ID A0A1W6LDP2_9BURK Unreviewed; 303 AA.
AC A0A1W6LDP2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:GLS97919.1};
GN ORFNames=A4W93_21930 {ECO:0000313|EMBL:ARN22347.1}, GCM10007918_52110
GN {ECO:0000313|EMBL:GLS97919.1};
OS Piscinibacter gummiphilus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Piscinibacter.
OX NCBI_TaxID=946333 {ECO:0000313|EMBL:ARN22347.1, ECO:0000313|Proteomes:UP000193427};
RN [1] {ECO:0000313|EMBL:ARN22347.1, ECO:0000313|Proteomes:UP000193427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS21 {ECO:0000313|EMBL:ARN22347.1,
RC ECO:0000313|Proteomes:UP000193427};
RA Tabata M., Kasai D., Fukuda M.;
RT "Complete genome sequence of natural rubber-degrading, novel Gram-negative
RT bacterium, Rhizobacter gummiphilus strain NS21.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GLS97919.1, ECO:0000313|Proteomes:UP001157201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 109400 {ECO:0000313|EMBL:GLS97919.1,
RC ECO:0000313|Proteomes:UP001157201};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [3] {ECO:0000313|EMBL:GLS97919.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 109400 {ECO:0000313|EMBL:GLS97919.1};
RA Sun Q., Mori K.;
RT "Draft genome sequence of Rhizobacter gummiphilus strain NBRC 109400.";
RL Submitted (JAN-2023) 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}.
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DR EMBL; CP015118; ARN22347.1; -; Genomic_DNA.
DR EMBL; BSPR01000020; GLS97919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6LDP2; -.
DR STRING; 946333.A4W93_21930; -.
DR KEGG; rgu:A4W93_21930; -.
DR OrthoDB; 9803155at2; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000193427; Chromosome.
DR Proteomes; UP001157201; 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; cd04250; AAK_NAGK-C; 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 InterPro; IPR041727; NAGK-C.
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:UP000193427};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00082}.
FT DOMAIN 36..279
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT BINDING 76..77
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT SITE 41
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT SITE 260
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
SQ SEQUENCE 303 AA; 32360 MW; BD36C9D43445F22A CRC64;
MSHEPPAAHD LTHIAPRDKA EILAEALPYI RKFHGKTIVI KYGGNAMTDP ALQQDFAEDV
VLLKLVGMNP VVVHGGGPQI EDALAKIGKK GTFIQGMRVT DEETMEVVEW VLAGQVQQDI
VGLINVAGGK AVGLTGRDGG LIRARKLRMV DHKDPSVVHD VGQVGEIESI DPSVVKALQD
DQFIPVISPL GFGANNENYN INADVVAGKL AEVLKAEKLM MLTNIPGVLD KAGNLLTNLS
AREIDELFAD GTISGGMLPK IASALEAAKN GVTAVHIIDG RVPHSMLLEI LSEQAYGTMI
RSH
//
