ID A0A176QEV5_9MICO Unreviewed; 332 AA.
AC A0A176QEV5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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:QFQ30005.1};
GN ORFNames=AWH69_09060 {ECO:0000313|EMBL:OAB88226.1}, EEW87_006215
GN {ECO:0000313|EMBL:QFQ30005.1};
OS Janibacter melonis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=262209 {ECO:0000313|EMBL:OAB88226.1, ECO:0000313|Proteomes:UP000076976};
RN [1] {ECO:0000313|EMBL:OAB88226.1, ECO:0000313|Proteomes:UP000076976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD11-4 {ECO:0000313|EMBL:OAB88226.1,
RC ECO:0000313|Proteomes:UP000076976};
RA Nair G.R., Kaur G., Chander A.M., Mayilraj S.;
RT "Janibacter melonis strain CD11_4 genome sequencing and assembly.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QFQ30005.1, ECO:0000313|Proteomes:UP000271708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M714 {ECO:0000313|EMBL:QFQ30005.1,
RC ECO:0000313|Proteomes:UP000271708};
RA Jin M., Zhao Q.R.;
RT "Complete Genome Sequence of Janibacter melonis M714 with both human health
RT impact and industrial applications.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QFQ30005.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M714 {ECO:0000313|EMBL:QFQ30005.1};
RA Zhao Q.;
RL Submitted (NOV-2019) 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; LQZG01000002; OAB88226.1; -; Genomic_DNA.
DR EMBL; CP044548; QFQ30005.1; -; Genomic_DNA.
DR RefSeq; WP_068274434.1; NZ_JADAKY010000001.1.
DR AlphaFoldDB; A0A176QEV5; -.
DR STRING; 262209.AWH69_09060; -.
DR GeneID; 59160747; -.
DR KEGG; jme:EEW87_006215; -.
DR OrthoDB; 9803155at2; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000076976; Unassembled WGS sequence.
DR Proteomes; UP000271708; Chromosome.
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:UP000076976};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00082}.
FT DOMAIN 48..290
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT BINDING 87..88
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT SITE 52
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT SITE 271
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
SQ SEQUENCE 332 AA; 34783 MW; AE51C86DEF43E904 CRC64;
MRVTPPPSSD PSATLRGAID AAALRVARTK ATTLVEALPW LERFRGSLVV VKYGGNAMTD
DALKRAFAED VVFLRYAGLR PVVVHGGGPQ IAAMLDRLGL ESEFKGGLRV TTPEVMDVVR
MVLMGQVGRE LVGLLNQHGP VAVGLSGEDA GLFGGRRRGV EIDGQHVDIG LVGDVEHVEP
SAVQDVLDAG RIPVVSTIAP DLDVEGQVLN VNADTAAAAL AVALGAHKLV VLTDVEGIYA
DWPDRDSLLS QLSVSGARRL LERVDAGMIP KLEACIRAVE GGVPQAHVVD GRQPHSMLLE
IFTREGIGTM LVPDGTEAAA AADEALVSGS PS
//