ID   ARGB_RHORT              Reviewed;         310 AA.
AC   Q2RP10;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=Rru_A3341;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(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   -!- 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; CP000230; ABC24135.1; -; Genomic_DNA.
DR   RefSeq; WP_011391088.1; NC_007643.1.
DR   RefSeq; YP_428422.1; NC_007643.1.
DR   AlphaFoldDB; Q2RP10; -.
DR   SMR; Q2RP10; -.
DR   STRING; 269796.Rru_A3341; -.
DR   EnsemblBacteria; ABC24135; ABC24135; Rru_A3341.
DR   KEGG; rru:Rru_A3341; -.
DR   PATRIC; fig|269796.9.peg.3455; -.
DR   eggNOG; COG0548; Bacteria.
DR   HOGENOM; CLU_053680_0_0_5; -.
DR   OMA; EGLYEDW; -.
DR   OrthoDB; 901370at2; -.
DR   PhylomeDB; Q2RP10; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000001929; 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..310
FT                   /note="Acetylglutamate kinase"
FT                   /id="PRO_0000264750"
FT   BINDING         79..80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            44
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            266
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ   SEQUENCE   310 AA;  33191 MW;  0FB73C685FEBF71D CRC64;
     MMTDSAPPEP IHAEIPEGWL HKAKTLSEAL PYMRRFAGLT IVIKYGGHAM GDPELAKTFA
     RDVVLLKQVG MNPVVVHGGG PQIGRMLDTL RIQSTFIDGL RVTDAATVDV VEMVLAGSIN
     KAIVTEINQA GGCAVGLSGK DGRLIQARKM VRKRHDPESN IERVLDLGFV GEPVVIDPHV
     LIQFRDSDII PVIAPIGIGE AGETFNINAD TAAGALAAQM KAARLLMLTD VKGVLDKDKQ
     LIQELSVDRA RLLKQEGTIS GGMIPKVETC IDAVERGVEA AVIVDGRVPH AVLLEIFTPR
     GAGTLIRASR