ID A0A158EVF5_9BURK Unreviewed; 456 AA.
AC A0A158EVF5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01105};
DE EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_01105};
DE AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_01105};
DE Short=AGS {ECO:0000256|HAMAP-Rule:MF_01105};
DE Short=NAGS {ECO:0000256|HAMAP-Rule:MF_01105};
GN Name=argA {ECO:0000256|HAMAP-Rule:MF_01105};
GN ORFNames=AWB64_00404 {ECO:0000313|EMBL:SAL11514.1};
OS Caballeronia sordidicola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=196367 {ECO:0000313|EMBL:SAL11514.1, ECO:0000313|Proteomes:UP000054893};
RN [1] {ECO:0000313|EMBL:SAL11514.1, ECO:0000313|Proteomes:UP000054893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22029 {ECO:0000313|EMBL:SAL11514.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|HAMAP-
CC Rule:MF_01105};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4. {ECO:0000256|ARBA:ARBA00004925,
CC ECO:0000256|HAMAP-Rule:MF_01105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01105}.
CC -!- MISCELLANEOUS: In bacteria which possess the bifunctional enzyme
CC ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA
CC fulfills an anaplerotic role. {ECO:0000256|HAMAP-Rule:MF_01105}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC {ECO:0000256|ARBA:ARBA00009145, ECO:0000256|HAMAP-Rule:MF_01105}.
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DR EMBL; FCOC02000001; SAL11514.1; -; Genomic_DNA.
DR RefSeq; WP_060816933.1; NZ_FCOC02000001.1.
DR AlphaFoldDB; A0A158EVF5; -.
DR OrthoDB; 9802238at2; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000054893; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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: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, ECO:0000256|HAMAP-
KW Rule:MF_01105};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01105};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_01105}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01105};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01105}.
FT DOMAIN 310..456
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 50357 MW; 1491A163818516CB CRC64;
MNTQTDLPAA QPPVSAEQEA PDQHAQFVDW MRSVAPYIHA FRNKTFVVAF GGELVQEGRL
NALVQDVGLL HAMGIHVVLV HGSRPQVEEQ LNLHGVESEF SHGLRITDAR ALESAKEAAG
EVRLDIEAAI SQGLPNTPMA HAHISVVSGN FVTARPVGIL DGVDFQHTGV VRKIDGDSIR
HSLTSSKLVL LSPLGFSPTG EAFNLSMEDV ASAAAIALRA DKIIFLTETP GLVDENNELV
REMSLDDAYR LHESGELQGD AAFYLKHTIR ACRGGVARAH IIPYALDGSI LLELFLHDGV
GTMISYENLE SLREATPDDV GGILTLIEPL EMDGTLVRRG RHQIERDIDH FSVIEHDGVL
FGCVALYPYT QERIGEMACL TVSPEAQGAG DGERLLKRVE QRARARGLTH IFVLTTRTEH
WFLKRGFVKV TVDDLPEDRR RLYNWQRKSL VLMKQL
//
