ID   ARGB_METBF              Reviewed;         322 AA.
AC   Q46D93;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=Mbar_A1181;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(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; CP000099; AAZ70149.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46D93; -.
DR   SMR; Q46D93; -.
DR   STRING; 269797.Mbar_A1181; -.
DR   PRIDE; Q46D93; -.
DR   EnsemblBacteria; AAZ70149; AAZ70149; Mbar_A1181.
DR   KEGG; mba:Mbar_A1181; -.
DR   eggNOG; arCOG00862; Archaea.
DR   HOGENOM; CLU_053680_0_0_2; -.
DR   OMA; EGLYEDW; -.
DR   UniPathway; UPA00068; UER00107.
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   PIRSF; PIRSF000728; NAGK; 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; Transferase.
FT   CHAIN           1..322
FT                   /note="Acetylglutamate kinase"
FT                   /id="PRO_0000264789"
FT   BINDING         85..86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            50
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            274
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ   SEQUENCE   322 AA;  35205 MW;  7893B1F7190A6E99 CRC64;
     MWRLAITRVF NDKFKNRFSD SYIMELKREN VLIEALPYMQ EFYDSIMVIK VGGNAMVSAQ
     IMEDIIKDIV LLRYVGIKPV IVHGGGPEIT EKMGRMGKKA EFFQGLRITD DETMEIAKMV
     LVGNINTKIV SLIGVCGGKG IGLTGYDGRM ILGHKQAAKK VLINGIETEV DIGWVGECEV
     INPDILHIVL ENGYIPVISP IAVDAKGNAL NINADIVAGD IAAALHAKKL ILMTDVSGLL
     RDMNDPNSHI SRVTLEDIDH LIAEGVIQGG MIPKLKGAAV AVKNGVEKAH IINGSVSHSM
     LLELFTDRGI GTMVYKFEKP KN