ID NAGS_CRYNJ Reviewed; 565 AA.
AC P0CM18; Q55W63; Q5KK32;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 06-MAR-2013, entry version 13.
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; OrderedLocusNames=CNC04430;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 /
OS ATCC MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC Tremellomycetes; Tremellales; Tremellaceae; Filobasidiella;
OC Filobasidiella/Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J.,
RA D'Souza C.A., Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J.,
RA Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I.,
RA Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E.,
RA Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L.,
RA Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A.,
RA Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R.,
RA Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W.,
RA Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen
RT Cryptococcus neoformans.";
RL Science 307:1321-1324(2005).
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; AE017343; AAW42706.1; -; Genomic_DNA.
DR RefSeq; XP_570013.1; XM_570013.1.
DR ProteinModelPortal; P0CM18; -.
DR GeneID; 3256636; -.
DR KEGG; cne:CNC04430; -.
DR KO; K00618; -.
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 Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR006855; DUF619.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF04768; DUF619; 2.
DR SUPFAM; SSF55729; Acyl_CoA_acyltransferase; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1 ? Mitochondrion (Potential).
FT CHAIN ? 565 Amino-acid acetyltransferase,
FT mitochondrial.
FT /FTId=PRO_0000372561.
FT DOMAIN 355 520 N-acetyltransferase.
SQ SEQUENCE 565 AA; 62641 MW; F575EB160554E3CB CRC64;
MLTGSSGKAF ILSILQASPS ARDSRSYLSS FAPPQPADIA TATPAATPSD GAQPPAQNPL
VNALLNPILR RPALVKIQGP FTDAQLESIC RGMAHLQKLG LVSVIVVDRD DLPSTESSDR
YEAQRQRAIV RHEVERVVHF LSRHRAAARP VFSTVARIAD PELEPEEAQK GVFVEEEGLD
HVRRAVGEGE IPVLLPVALD SGCRSRRIPA NRVLLALASA MSTHTSSPVD LTPRRLLVIN
REGGIPSYAR QGLPHLYINL ASEFSYINRT FQPQWNDSHP TALSNLFLAN GCLAHMPREA
SALIVSHRSP AALIANLITN KPAHSASLPH ALLVESEGRI TRDTPTLIRK GLPVRVLRSM
EEVDQDKLTH LLETSFKRTL DREGFYNRLK NDLDFVIVIG DYAGAAVCTL EGKPVSDSFA
YPPNHPEPIC YLDKFAVHPS HQGDGTVDFL WVALRDETYG LGQLDASNPS IGSLRGVGRG
RDLVWRSRSD NPVNKWYYER SSGFLKTRDE KWKVFWCDAE QRLGEIWRER EFGGGRLVRV
VEKEEKGRVK WWEEVIGAIP SAWSA
//