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Database: UniProt/SWISS-PROT
Entry: NAGS_ASPNC
LinkDB: NAGS_ASPNC
Original site: 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   01-MAY-2013, entry version 37.
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; Trichocomaceae;
OC   mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G.,
RA   Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K.,
RA   Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M.,
RA   Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M.,
RA   Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M.,
RA   van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S.,
RA   Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T.,
RA   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.,
RA   van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P.,
RA   van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C.,
RA   Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G.,
RA   Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U.,
RA   Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B.,
RA   Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory
RT   Aspergillus niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: N-acetylglutamate synthase involved in arginine
CC       biosynthesis (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-
CC       glutamate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 1/4.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the acetyltransferase family.
CC   -!- SIMILARITY: Contains 1 N-acetyltransferase domain.
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DR   EMBL; AM270051; CAK44592.1; -; Genomic_DNA.
DR   RefSeq; XP_001390189.1; XM_001390152.1.
DR   STRING; 5061.CADANGAP00003233; -.
DR   EnsemblFungi; CADANGAT00003318; CADANGAP00003233; CADANGAG00003318.
DR   GeneID; 4980283; -.
DR   KEGG; ang:ANI_1_1218034; -.
DR   eggNOG; COG5630; -.
DR   HOGENOM; HOG000111164; -.
DR   KO; K00618; -.
DR   OrthoDB; EOG4X6GJ3; -.
DR   UniPathway; UPA00068; UER00106.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR006855; DUF619.
DR   InterPro; IPR011190; GlcNAc_Synth_fun.
DR   Pfam; PF04768; DUF619; 1.
DR   PIRSF; PIRSF007892; NAGS_fungal; 1.
DR   PROSITE; PS51186; GNAT; FALSE_NEG.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW   Mitochondrion; Transferase; Transit peptide.
FT   TRANSIT       1     44       Mitochondrion (Potential).
FT   CHAIN        45    726       Amino-acid acetyltransferase,
FT                                mitochondrial.
FT                                /FTId=PRO_5000219763.
FT   DOMAIN      547    706       N-acetyltransferase.
FT   COMPBIAS     59     64       Poly-Ser.
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
//
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