ID   ARGB_CUPNH              Reviewed;         305 AA.
AC   Q0KF61;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Acetylglutamate kinase {ECO:0000255|HAMAP-Rule:MF_00082};
DE            EC=2.7.2.8 {ECO:0000255|HAMAP-Rule:MF_00082};
DE   AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00082};
DE   AltName: Full=NAG kinase {ECO:0000255|HAMAP-Rule:MF_00082};
DE            Short=NAGK {ECO:0000255|HAMAP-Rule:MF_00082};
GN   Name=argB {ECO:0000255|HAMAP-Rule:MF_00082}; OrderedLocusNames=H16_A0208;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-
CC       glutamate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00082};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 2/4. {ECO:0000255|HAMAP-
CC       Rule:MF_00082}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00082}.
CC   -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00082}.
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DR   EMBL; AM260479; CAJ91360.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0KF61; -.
DR   SMR; Q0KF61; -.
DR   STRING; 381666.H16_A0208; -.
DR   EnsemblBacteria; CAJ91360; CAJ91360; H16_A0208.
DR   KEGG; reh:H16_A0208; -.
DR   eggNOG; COG0548; Bacteria.
DR   HOGENOM; CLU_053680_0_0_4; -.
DR   OMA; EGLYEDW; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000008210; Chromosome 1.
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; -; 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; IPR041727; NAGK-C.
DR   Pfam; PF00696; AA_kinase; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00761; argB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW   Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..305
FT                   /note="Acetylglutamate kinase"
FT                   /id="PRO_0000335657"
FT   BINDING         78..79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            43
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            262
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ   SEQUENCE   305 AA;  32502 MW;  65210E5B48507323 CRC64;
     MNADNPGPAA TTVAAIAPAL KAEILAEALP YIRKFHGKTI VVKYGGNAMT EEKLKHGFAR
     DVILLKLVGM NPVVVHGGGP QIDEALKKVG KVGTFVQGMR VTDEETMEVV EWVLGGEVQQ
     DIVMLINQYG GQAVGLTGKD GGLIRAKRLQ MPDRENPGAF IDIGYVGDIE AINPAVVKAL
     QDDAFIPVIS PIGFSDDGQA YNINADVVAG KMAEILKAEK LVMMTNIPGV MDKKGNLLTD
     LSAREIEELF ADGTISGGML PKISSALDAA KSGVHSVHII DGRIEHSLLL EILTEQAFGT
     MIRSH