ARGB_CLAMS
ID ARGB_CLAMS Reviewed; 303 AA.
AC B0RHD2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 91.
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=CMS1233;
OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX NCBI_TaxID=31964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX PubMed=18192393; DOI=10.1128/jb.01598-07;
RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA Parkhill J., Ishimaru C.A.;
RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT sepedonicus suggests recent niche adaptation.";
RL J. Bacteriol. 190:2150-2160(2008).
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=CAQ01349.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM849034; CAQ01349.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; B0RHD2; -.
DR SMR; B0RHD2; -.
DR STRING; 31964.CMS1233; -.
DR EnsemblBacteria; CAQ01349; CAQ01349; CMS1233.
DR KEGG; cms:CMS1233; -.
DR eggNOG; COG0548; Bacteria.
DR HOGENOM; CLU_053680_0_0_11; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000001318; 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_0000335620"
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 199
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 260
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ SEQUENCE 303 AA; 31762 MW; 23AD489729AD2327 CRC64;
MTAIAQQAAD RDQAQAESKA AILIESLSWL QRFHDRIVVV KFGGNAMVDE ELTRTFAEDV
VYLRYAGLRP VVVHGGGPQI SAMLTRLGID SEFRGGYRVT TPEVLEVVRM VLTGQVSRDV
VRGINAHGPL AAAVSGEDAG LFTGRRRGAV VDGVEVDLGL VGDVVSVDPT AVLAQLDAGR
IPVVSSIAPD ESDPAVSLNV NADAAAAALA VALGAEKLVI LTDVAGLYRD WPDRGSLVSD
IRADELRALL PSLESGMIPK MAACLEAVDG GVPKAAIIDG RIPHSMLLEI FTTNGIGTEV
VPA
