLAG LIIAGEYEGG
AILTWELPPG VEDDGSEASQ ARMVPYLDKF AVLKRSQGAG GVADIVFNAM VRSCFPNGVC
WRSRKDNPVN KWYFERSQGT WKLSDMNWTM FWTTPGLTED SQKFRDYEAV CRSIQPSWAD
DTGVVD
