ID   ARGB_SYNAS              Reviewed;         296 AA.
AC   Q2LT95;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=SYNAS_14260;
GN   ORFNames=SYN_02154;
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB;
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC77305.1; -; Genomic_DNA.
DR   RefSeq; WP_011417327.1; NC_007759.1.
DR   AlphaFoldDB; Q2LT95; -.
DR   SMR; Q2LT95; -.
DR   STRING; 56780.SYN_02154; -.
DR   EnsemblBacteria; ABC77305; ABC77305; SYN_02154.
DR   KEGG; sat:SYN_02154; -.
DR   eggNOG; COG0548; Bacteria.
DR   HOGENOM; CLU_053680_0_0_7; -.
DR   OMA; EGLYEDW; -.
DR   OrthoDB; 901370at2; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000001933; 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..296
FT                   /note="Acetylglutamate kinase"
FT                   /id="PRO_0000264777"
FT   BINDING         67..68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            32
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            254
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ   SEQUENCE   296 AA;  32072 MW;  17B31ACDCE69709D CRC64;
     MNTIEKPTEK AEILLEALPY IRRFYNRTVV IKYGGHAMVD DELKQSFAKD VLMMKYIGIN
     PVVVHGGGPQ IGSFLKKLGK DSKFIQGMRV TDEETMNIVE MVLVGKVNKE IVGLINHAGG
     KAVGLSGKDG SLIRAEKYYL SAEKAKDTPP EIIDIGLVGK VKEINADLIT SLVRDGFIPV
     IAPTGAGDSG ETYNINADIV AGAIAAALKA EKLILLTDVA GVLNKQGELI NTMNNMEALE
     MIHEGVIEGG MFPKVKCCMK SLREGVRKAH IVDGRLKHAI LLEMFTDKGI GTELVL