ID A0A099W1V5_9LIST Unreviewed; 250 AA.
AC A0A099W1V5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Acetylglutamate kinase {ECO:0000256|HAMAP-Rule:MF_00082};
DE EC=2.7.2.8 {ECO:0000256|HAMAP-Rule:MF_00082};
DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00082};
DE AltName: Full=NAG kinase {ECO:0000256|HAMAP-Rule:MF_00082};
DE Short=NAGK {ECO:0000256|HAMAP-Rule:MF_00082};
GN Name=argB {ECO:0000256|HAMAP-Rule:MF_00082,
GN ECO:0000313|EMBL:MBC1245067.1};
GN ORFNames=EP57_14600 {ECO:0000313|EMBL:KGL38398.1}, HB759_06125
GN {ECO:0000313|EMBL:MBC1331528.1}, HB810_00555
GN {ECO:0000313|EMBL:MBC1245067.1}, HBP98_07725
GN {ECO:0000313|EMBL:MBC2371881.1}, HCA52_14250
GN {ECO:0000313|EMBL:MBC1794590.1}, HCA55_07870
GN {ECO:0000313|EMBL:MBC1796640.1}, HCA78_13850
GN {ECO:0000313|EMBL:MBC2004864.1}, HCB02_05695
GN {ECO:0000313|EMBL:MBC2104465.1}, HCB06_07780
GN {ECO:0000313|EMBL:MBC2116502.1}, HCB08_10440
GN {ECO:0000313|EMBL:MBC2207252.1}, HCB25_05235
GN {ECO:0000313|EMBL:MBC2243463.1}, HCB29_13350
GN {ECO:0000313|EMBL:MBC2164075.1}, HCJ32_11335
GN {ECO:0000313|EMBL:MBC1945538.1}, HCJ43_16030
GN {ECO:0000313|EMBL:MBC1976768.1};
OS Listeria booriae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1552123 {ECO:0000313|EMBL:KGL38398.1, ECO:0000313|Proteomes:UP000029844};
RN [1] {ECO:0000313|EMBL:KGL38398.1, ECO:0000313|Proteomes:UP000029844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL A5-0281 {ECO:0000313|EMBL:KGL38398.1,
RC ECO:0000313|Proteomes:UP000029844};
RA den Bakker H.C.;
RT "Novel Listeriaceae from food processing environments.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000528739, ECO:0000313|Proteomes:UP000529446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL L7-0153 {ECO:0000313|EMBL:MBC2243463.1,
RC ECO:0000313|Proteomes:UP000550367}, FSL L7-0217
RC {ECO:0000313|EMBL:MBC2207252.1, ECO:0000313|Proteomes:UP000572892},
RC FSL L7-0256 {ECO:0000313|EMBL:MBC2164075.1,
RC ECO:0000313|Proteomes:UP000528739}, FSL L7-0335
RC {ECO:0000313|EMBL:MBC2104465.1, ECO:0000313|Proteomes:UP000565263},
RC FSL L7-0360 {ECO:0000313|EMBL:MBC2116502.1,
RC ECO:0000313|Proteomes:UP000529446}, FSL L7-0435
RC {ECO:0000313|EMBL:MBC2004864.1, ECO:0000313|Proteomes:UP000546806},
RC FSL L7-0520 {ECO:0000313|EMBL:MBC1976768.1,
RC ECO:0000313|Proteomes:UP000587214}, FSL L7-0729
RC {ECO:0000313|EMBL:MBC1945538.1, ECO:0000313|Proteomes:UP000552349},
RC FSL L7-0978 {ECO:0000313|EMBL:MBC1794590.1,
RC ECO:0000313|Proteomes:UP000539064}, FSL L7-0990
RC {ECO:0000313|EMBL:MBC1796640.1, ECO:0000313|Proteomes:UP000548082},
RC FSL L7-1827 {ECO:0000313|EMBL:MBC1245067.1,
RC ECO:0000313|Proteomes:UP000574869}, FSL L7-1833
RC {ECO:0000313|EMBL:MBC1331528.1, ECO:0000313|Proteomes:UP000532866},
RC and FSL L7-1850 {ECO:0000313|EMBL:MBC2371881.1,
RC ECO:0000313|Proteomes:UP000546244};
RA Liao J., Wiedmann M.;
RT "Soil Listeria distribution.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-
CC glutamate. {ECO:0000256|HAMAP-Rule:MF_00082}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00082};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4. {ECO:0000256|ARBA:ARBA00004828,
CC ECO:0000256|HAMAP-Rule:MF_00082}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082}.
CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00082}.
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:KGL38398.1}.
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DR EMBL; JNFA01000029; KGL38398.1; -; Genomic_DNA.
DR EMBL; JAAROQ010000001; MBC1245067.1; -; Genomic_DNA.
DR EMBL; JAAROL010000001; MBC1331528.1; -; Genomic_DNA.
DR EMBL; JAARVG010000015; MBC1794590.1; -; Genomic_DNA.
DR EMBL; JAARVD010000003; MBC1796640.1; -; Genomic_DNA.
DR EMBL; JAASVH010000007; MBC1945538.1; -; Genomic_DNA.
DR EMBL; JAASWF010000016; MBC1976768.1; -; Genomic_DNA.
DR EMBL; JAARWW010000006; MBC2004864.1; -; Genomic_DNA.
DR EMBL; JAARXL010000002; MBC2104465.1; -; Genomic_DNA.
DR EMBL; JAARXI010000004; MBC2116502.1; -; Genomic_DNA.
DR EMBL; JAARYE010000006; MBC2164075.1; -; Genomic_DNA.
DR EMBL; JAARYN010000003; MBC2207252.1; -; Genomic_DNA.
DR EMBL; JAARYY010000003; MBC2243463.1; -; Genomic_DNA.
DR EMBL; JAARMV010000002; MBC2371881.1; -; Genomic_DNA.
DR RefSeq; WP_036087743.1; NZ_UGPF01000004.1.
DR AlphaFoldDB; A0A099W1V5; -.
DR STRING; 1552123.EP57_14600; -.
DR GeneID; 58718571; -.
DR eggNOG; COG0548; Bacteria.
DR OrthoDB; 9803155at2; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000029844; Unassembled WGS sequence.
DR Proteomes; UP000528739; Unassembled WGS sequence.
DR Proteomes; UP000529446; Unassembled WGS sequence.
DR Proteomes; UP000532866; Unassembled WGS sequence.
DR Proteomes; UP000539064; Unassembled WGS sequence.
DR Proteomes; UP000546244; Unassembled WGS sequence.
DR Proteomes; UP000546806; Unassembled WGS sequence.
DR Proteomes; UP000548082; Unassembled WGS sequence.
DR Proteomes; UP000550367; Unassembled WGS sequence.
DR Proteomes; UP000552349; Unassembled WGS sequence.
DR Proteomes; UP000565263; Unassembled WGS sequence.
DR Proteomes; UP000572892; Unassembled WGS sequence.
DR Proteomes; UP000574869; Unassembled WGS sequence.
DR Proteomes; UP000587214; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04238; AAK_NAGK-like; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR HAMAP; MF_00082; ArgB; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR037528; ArgB.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR001057; Glu/AcGlu_kinase.
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 PIRSF; PIRSF000728; NAGK; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00082};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_00082};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00082}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00082};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00082}; Reference proteome {ECO:0000313|Proteomes:UP000029844};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00082}.
FT DOMAIN 4..234
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT BINDING 41..42
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT SITE 8
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT SITE 215
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
SQ SEQUENCE 250 AA; 26270 MW; 9A0A14D76C719B04 CRC64;
MNEIIVVKIG GVAGSHLHES FFNQIKAWQE QGKQVVLVHG GGVQINKMME ALQIPVETKA
GLRVTTKETL AVTKMVLIGQ VQPEIVTALD QEGISAVGLH AGDAGLMHAE QLADKELGFV
GEITEVQTDL IQSLTEQQIV PVIAPLGLTT TAQWLNVNAD LAACAIAGAL EAEQLILLTD
VAGVLEEGKV MAQIDTADLE TLFAKEIITG GMIPKLASAK NAVTQGVGQV IITNEITKQG
TIISDGVKVG
//
