ARGB_SALHS
ID ARGB_SALHS Reviewed; 257 AA.
AC B4TCQ5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=SeHA_C4450;
OS Salmonella heidelberg (strain SL476).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL476;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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 -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-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; CP001120; ACF67299.1; -; Genomic_DNA.
DR AlphaFoldDB; B4TCQ5; -.
DR SMR; B4TCQ5; -.
DR KEGG; seh:SeHA_C4450; -.
DR HOGENOM; CLU_053680_1_1_6; -.
DR OMA; EGLYEDW; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000001866; 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; cd04249; AAK_NAGK-NC; 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; IPR041731; NAGK-NC.
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..257
FT /note="Acetylglutamate kinase"
FT /id="PRO_1000092882"
FT BINDING 43..44
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 180..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 208..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 7
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 216
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ SEQUENCE 257 AA; 26876 MW; 0C8B0D704F220D3B CRC64;
MNPLIIKLGG VLLDSEEALE RLFTALVNYR ESHQRPLVIV HGGGCVVDEL MKGLNLPVKK
KDGLRVTPAD QIGIITGALA GTANKTLLAW AKKHHIASVG LFLGDGDSVN VTQLDEALGH
VGLAQPGSPK LINMLLENGF LPVVSSIGVT DDGQLMNVNA DQAATALAAT LGADLILLSD
VSGILDGKGQ RIAEMTASKA EQLIDQGIIT DGMIVKVNAA LDAARALGRP VDIASWRHAE
QLPALFNGTP IGTRILA
