ID A0A2A3LJZ4_9GAMM Unreviewed; 441 AA.
AC A0A2A3LJZ4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Acetylglutamate kinase {ECO:0000256|ARBA:ARBA00021197, ECO:0000256|PIRNR:PIRNR036441};
DE EC=2.7.2.8 {ECO:0000256|ARBA:ARBA00013065, ECO:0000256|PIRNR:PIRNR036441};
GN ORFNames=CMZ84_01520 {ECO:0000313|EMBL:PBJ83251.1};
OS Xanthomonadaceae bacterium NML93-0399.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae.
OX NCBI_TaxID=2032565 {ECO:0000313|EMBL:PBJ83251.1, ECO:0000313|Proteomes:UP000218035};
RN [1] {ECO:0000313|EMBL:PBJ83251.1, ECO:0000313|Proteomes:UP000218035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML93-0399 {ECO:0000313|EMBL:PBJ83251.1,
RC ECO:0000313|Proteomes:UP000218035};
RA Bernier A.-M., Bernard K.;
RT "Clinical and environmental strains of Xanthomonadaceae.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-
CC phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001679,
CC ECO:0000256|PIRNR:PIRNR036441};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004828}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR036441}.
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:PBJ83251.1}.
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DR EMBL; NTJI01000001; PBJ83251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3LJZ4; -.
DR OrthoDB; 9803155at2; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000218035; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04252; AAK_NAGK-fArgBP; 1.
DR CDD; cd04264; DUF619-NAGS; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011242; ArgB_GNAT.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR041734; NAGK-fArgBP.
DR InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR NCBIfam; TIGR00761; argB; 1.
DR PANTHER; PTHR23342; N-ACETYLGLUTAMATE SYNTHASE; 1.
DR PANTHER; PTHR23342:SF0; N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF04768; NAT; 1.
DR PIRSF; PIRSF036441; NAGK_DUF619; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR PROSITE; PS51186; GNAT; 1.
DR PROSITE; PS51731; GNAT_NAGS; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR036441};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571,
KW ECO:0000256|PIRNR:PIRNR036441};
KW ATP-binding {ECO:0000256|PIRNR:PIRNR036441};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR036441};
KW Kinase {ECO:0000256|PIRNR:PIRNR036441, ECO:0000313|EMBL:PBJ83251.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR036441};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036441}.
FT DOMAIN 294..440
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51731"
FT DOMAIN 297..441
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 79..80
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036441-50"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036441-50"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036441-50"
FT SITE 46
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR036441-51"
FT SITE 251
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR036441-51"
SQ SEQUENCE 441 AA; 48388 MW; D4E1525C9A65CF8D CRC64;
MNIPATHVQT RQTIVRLLSS MASAKEISQY LKRFSQLDAM RFAVVKVGGA VLRDELDDLT
SSLSFLQEVG LTPIVLHGAG PQLDVELAAA GIEKKTVGGL RVTSPEGLAI VRRVFQAANL
RLVEALQKNG ARATSITGGV FEATYLDQAT YGLVGEVNAV NLAPIEASLQ AGSIPVITSL
GETASGQILN INADFAANEL VRKLQPYKII FLTGTGGLLD ADGQVIDSIN LSTEYDHLIE
QPWLHGGMKV KIEQIKNLLE GLPMASSVSI TRPADLAKEL FTHKGSGTLV RRGEQVLRVT
DWSELDLARL KSLIESSFGR ELAPDYFERT PLLRAYVSEN YRAAVILTQG EGTVYLDKFA
VLDDAQGEGL GRAVWNVMRE ETPQLFWRSR HDNAVNIFYY AESDGCIKQP KWKVFWYGLD
GFEQIQRCVA HCETRVPTLV G
//
