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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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
//