ARGB_ECOLI
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 03-AUG-2022, entry version 141.
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, ECO:0000303|PubMed:2851495};
GN OrderedLocusNames=b3959, JW5553;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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=0.20 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; P0A6C8; -.
DR PRIDE; P0A6C8; -.
DR EnsemblBacteria; AAC76941; AAC76941; b3959.
DR EnsemblBacteria; BAE77352; BAE77352; BAE77352.
DR GeneID; 66672131; -.
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; EGLYEDW; -.
DR PhylomeDB; P0A6C8; -.
DR BioCyc; EcoCyc:ACETYLGLUTKIN-MON; -.
DR BioCyc; MetaCyc:ACETYLGLUTKIN-MON; -.
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:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04249; AAK_NAGK-NC; 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; IPR041731; NAGK-NC.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF000728; NAGK; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR TIGRFAMs; TIGR00761; argB; 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 N-
FT 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 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 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
