ID A0A0Q7PNF9_9GAMM Unreviewed; 440 AA.
AC A0A0Q7PNF9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=ASD14_05835 {ECO:0000313|EMBL:KQY52790.1};
OS Lysobacter sp. Root494.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1736549 {ECO:0000313|EMBL:KQY52790.1, ECO:0000313|Proteomes:UP000051738};
RN [1] {ECO:0000313|EMBL:KQY52790.1, ECO:0000313|Proteomes:UP000051738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root494 {ECO:0000313|EMBL:KQY52790.1,
RC ECO:0000313|Proteomes:UP000051738};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY52790.1, ECO:0000313|Proteomes:UP000051738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root494 {ECO:0000313|EMBL:KQY52790.1,
RC ECO:0000313|Proteomes:UP000051738};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQY52790.1}.
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DR EMBL; LMFH01000005; KQY52790.1; -; Genomic_DNA.
DR RefSeq; WP_056132168.1; NZ_LMFH01000005.1.
DR AlphaFoldDB; A0A0Q7PNF9; -.
DR STRING; 1736549.ASD14_05835; -.
DR OrthoDB; 9803155at2; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000051738; 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: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; 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; 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:KQY52790.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR036441};
KW Reference proteome {ECO:0000313|Proteomes:UP000051738};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036441}.
FT DOMAIN 293..439
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51731"
FT BINDING 78..79
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036441-50"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036441-50"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036441-50"
FT SITE 45
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR036441-51"
FT SITE 250
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR036441-51"
SQ SEQUENCE 440 AA; 48899 MW; A36BDC835A607B94 CRC64;
MNDARDIQTR QTIVRLLSSM ASAKEISQYL KRFSQLDAKR FAVVKVGGAV LRDDLDALTS
SLAFLQDVGL TPIVIHGAGP QLDEELSAAG IVKQTVNGLR ITSPEALAIV RRVFHSQNLK
LVESLQAFDA RATSIVSGVF EAEYLDRDTY GLVGEVKRVD LAPIEAALKA GSIPVIASLG
ETAGGQILNV NADFAANELV QVLQPYKIVF LTGTGGLLDD NGRVIDSINL STEYEHLIEQ
PWINGGMRVK IEQIKDLLDK LPLTSSVSIT KPSELAKELF THKGSGTLVR RGERVLEVSE
WKDLDPERLR GLIESAFGRR LVPDYFERTR LHRAYVSENY RAAVILTAED AGIYLDKFAV
LDEAQGEGLG RAVWQVMREQ NPRLFWRSRH GNSVNPFYYS ESDGCYKQEK WKVFWYGVEG
FGEIERCVAH CAMRVPTLAD
//
