ID   C1DAY0_LARHH            Unreviewed;       300 AA.
AC   C1DAY0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   02-SEP-2026, entry version 94.
DE   RecName: Full=Acetylglutamate kinase {ECO:0000256|HAMAP-Rule:MF_00082};
DE            EC=2.7.2.8 {ECO:0000256|HAMAP-Rule:MF_00082};
DE   AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00082};
DE   AltName: Full=NAG kinase {ECO:0000256|HAMAP-Rule:MF_00082};
DE            Short=NAGK {ECO:0000256|HAMAP-Rule:MF_00082};
GN   Name=argB-1 {ECO:0000313|EMBL:ACO75319.1};
GN   Synonyms=argB {ECO:0000256|HAMAP-Rule:MF_00082};
GN   OrderedLocusNames=LHK_02337 {ECO:0000313|EMBL:ACO75319.1};
OS   Laribacter hongkongensis (strain HLHK9).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Laribacter.
OX   NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO75319.1, ECO:0000313|Proteomes:UP000002010};
RN   [1] {ECO:0000313|EMBL:ACO75319.1, ECO:0000313|Proteomes:UP000002010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLHK9 {ECO:0000313|EMBL:ACO75319.1,
RC   ECO:0000313|Proteomes:UP000002010};
RX   PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA   Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA   Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA   Pallen M.J., Lok S., Yuen K.Y.;
RT   "The complete genome and proteome of Laribacter hongkongensis reveal
RT   potential mechanisms for adaptations to different temperatures and
RT   habitats.";
RL   PLoS Genet. 5:E1000416-E1000416(2009).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-
CC       glutamate. {ECO:0000256|HAMAP-Rule:MF_00082}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-L-glutamate + ATP = N-acetyl-L-glutamyl 5-phosphate +
CC         ADP; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337,
CC         ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00048141, ECO:0000256|HAMAP-
CC         Rule:MF_00082};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 2/4. {ECO:0000256|ARBA:ARBA00004828,
CC       ECO:0000256|HAMAP-Rule:MF_00082}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082}.
CC   -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00082}.
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DR   EMBL; CP001154; ACO75319.1; -; Genomic_DNA.
DR   RefSeq; WP_012697805.1; NC_012559.1.
DR   AlphaFoldDB; C1DAY0; -.
DR   STRING; 557598.LHK_02337; -.
DR   GeneID; 75110010; -.
DR   KEGG; lhk:LHK_02337; -.
DR   eggNOG; COG0548; Bacteria.
DR   HOGENOM; CLU_053680_0_0_4; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000002010; 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:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04250; AAK_NAGK-C; 1.
DR   FunFam; 3.40.1160.10:FF:000004; Acetylglutamate kinase; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 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; IPR041727; NAGK-C.
DR   NCBIfam; TIGR00761; argB; 1.
DR   PANTHER; PTHR23342; N-ACETYLGLUTAMATE SYNTHASE; 1.
DR   PANTHER; PTHR23342:SF0; N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000728; NAGK; 1.
DR   PRINTS; PR01469; CARBMTKINASE.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00082};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   Rule:MF_00082};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00082}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00082};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00082}; Reference proteome {ECO:0000313|Proteomes:UP000002010};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00082}.
FT   DOMAIN          34..275
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
FT   BINDING         74..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT   SITE            39
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT   SITE            256
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
SQ   SEQUENCE   300 AA;  31515 MW;  958CE2ABDADE618F CRC64;
     MVIQSEVPAH LHNAQDTAAI LAEALPYIRA FSGKTIVVKY GGNAMTDPEL KAGFARDVVM
     LKLVGLNPVV VHGGGPQINQ LLSRLGKQGE FVSGMRVTDD ETMDVVEMVL GGLVNKEIVS
     LINQAGGKAV GLTGLDGHFI RARKLYVQDE QDTTVDIGKV GEVDSIDPTV VGLLTTQDFI
     PVIAPIGVGP DGAAYNINAD LVAGKLAETL HAEKLILMTN TSGVLDRQGQ LISHLDSERA
     ATLFADGTIS GGMIPKVQSA LDTTRQGVGS VHIIDGRVKH ALLLEILTDL GTGTAICTTL
//