NAGS_ASPFU
ID NAGS_ASPFU Reviewed; 716 AA.
AC Q4X122;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 90.
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=AFUA_2G11490;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000001; EAL93443.2; -; Genomic_DNA.
DR RefSeq; XP_755481.2; XM_750388.2.
DR AlphaFoldDB; Q4X122; -.
DR SMR; Q4X122; -.
DR STRING; 746128.CADAFUBP00002663; -.
DR EnsemblFungi; EAL93443; EAL93443; AFUA_2G11490.
DR GeneID; 3512781; -.
DR KEGG; afm:AFUA_2G11490; -.
DR VEuPathDB; FungiDB:Afu2g11490; -.
DR eggNOG; KOG2436; Eukaryota.
DR HOGENOM; CLU_013088_0_0_1; -.
DR InParanoid; Q4X122; -.
DR OMA; WAMFWTT; -.
DR OrthoDB; 769117at2759; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000002530; Chromosome 2.
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 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..716
FT /note="Amino-acid acetyltransferase, mitochondrial"
FT /id="PRO_0000372552"
FT DOMAIN 537..706
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 37..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 716 AA; 78710 MW; BAA6D761975755A0 CRC64;
MSLHTGWPRT VNSSFLKKHR SSLCTCQHTS SVLPRSFSTT PDRHVQQSAD FSSTSRSYDR
LGRRAREKLL DREFFLSLLS SATTKREAKS YLARLKAQHP KSPDANKPEP EKSATAPTLP
SGVNLGSFYG ASRSVYESPV FRQGPSPSAP PSLEPVERLH LALVRLSTPQ SLDDNIIDGV
AKTLSQLNRL GLTCCVVVDP GTEGVASALR QVAIEQADRL AVAIQKQPDS KSLRLDSVFS
IDPSRPGLPQ VFSRKALLNP LRHGHTVILT PIAYTEDVPR AIIVPANDAV IALTKELAGL
ASIPDPDEDP MVTAERIGRL QKEVSLDRVI LLDPLGGIPA FNRRQPSHVF INMEQEYDDI
ENELLQAREM VPATETSLLK AGPNSVADNN PISKFVHAEV VPVPSGSTPE LKTAVPQRSA
IEGHLENLRV AQKALAMLPA ASSGIITSPF EVASSAQTSP TSEFSAVGTR RQRNPLIHNL
LTDKPLLSSS LPMSRRGPTN NGQGAVYPVT SHTTFVKRGM PLTMLPNPWT EPWTPQSRPR
LKLDDPSIDL PRLVHLIEDS FDRKLDVQDY LNRVNDRLAG LIIAGEYEGG AILTWELPPG
VEDDGSEASN ARMVPYLDKF AVLKRSQGAG GVADIVFNAM VRSCFPNGVC WRSRKNNPVN
KWYFERSLGT WKLSDTNWTM FWTTPGLVED SQKFRDYEAV CRSIQPSWAD DTGVVD
