ID   ARGB_CYAM1              Reviewed;         290 AA.
AC   Q85FW5;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, 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};
OS   Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC   Cyanidioschyzon.
OX   NCBI_TaxID=280699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3377 / 10D;
RX   PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA   Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA   Shin-i T., Kohara Y., Kuroiwa T.;
RT   "Complete sequence and analysis of the plastid genome of the unicellular
RT   red alga Cyanidioschyzon merolae.";
RL   DNA Res. 10:67-77(2003).
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: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       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; AB002583; BAC76228.1; -; Genomic_DNA.
DR   RefSeq; NP_849066.1; NC_004799.1.
DR   AlphaFoldDB; Q85FW5; -.
DR   SMR; Q85FW5; -.
DR   STRING; 45157.CMV160CT; -.
DR   EnsemblPlants; CMV160CT; CMV160CT; CMV160C.
DR   GeneID; 844864; -.
DR   Gramene; CMV160CT; CMV160CT; CMV160C.
DR   KEGG; cme:CymeCp134; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_053680_0_1_1; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000007014; Chloroplast.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0034618; F:arginine binding; IEA:EnsemblPlants.
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; Chloroplast;
KW   Kinase; Nucleotide-binding; Plastid; Reference proteome; Transferase.
FT   CHAIN           1..290
FT                   /note="Acetylglutamate kinase"
FT                   /id="PRO_0000112707"
FT   BINDING         72..73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            40
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            248
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ   SEQUENCE   290 AA;  31476 MW;  274F9419D35203C0 CRC64;
     MQQQINPEII QEISDDLRVQ VLTEALPYIQ KWRNEIMVIK YGGAVVKQDA DIIKDILFLT
     CCGFQIVVVH GGGPLINEWL KQLNKSPQYW EGIRVTDKVT MEIVEMVLAG KVNKQLVGSI
     NANGGKAIGL CGKDANLIVA KASSKKELGL VGEIEQIHPQ VIDMLLEKHY IPVIASVAAS
     HDGTTYNLNA DVVAGELAIK LKAKKLIFLT DTKGILADIN NENSVISTLN LKEAKNLANT
     ISGGMIPKVN ACICAVENGV EAAHIIGGKE KHQLLLELLT EKGRGSMIVV