ARGB_DESRM
ID ARGB_DESRM Reviewed; 287 AA.
AC A4J169;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Dred_0273;
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
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., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) 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}.
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DR EMBL; CP000612; ABO48822.1; -; Genomic_DNA.
DR RefSeq; WP_011876660.1; NC_009253.1.
DR AlphaFoldDB; A4J169; -.
DR SMR; A4J169; -.
DR STRING; 349161.Dred_0273; -.
DR EnsemblBacteria; ABO48822; ABO48822; Dred_0273.
DR KEGG; drm:Dred_0273; -.
DR eggNOG; COG0548; Bacteria.
DR HOGENOM; CLU_053680_0_0_9; -.
DR OMA; EGLYEDW; -.
DR OrthoDB; 901370at2; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000001556; 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..287
FT /note="Acetylglutamate kinase"
FT /id="PRO_1000071217"
FT BINDING 64..65
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 29
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 244
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ SEQUENCE 287 AA; 30548 MW; B84A6EE0DAA3A2AF CRC64;
MISPLEKAGI LVEALPYIKK FSGKTIVIKY GGHAMLNADL KKAVMTDLVL MKFVGINPVV
VHGGGPEITG MLHRLGIESQ FVSGLRVTDA PTMEVVEMVL GKLNKEIVAL INGLGGRSVG
LSGKDANLIM ANKKYSNDCQ DIGFVGEVTG VNPQLLQTVI QEGYIPVVSP VGISTEGETY
NINADTVASA IATALKADKL IILTDVEGIL EDRQDKGTLI STVKMEDIPR LIERGVIQGG
MIPKVECCMQ AIQTGVATTH ILDGRVPHSI LLEVFTDKGI GTMVVSD
