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Database: UniProt
Entry: I1IUH9_BRADI
LinkDB: I1IUH9_BRADI
Original site: I1IUH9_BRADI 
ID   I1IUH9_BRADI            Unreviewed;       586 AA.
AC   I1IUH9;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=amino-acid N-acetyltransferase {ECO:0000256|ARBA:ARBA00012697};
DE            EC=2.3.1.1 {ECO:0000256|ARBA:ARBA00012697};
GN   Name=100828645 {ECO:0000313|EnsemblPlants:KQJ92335};
GN   ORFNames=BRADI_4g42970v3 {ECO:0000313|EMBL:KQJ92335.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ92335.1};
RN   [1] {ECO:0000313|EMBL:KQJ92335.1, ECO:0000313|EnsemblPlants:KQJ92335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ92335.1,
RC   ECO:0000313|EnsemblPlants:KQJ92335};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQJ92335.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ92335.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQJ92335}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ92335};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00000016};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004925}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC       {ECO:0000256|ARBA:ARBA00009145}.
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DR   EMBL; CM000883; KQJ92335.1; -; Genomic_DNA.
DR   RefSeq; XP_003578936.1; XM_003578888.3.
DR   AlphaFoldDB; I1IUH9; -.
DR   STRING; 15368.I1IUH9; -.
DR   EnsemblPlants; KQJ92335; KQJ92335; BRADI_4g42970v3.
DR   GeneID; 100828645; -.
DR   Gramene; KQJ92335; KQJ92335; BRADI_4g42970v3.
DR   KEGG; bdi:100828645; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_024773_1_0_1; -.
DR   InParanoid; I1IUH9; -.
DR   OMA; KRKYNWD; -.
DR   OrthoDB; 46762at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000008810; Chromosome 4.
DR   ExpressionAtlas; I1IUH9; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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   CDD; cd04237; AAK_NAGS-ABP; 1.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   HAMAP; MF_01105; N_acetyl_glu_synth; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR033719; NAGS_kin.
DR   InterPro; IPR010167; NH2A_AcTrfase.
DR   NCBIfam; TIGR01890; N-Ac-Glu-synth; 1.
DR   PANTHER; PTHR30602; AMINO-ACID ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR30602:SF9; AMINO-ACID N-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   PIRSF; PIRSF000423; ArgA; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          424..571
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   586 AA;  63275 MW;  D98E8753BCB29C84 CRC64;
     MASFATARLA GGGVLLRAVG DDTSRGLPSG RLCLPSPRRR LPSVRCCAAR HPAGGGGGNG
     SGGMDAGTEF VGFFREAWPY IRGHSGSTFV VVISSEVVAG PHLDRILQDI SLLHGLGINF
     VLVPGTHVHI DKLLTQRGGK AKYVGQYRVT DSDSLDAAME AAGRIRLTIE AKLSPGPPML
     NLRRHGDIGH RHGLVDNVAS GNFLGAKRRG VVNGIDYGFT GEVKKIDVSR IKERLDSHSI
     VVVSNMGYSS SGEVLNCNTY EVATACALAI EADKLICVVD GQIFDEHGRV IHFMSLDEAD
     MLIRKRAKQS DIAASYVKVV DEEDHEPSSN GRGHLNGYAA SFKNGLGFNN GNGIYSGEQG
     FAIGGEERLS RSNGYLSELA AAAYVCHGGV QRVHIIDGTV DGSLLLELFT RDGAGTMIAR
     DVYEGTRMAT EEDLPGIRKL IYPLEESGVL VRRTDKELLE ALYSFYVVER DGSIVACAAL
     FPFPENESGE VAAIAVSEEC RGKGLGDKLL DYIEKEALSL GLGKLFLLTT RTADWFVRRG
     FSECSIESIP EQRRKRINLS RGSKYYIKEL LQKHVVSLAA NNFVAS
//
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