ID   D4AY60_ARTBC            Unreviewed;       677 AA.
AC   D4AY60;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   01-MAY-2013, entry version 18.
DE   RecName: Full=Amino-acid acetyltransferase, mitochondrial;
DE            EC=2.3.1.1;
DE   AltName: Full=Glutamate N-acetyltransferase;
DE   AltName: Full=N-acetylglutamate synthase;
GN   ORFNames=ARB_01129;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371)
OS   (Trichophyton mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Arthroderma.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K.,
RA   Feuermann M., Pedruzzi I., Priebe S., Groth M., Winkler R., Li W.,
RA   Kniemeyer O., Schroeckh V., Hertweck C., Hube B., White T.C.,
RA   Platzer M., Guthke R., Heitman J., Woestemeyer J., Zipfel P.F.,
RA   Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the acetyltransferase family.
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DR   EMBL; ABSU01000018; EFE31876.1; -; Genomic_DNA.
DR   RefSeq; XP_003012516.1; XM_003012470.1.
DR   GeneID; 9526587; -.
DR   KEGG; abe:ARB_01129; -.
DR   KO; K00618; -.
DR   UniPathway; UPA00068; -.
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.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW   Mitochondrion; Transferase.
SQ   SEQUENCE   677 AA;  74792 MW;  AA3833C4ED303524 CRC64;
     MNPKAALRLR LLQHQPNTSR CHGYGSLPPS KRRCFSHFTP APSPSLVHRI HAHTQYPVEI
     PDQLGQSAKE KEEDKEFFLD LLSSATTKRE AKSYLSRFSP QPPPSNAQQE DRVSTNPQAA
     DTGRKYTEVS ITSSTGEKLS PTYDISKPKD TITESLHVAL VKIKNPESLD EQCLHGISKT
     LSQLSRLSMC CCIVLEVNTP GNDIDYRKLA STQASRIAAR IDKVHSPGAR RLDSAVSLDP
     STHDVSILSR NFLLSPLSRG QIVVIDPVGY TNDTSKALPV AADEIILALT KELAGLSSKF
     GLSEASADTV QNVPQPQRDI SIERLIILDP LGGIPSLGRG LHKSHVFINL EQEYEDIQNE
     ITQAIPNPPE SAHSGLQAEL EGHLANLTLL QKALALLPTS SSGLITTPQG ATTLPLNHNG
     IYGTPAVGTR QRRNPLIHNL LTDKPVLSAS LPARRRGGEK CDNDPNSQPS HPTFVKHGMP
     LIMIPDPRVK CWTAAHNDGS RINLDDPAID LPRLVHLIDD SFNRKLDVKH YLDRVKDRLA
     GLIIAGEYEG GAILTWELPP GVPDDGSPES MSRMVPYLDK FAVLKRSQGA GGVADIVFNA
     MVRTCFPEGV CWRSRKNNPV NKWYFERSRG TWKLPDSNWA MFWTTDNVPE NEQLFEDYES
     VCRSIQPSWA DNKKEVD
//