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Database: UniProt
Entry: A0A2U1NYB2_ARTAN
LinkDB: A0A2U1NYB2_ARTAN
Original site: A0A2U1NYB2_ARTAN 
ID   A0A2U1NYB2_ARTAN        Unreviewed;       574 AA.
AC   A0A2U1NYB2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=amino-acid N-acetyltransferase {ECO:0000256|ARBA:ARBA00012697};
DE            EC=2.3.1.1 {ECO:0000256|ARBA:ARBA00012697};
GN   ORFNames=CTI12_AA206750 {ECO:0000313|EMBL:PWA78447.1};
OS   Artemisia annua (Sweet wormwood).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC   Artemisiinae; Artemisia.
OX   NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA78447.1, ECO:0000313|Proteomes:UP000245207};
RN   [1] {ECO:0000313|EMBL:PWA78447.1, ECO:0000313|Proteomes:UP000245207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PWA78447.1};
RX   PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA   Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA   Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA   Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT   "The genome of Artemisia annua provides insight into the evolution of
RT   Asteraceae family and artemisinin biosynthesis.";
RL   Mol. Plant 11:776-788(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWA78447.1}.
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DR   EMBL; PKPP01001987; PWA78447.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1NYB2; -.
DR   STRING; 35608.A0A2U1NYB2; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000245207; Unassembled WGS sequence.
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   PANTHER; PTHR30602; AMINO-ACID ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR30602:SF12; AMINO-ACID ACETYLTRANSFERASE NAGS1, CHLOROPLASTIC-RELATED; 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   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245207};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          413..561
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   574 AA;  63756 MW;  FCCAC7D6F8BEAA31 CRC64;
     MSILNPKHYV PMQHHEYSWW NTTKCGRKYL RVFGINKIGT MLTTKCKVSN DYNDCRTDSD
     WKNDRFVEMM REAWPYFKAY RGRTFVVVLC AEIIESNNLG AILEDISLLH GLGIKFVLVP
     GTHVQIDSLL VEKGCEPKYV GRYRITDPDS LKAEMDSAGR ITQMIQAKLS PGPSLNNIRR
     HGYNSRSHES VGVASGNFLA AKKRGVVEGV DYGATGEVKK IDVPRIRENL DAHSIVILSN
     LGYSSSGDVL NCNTYEVATA CALALEAEKL ICVIDGPILD KMGRLIRFLT LEDADRLIRE
     RAQQSEIAAS YVRATGEEDS TKSQNGNGCS STFQNGVGFD HGNGFWFSGF AIGGQERLSR
     SNGYLSELAA AAYVCRGGVQ RVHLLDGNIG GVLLKELYQR DGVGTMVASD LYEGARSAEV
     TDLEAIRQLL KPLEDSGTLI RRTDDEMLNA LGSFVVVERE NHIIACAALI PFYNDNCGEV
     AAFVVSPDCR GQGQGDKLLE YIEKKASANG LRTLFLLTTR TEDWFVRRGY SECSIESIPD
     ERRKRINRSR GSKCYMKQLL PDTSGIRVNN SFAE
//
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