ID   ARGB_SHEHH              Reviewed;         270 AA.
AC   B0TL87;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 68.
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=Shal_4092;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABZ78632.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000931; ABZ78632.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_049763942.1; NC_010334.1.
DR   AlphaFoldDB; B0TL87; -.
DR   SMR; B0TL87; -.
DR   STRING; 458817.Shal_4092; -.
DR   EnsemblBacteria; ABZ78632; ABZ78632; Shal_4092.
DR   KEGG; shl:Shal_4092; -.
DR   eggNOG; COG0548; Bacteria.
DR   HOGENOM; CLU_053680_1_1_6; -.
DR   OrthoDB; 901370at2; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000001317; 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   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   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000728; NAGK; 1.
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; Transferase.
FT   CHAIN           1..270
FT                   /note="Acetylglutamate kinase"
FT                   /id="PRO_0000335663"
FT   BINDING         53..54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            18
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            226
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ   SEQUENCE   270 AA;  27994 MW;  0E1C05763BAC189D CRC64;
     MANTRAISSG AKPVMVLKVG GALLQCEMGM ARLMEAAAKI IANGQPIIMV HGGGCLVDEQ
     LKANGMTTKK LDGLRVTPQE QIPVIVGALA GTSNKTLQAA AIKAGVTSLG MSLADAGMMS
     AKVKDPQLGL VGEVEPKDAS YLEFVLSKGW MPIVSSIAIS EQGEMLNVNA DQAATALAKL
     VSGSLVLLSD VSGVLDGKGQ LISSLNRAQV NELTKIGVIE KGMKVKVEAA LDVAESMGQA
     VQIASWRHAQ QLIALSRGET VGTQIQPQIQ