ID   ARGB_ENDTX              Reviewed;         249 AA.
AC   B1H0L5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=TGRD_564;
OS   Endomicrobium trichonymphae.
OC   Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC   Endomicrobium.
OX   NCBI_TaxID=1408204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Complete genome of the uncultured termite group 1 bacteria in a single
RT   host protist cell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008).
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; AP009510; BAG14047.1; -; Genomic_DNA.
DR   RefSeq; WP_015423572.1; NC_020419.1.
DR   RefSeq; YP_001956508.1; NC_020419.1.
DR   AlphaFoldDB; B1H0L5; -.
DR   SMR; B1H0L5; -.
DR   STRING; 471821.TGRD_564; -.
DR   EnsemblBacteria; BAG14047; BAG14047; TGRD_564.
DR   KEGG; rsd:TGRD_564; -.
DR   PATRIC; fig|471821.5.peg.914; -.
DR   HOGENOM; CLU_053680_0_0_0; -.
DR   OrthoDB; 901370at2; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000001691; 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   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; IPR001057; Glu/AcGlu_kinase.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000728; NAGK; 1.
DR   PRINTS; PR00474; GLU5KINASE.
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; Transferase.
FT   CHAIN           1..249
FT                   /note="Acetylglutamate kinase"
FT                   /id="PRO_1000202574"
FT   BINDING         42..43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            8
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            215
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ   SEQUENCE   249 AA;  26755 MW;  A4C2266C3EE05E9D CRC64;
     MSELTVVKFG GSLTENPQAQ NKFLEELTLI SKRQNIILVH GGGPEINALL EKFAITSRFV
     NGLRFTDADT LGVVELALSG KVNRVLTTGL IKNGANAVGI SGKDGKSVIC RQVEYLGFVG
     EPVKVNRKLI DILIKSRFLP VIASIAADVE GNIMNVNADT LAASIAVAFK AQKLIFLTDV
     AGVFDKNNNI IKEIKIKEIN SLIEDKTITG GMIPKIKGCA ESVKKGLKEV WIAEGISGIQ
     KIKGTVIKK