NAGS_PICST
ID NAGS_PICST Reviewed; 581 AA.
AC A3GG03;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 25-MAY-2022, entry version 71.
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=PICST_51037;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; AAVQ01000001; EAZ63850.2; -; Genomic_DNA.
DR RefSeq; XP_001387873.2; XM_001387836.1.
DR AlphaFoldDB; A3GG03; -.
DR SMR; A3GG03; -.
DR STRING; 4924.XP_001387873.2; -.
DR EnsemblFungi; EAZ63850; EAZ63850; PICST_51037.
DR GeneID; 4851202; -.
DR KEGG; pic:PICST_51037; -.
DR eggNOG; KOG2436; Eukaryota.
DR HOGENOM; CLU_013088_0_0_1; -.
DR InParanoid; A3GG03; -.
DR OMA; WAMFWTT; -.
DR OrthoDB; 769117at2759; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000002258; Chromosome 1.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..581
FT /note="Amino-acid acetyltransferase, mitochondrial"
FT /id="PRO_0000372575"
FT DOMAIN 401..558
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 581 AA; 66705 MW; 8ADAA34E3377BA1B CRC64;
MSKLKNLNRE FISNLKSHKL ITDAKRNLIL SILKSTTTKR EARNYLNKYQ NQFDFGDLKI
SSSAKYEQDV SKLTKRDSQR ELFVNRYLNK QNPFINIYDD ETKLKKIPLR VALFKLKFLN
IDPKEWRGIA ETFKRLVNLG ISPIVFLDYD HLPTDSFKYN ELYMINQVNK VMNYLGKPEE
EGNLKTTVLR SLFTVENKER GPVINSLESI LIPLYQGIIP FIQPIIYNAE STFQQFINSN
QLLYSLCESL LDKKDLLSVE KIVMIDPIGG IPSVERNQTS HVFINLSQEY SDIVSELYIG
HIEPDQRDLH LANLNTMHEI LTLASSKSGN DDTTGIITTP FIMSVNDDLI NPIIYNVLTD
RPIISSSLPS SNNRTPQLST SILKKGVDVR SYDADNYARK FTLHNLIEDE LVDKNRLVAL
LDDSFGKNLD TDSYFDRINN SLATLVIVGD YDGAAIITWE YSGTNKIAYL DKFAIAKKNQ
GLPGLADVIF KIILSSHPHE LIWRSRKVNP VNKWYFERCV GSMSSPESQW RIFYTGDIFN
RRIDKRRKRI VGSEAVNISD KLVQYSEICE GIPPSFFSSK E