ID   ARGB_CHLPD              Reviewed;         303 AA.
AC   A1BG26;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 81.
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=Cpha266_1322;
OS   Chlorobium phaeobacteroides (strain DSM 266).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 266;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABL65353.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000492; ABL65353.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041467235.1; NC_008639.1.
DR   AlphaFoldDB; A1BG26; -.
DR   SMR; A1BG26; -.
DR   STRING; 290317.Cpha266_1322; -.
DR   EnsemblBacteria; ABL65353; ABL65353; Cpha266_1322.
DR   KEGG; cph:Cpha266_1322; -.
DR   eggNOG; COG0548; Bacteria.
DR   HOGENOM; CLU_053680_0_0_10; -.
DR   OrthoDB; 901370at2; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000008701; 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; -; 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   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; Reference proteome; Transferase.
FT   CHAIN           1..303
FT                   /note="Acetylglutamate kinase"
FT                   /id="PRO_0000335617"
FT   BINDING         76..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            41
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            251
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ   SEQUENCE   303 AA;  32373 MW;  F69B40FF6C1B3FFC CRC64;
     MNPLCSELKS GRNAPPAAIG QVLIEALPYI RKFEGKTFVI KYGGSAMKDD KLKNSFAQNV
     TLLRKVGINV VLVHGGGDAI TRTAEKMGLS SRFHHGKRVT DIEMISVVQM TLAGKVNQDI
     VRLISEHGGK AVGVTGLDAD TIKAIPCQNA DKLGLVGDVE SINTLYIDLL CRAGLIPVIA
     PIGYDEDGSI YNINADDAAS SIAIALKAEK LIYVSDVEGI HVGERILKTI CKAEAADFIE
     QGIISGGMIP KVLSAFKTLD GGVGKIHLID GKFTHSLLLE IFTHEGVGTQ FIAEQDNDNP
     GKR