ID   ARGB_PELUB              Reviewed;         288 AA.
AC   Q4FNF2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   02-SEP-2026, entry version 116.
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};
GN   OrderedLocusNames=SAR11_0465;
OS   Pelagibacter ubique (strain HTCC1062).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Candidatus Pelagibacterales; Candidatus Pelagibacteraceae;
OC   Candidatus Pelagibacter.
OX   NCBI_TaxID=335992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062;
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA   Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA   Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(2005).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-
CC       glutamate. {ECO:0000255|HAMAP-Rule:MF_00082}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-L-glutamate + ATP = N-acetyl-L-glutamyl 5-phosphate +
CC         ADP; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337,
CC         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; CP000084; AAZ21287.1; -; Genomic_DNA.
DR   RefSeq; WP_011281731.1; NC_007205.1.
DR   AlphaFoldDB; Q4FNF2; -.
DR   SMR; Q4FNF2; -.
DR   STRING; 335992.SAR11_0465; -.
DR   GeneID; 66294964; -.
DR   KEGG; pub:SAR11_0465; -.
DR   eggNOG; COG0548; Bacteria.
DR   HOGENOM; CLU_053680_0_0_5; -.
DR   OrthoDB; 9803155at2; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000002528; 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:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04250; AAK_NAGK-C; 1.
DR   FunFam; 3.40.1160.10:FF:000004; Acetylglutamate kinase; 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; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW   Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..288
FT                   /note="Acetylglutamate kinase"
FT                   /id="PRO_0000264728"
FT   BINDING         73..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            38
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            246
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ   SEQUENCE   288 AA;  31886 MW;  DE374EB344751582 CRC64;
     MSSLREEELI NILPKDGPTV EEVKKYLEKY NDEFIIIKCG GSVLVDPKLF KVFIEDVVVL
     KKLGFNPIIV HGGGKRINSK LLEVNIKSNF INGLRVTDKD TINIVEDVLI EFNKEIVEAL
     NELDCKAKRI TSKENNIITV VQENKDLGFV GRPTGINKEF LTEIIKANKV PVIAPLGLDK
     DNQTFNINAD TTAGSIAIEL KARRLMIISD VEGVLDSEKK LIPEINSKKA NELIDQEVIS
     GGMIPKIKNC LDVASNGVKA VVIIDGRKNH SLLFELLSDK GSGTLIRE
//