ID   ARGB_ECOLI              Reviewed;         258 AA.
AC   P0A6C8; P11445; Q2M8Q4;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 149.
DE   RecName: Full=Acetylglutamate kinase {ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000305};
DE            EC=2.7.2.8 {ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:10393305, ECO:0000269|PubMed:14623187};
DE   AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000305};
DE   AltName: Full=NAG kinase {ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000305};
DE            Short=NAGK {ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000303|PubMed:10393305};
GN   Name=argB {ECO:0000255|HAMAP-Rule:MF_00082,
GN   ECO:0000303|PubMed:2851495}; OrderedLocusNames=b3959, JW5553;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2851495; DOI=10.1016/0378-1119(88)90030-3;
RA   Parsot C., Boyen A., Cohen G.N., Glansdorff N.;
RT   "Nucleotide sequence of Escherichia coli argB and argC genes: comparison of
RT   N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde
RT   dehydrogenase with homologous and analogous enzymes.";
RL   Gene 68:275-283(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA   Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT   "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT   from 89.2 to 92.8 minutes.";
RL   Nucleic Acids Res. 21:5408-5417(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-8, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP   CRYSTALLIZATION.
RX   PubMed=10393305; DOI=10.1107/s0907444999005351;
RA   Gil F., Ramon-Maiques S., Marina A., Fita I., Rubio V.;
RT   "N-acetyl-L-glutamate kinase from Escherichia coli: cloning of the gene,
RT   purification and crystallization of the recombinant enzyme and preliminary
RT   X-ray analysis of the free and ligand-bound forms.";
RL   Acta Crystallogr. D 55:1350-1352(1999).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   MUTAGENESIS OF LYS-8; ARG-66; ASN-158 AND ASP-162.
RX   PubMed=14623187; DOI=10.1016/j.jmb.2003.09.038;
RA   Marco-Marin C., Ramon-Maiques S., Tavarez S., Rubio V.;
RT   "Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and
RT   aspartokinase III probes the catalytic and substrate-binding mechanisms of
RT   these amino acid kinase family enzymes and allows three-dimensional
RT   modelling of aspartokinase.";
RL   J. Mol. Biol. 334:459-476(2003).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ATP
RP   ANALOG, AND SUBUNIT.
RX   PubMed=12005432; DOI=10.1016/s0969-2126(02)00721-9;
RA   Ramon-Maiques S., Marina A., Gil-Ortiz F., Fita I., Rubio V.;
RT   "Structure of acetylglutamate kinase, a key enzyme for arginine
RT   biosynthesis and a prototype for the amino acid kinase enzyme family,
RT   during catalysis.";
RL   Structure 10:329-342(2002).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; ATP AND
RP   TRANSITION STATE ANALOG.
RX   PubMed=12875848; DOI=10.1016/s0022-2836(03)00716-2;
RA   Gil-Ortiz F., Ramon-Maiques S., Fita I., Rubio V.;
RT   "The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase,
RT   determined from the structures of crystalline complexes, including a
RT   complex with an AlF(4)(-) transition state mimic.";
RL   J. Mol. Biol. 331:231-244(2003).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-
CC       glutamate. {ECO:0000255|HAMAP-Rule:MF_00082,
CC       ECO:0000269|PubMed:10393305, ECO:0000269|PubMed:14623187}.
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         ECO:0000269|PubMed:10393305, ECO:0000269|PubMed:14623187};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.2 mM for N-acetyl-L-glutamate {ECO:0000269|PubMed:14623187};
CC         KM=0.29 mM for ATP {ECO:0000269|PubMed:14623187};
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, ECO:0000305}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00082,
CC       ECO:0000269|PubMed:10393305, ECO:0000269|PubMed:12005432,
CC       ECO:0000269|PubMed:12875848}.
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, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE77352.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M21446; AAA23478.1; -; Genomic_DNA.
DR   EMBL; U00006; AAC43065.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76941.3; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77352.1; ALT_INIT; Genomic_DNA.
DR   PIR; JT0331; KIECAE.
DR   RefSeq; NP_418394.3; NC_000913.3.
DR   RefSeq; WP_001302318.1; NZ_STEB01000037.1.
DR   PDB; 1GS5; X-ray; 1.50 A; A=1-258.
DR   PDB; 1GSJ; X-ray; 1.85 A; A=1-258.
DR   PDB; 1OH9; X-ray; 1.91 A; A=1-258.
DR   PDB; 1OHA; X-ray; 1.90 A; A=1-258.
DR   PDB; 1OHB; X-ray; 1.90 A; A=1-258.
DR   PDB; 2WXB; X-ray; 2.00 A; A/B=1-258.
DR   PDB; 2X2W; X-ray; 2.00 A; A/B=1-258.
DR   PDBsum; 1GS5; -.
DR   PDBsum; 1GSJ; -.
DR   PDBsum; 1OH9; -.
DR   PDBsum; 1OHA; -.
DR   PDBsum; 1OHB; -.
DR   PDBsum; 2WXB; -.
DR   PDBsum; 2X2W; -.
DR   AlphaFoldDB; P0A6C8; -.
DR   SMR; P0A6C8; -.
DR   BioGRID; 4261889; 7.
