ID K3ZRS1_SETIT Unreviewed; 592 AA.
AC K3ZRS1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=amino-acid N-acetyltransferase {ECO:0000256|ARBA:ARBA00012697};
DE EC=2.3.1.1 {ECO:0000256|ARBA:ARBA00012697};
GN Name=101773856 {ECO:0000313|EnsemblPlants:KQL26458};
GN ORFNames=SETIT_2G371200v2 {ECO:0000313|EMBL:RCV13753.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV13753.1};
RN [1] {ECO:0000313|EMBL:RCV13753.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL26458,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV13753.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV13753.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV13753.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQL26458}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL26458};
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; AGNK02001319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003529; RCV13753.1; -; Genomic_DNA.
DR RefSeq; XP_004958159.1; XM_004958102.1.
DR AlphaFoldDB; K3ZRS1; -.
DR STRING; 4555.K3ZRS1; -.
DR EnsemblPlants; KQL26458; KQL26458; SETIT_029301mg.
DR GeneID; 101773856; -.
DR Gramene; KQL26458; KQL26458; SETIT_029301mg.
DR KEGG; sita:101773856; -.
DR eggNOG; KOG2436; Eukaryota.
DR HOGENOM; CLU_024773_1_0_1; -.
DR InParanoid; K3ZRS1; -.
DR OMA; KRKYNWD; -.
DR OrthoDB; 46762at2759; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000004995; Chromosome II.
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 SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 2.
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:UP000004995};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 431..578
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 64447 MW; CA8CB3BA6AFACAC2 CRC64;
MATWAPGARL AGEVSRPGAQ TSANGLTCGR LRRVAVTRRW RGRGVRCCAV SKSGSGAAAA
AAVDPGEEFV GFFREAWPYI RGHRGSTFVV VISSEVVSGP HFDRVLQDIS LLHGLGIKFV
LVPGTHVQID KLLSERGKKA KYVGQYRITD SDSLEAAMEA AGRIRLTIEA KLSPGPPMLN
LRRHGVIGRW HGLVDNVASG NFLGAKRRGV VNGIDYGFTG EVKKIDVSRI RERLDSDSIV
VVSNMGYSSS GEVLNCNTYE VATACALAME ADKLVCVVDG QIFDEHGRVI HFMSIEEADL
LIRKRAKQSD IAANYVKVVD EEGINSLQKG DYKPSLNSRA HVNGYAAAFQ NGLGFNNGNG
IYSGEQGFAI GGEEQLSRSN GYLSELAAAA YVCHGGVQRV HIIDGTVDGS LLLELFTRDG
AGTMIARDVY EGTRMATAED LHGIRKIIRP LEDSGVFVRR TDAELLDALN SFYVVERDGS
IIACAALFPF PEDKSGEVAA IAVSEECRGR GQGDKLLDYV EKVALSLGLE KLFLLTTRTA
DWFVRRGFSE CSIDSIPEQR RKRINLSRGS KYYIKQLQPK HAGVTTNNFI IR
//