DR   DIP; DIP-9136N; -.
DR   IntAct; P0A6C8; 2.
DR   STRING; 511145.b3959; -.
DR   DrugBank; DB04075; N-Acetyl-L-Glutamate.
DR   DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR   DrugBank; DB04444; Tetrafluoroaluminate Ion.
DR   jPOST; P0A6C8; -.
DR   PaxDb; 511145-b3959; -.
DR   EnsemblBacteria; AAC76941; AAC76941; b3959.
DR   GeneID; 75203211; -.
DR   GeneID; 948464; -.
DR   KEGG; ecj:JW5553; -.
DR   KEGG; eco:b3959; -.
DR   PATRIC; fig|1411691.4.peg.2746; -.
DR   EchoBASE; EB0062; -.
DR   eggNOG; COG0548; Bacteria.
DR   HOGENOM; CLU_053680_1_1_6; -.
DR   InParanoid; P0A6C8; -.
DR   OMA; HVYNVNA; -.
DR   OrthoDB; 5915023at2; -.
DR   PhylomeDB; P0A6C8; -.
DR   BioCyc; EcoCyc:ACETYLGLUTKIN-MONOMER; -.
DR   BioCyc; MetaCyc:ACETYLGLUTKIN-MONOMER; -.
DR   BRENDA; 2.7.2.8; 2026.
DR   SABIO-RK; P0A6C8; -.
DR   UniPathway; UPA00068; UER00107.
DR   EvolutionaryTrace; P0A6C8; -.
DR   PRO; PR:P0A6C8; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:arginine biosynthetic process; IDA:EcoCyc.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
DR   GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04249; AAK_NAGK-NC; 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; IPR041731; NAGK-NC.
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   SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10393305"
FT   CHAIN           2..258
FT                   /note="Acetylglutamate kinase"
FT                   /id="PRO_0000112614"
FT   BINDING         44..45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082,
FT                   ECO:0000269|PubMed:12005432, ECO:0000269|PubMed:12875848"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082,
FT                   ECO:0000269|PubMed:12005432, ECO:0000269|PubMed:12875848"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082,
FT                   ECO:0000269|PubMed:12005432, ECO:0000269|PubMed:12875848"
FT   BINDING         181..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082,
FT                   ECO:0000269|PubMed:12875848"
FT   BINDING         209..211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082,
FT                   ECO:0000269|PubMed:12875848"
FT   SITE            8
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082,
FT                   ECO:0000305|PubMed:12875848"
FT   SITE            217
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082,
FT                   ECO:0000305|PubMed:12875848"
FT   MUTAGEN         8
FT                   /note="K->R: Reduces activity 50-fold. Increases KM for
FT                   N-acetyl-L-glutamate and ATP about 10-fold."
FT                   /evidence="ECO:0000269|PubMed:14623187"
FT   MUTAGEN         66
FT                   /note="R->K: Increases KM for N-acetyl-L-glutamate over
FT                   1000-fold. Increases KM for ATP nearly 20-fold."
FT                   /evidence="ECO:0000269|PubMed:14623187"
FT   MUTAGEN         158
FT                   /note="N->Q: Increases KM for N-acetyl-L-glutamate over
FT                   1000-fold. Increases KM for ATP over 20-fold."
FT                   /evidence="ECO:0000269|PubMed:14623187"
FT   MUTAGEN         162
FT                   /note="D->E: Reduces activity over 99%. No effect on KM for
FT                   N-acetyl-L-glutamate and ATP."
FT                   /evidence="ECO:0000269|PubMed:14623187"
FT   STRAND          5..9
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   HELIX           11..15
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   HELIX           17..31
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   STRAND          38..42
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   HELIX           45..55
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   STRAND          61..66
FT                   /evidence="ECO:0007829|PDB:2X2W"
FT   HELIX           70..81
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   HELIX           83..94
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   STRAND          99..102
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   HELIX           106..108
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   STRAND          110..114
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   STRAND          120..127
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   HELIX           131..138
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   STRAND          142..145
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   STRAND          147..150
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   HELIX           161..172
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   STRAND          175..184
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   STRAND          194..197
FT                   /evidence="ECO:0007829|PDB:2WXB"
FT   HELIX           198..206
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   HELIX           213..228
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   STRAND          232..238
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   HELIX           240..242
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   HELIX           243..247
FT                   /evidence="ECO:0007829|PDB:1GS5"
FT   STRAND          252..256
FT                   /evidence="ECO:0007829|PDB:1GS5"
SQ   SEQUENCE   258 AA;  27160 MW;  8B916B8CBC143738 CRC64;
     MMNPLIIKLG GVLLDSEEAL ERLFSALVNY RESHQRPLVI VHGGGCVVDE LMKGLNLPVK
     KKNGLRVTPA DQIDIITGAL AGTANKTLLA WAKKHQIAAV GLFLGDGDSV KVTQLDEELG
     HVGLAQPGSP KLINSLLENG YLPVVSSIGV TDEGQLMNVN ADQAATALAA TLGADLILLS
     DVSGILDGKG QRIAEMTAAK AEQLIEQGII TDGMIVKVNA ALDAARTLGR PVDIASWRHA
     EQLPALFNGM PMGTRILA
//