Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetylglutamate kinase

Gene

argB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate.

Pathway: L-arginine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Amino-acid acetyltransferase (argA), Amino-acid acetyltransferase (argA)
  2. Acetylglutamate kinase (argB), Acetylglutamate kinase (argB)
  3. N-acetyl-gamma-glutamyl-phosphate reductase (argC), N-acetyl-gamma-glutamyl-phosphate reductase (argC)
  4. Acetylornithine/succinyldiaminopimelate aminotransferase (argD), Acetylornithine/succinyldiaminopimelate aminotransferase (argD)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei8 – 81Transition state stabilizer
Binding sitei66 – 661Substrate2 Publications
Binding sitei158 – 1581Substrate2 Publications
Sitei217 – 2171Transition state stabilizer

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi181 – 1866ATP1 Publication
Nucleotide bindingi209 – 2113ATP1 Publication

GO - Molecular functioni

  • acetylglutamate kinase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-HAMAP

GO - Biological processi

  • arginine biosynthetic process Source: EcoCyc
  • cellular response to DNA damage stimulus Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ACETYLGLUTKIN-MONOMER.
ECOL316407:JW5553-MONOMER.
MetaCyc:ACETYLGLUTKIN-MONOMER.
BRENDAi2.7.2.8. 2026.
SABIO-RKP0A6C8.
UniPathwayiUPA00068; UER00107.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylglutamate kinase (EC:2.7.2.8)
Alternative name(s):
N-acetyl-L-glutamate 5-phosphotransferase
NAG kinase
Short name:
AGK
Gene namesi
Name:argB
Ordered Locus Names:b3959, JW5553
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10064. argB.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81K → R: Reduces activity 50-fold. Increases KM for N-acetyl-L-glutamate and ATP about 10-fold. 1 Publication
Mutagenesisi66 – 661R → K: Increases KM for N-acetyl-L-glutamate over 1000-fold. Increases KM for ATP nearly 20-fold. 1 Publication
Mutagenesisi158 – 1581N → Q: Increases KM for N-acetyl-L-glutamate over 1000-fold. Increases KM for ATP over 20-fold. 1 Publication
Mutagenesisi162 – 1621D → E: Reduces activity over 99%. No effect on KM for N-acetyl-L-glutamate and ATP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 258258Acetylglutamate kinasePRO_0000112614Add
BLAST

Proteomic databases

PaxDbiP0A6C8.
PRIDEiP0A6C8.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

DIPiDIP-9136N.
IntActiP0A6C8. 2 interactions.
MINTiMINT-1309378.
STRINGi511145.b3959.

Structurei

Secondary structure

1
258
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Helixi11 – 155Combined sources
Helixi17 – 3115Combined sources
Beta strandi38 – 425Combined sources
Helixi45 – 5511Combined sources
Helixi70 – 8112Combined sources
Helixi83 – 9412Combined sources
Beta strandi99 – 1024Combined sources
Helixi106 – 1083Combined sources
Beta strandi110 – 1145Combined sources
Helixi117 – 1193Combined sources
Beta strandi120 – 1278Combined sources
Helixi131 – 1388Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi147 – 1504Combined sources
Beta strandi156 – 1583Combined sources
Helixi161 – 17212Combined sources
Beta strandi175 – 18410Combined sources
Helixi198 – 2069Combined sources
Helixi213 – 22816Combined sources
Beta strandi232 – 2387Combined sources
Helixi240 – 2423Combined sources
Helixi243 – 2475Combined sources
Beta strandi252 – 2565Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GS5X-ray1.50A1-258[»]
1GSJX-ray1.85A1-258[»]
1OH9X-ray1.91A1-258[»]
1OHAX-ray1.90A1-258[»]
1OHBX-ray1.90A1-258[»]
2WXBX-ray2.00A/B1-258[»]
2X2WX-ray2.00A/B1-258[»]
ProteinModelPortaliP0A6C8.
SMRiP0A6C8. Positions 1-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6C8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 452Substrate binding

Sequence similaritiesi

Belongs to the acetylglutamate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0548.
HOGENOMiHOG000233260.
InParanoidiP0A6C8.
KOiK00930.
OMAiGIESKMV.
OrthoDBiEOG6JB13D.
PhylomeDBiP0A6C8.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
HAMAPiMF_00082_B. ArgB_B.
InterProiIPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000728. NAGK. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00761. argB. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6C8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMNPLIIKLG GVLLDSEEAL ERLFSALVNY RESHQRPLVI VHGGGCVVDE
60 70 80 90 100
LMKGLNLPVK KKNGLRVTPA DQIDIITGAL AGTANKTLLA WAKKHQIAAV
110 120 130 140 150
GLFLGDGDSV KVTQLDEELG HVGLAQPGSP KLINSLLENG YLPVVSSIGV
160 170 180 190 200
TDEGQLMNVN ADQAATALAA TLGADLILLS DVSGILDGKG QRIAEMTAAK
210 220 230 240 250
AEQLIEQGII TDGMIVKVNA ALDAARTLGR PVDIASWRHA EQLPALFNGM

PMGTRILA
Length:258
Mass (Da):27,160
Last modified:June 7, 2005 - v1
Checksum:i8B916B8CBC143738
GO

Sequence cautioni

The sequence BAE77352.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21446 Genomic DNA. Translation: AAA23478.1.
U00006 Genomic DNA. Translation: AAC43065.1.
U00096 Genomic DNA. Translation: AAC76941.3.
AP009048 Genomic DNA. Translation: BAE77352.1. Different initiation.
PIRiJT0331. KIECAE.
RefSeqiNP_418394.3. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76941; AAC76941; b3959.
BAE77352; BAE77352; BAE77352.
GeneIDi948464.
KEGGiecj:Y75_p3229.
eco:b3959.
PATRICi32123439. VBIEscCol129921_4080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21446 Genomic DNA. Translation: AAA23478.1.
U00006 Genomic DNA. Translation: AAC43065.1.
U00096 Genomic DNA. Translation: AAC76941.3.
AP009048 Genomic DNA. Translation: BAE77352.1. Different initiation.
PIRiJT0331. KIECAE.
RefSeqiNP_418394.3. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GS5X-ray1.50A1-258[»]
1GSJX-ray1.85A1-258[»]
1OH9X-ray1.91A1-258[»]
1OHAX-ray1.90A1-258[»]
1OHBX-ray1.90A1-258[»]
2WXBX-ray2.00A/B1-258[»]
2X2WX-ray2.00A/B1-258[»]
ProteinModelPortaliP0A6C8.
SMRiP0A6C8. Positions 1-258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9136N.
IntActiP0A6C8. 2 interactions.
MINTiMINT-1309378.
STRINGi511145.b3959.

Proteomic databases

PaxDbiP0A6C8.
PRIDEiP0A6C8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76941; AAC76941; b3959.
BAE77352; BAE77352; BAE77352.
GeneIDi948464.
KEGGiecj:Y75_p3229.
eco:b3959.
PATRICi32123439. VBIEscCol129921_4080.

Organism-specific databases

EchoBASEiEB0062.
EcoGeneiEG10064. argB.

Phylogenomic databases

eggNOGiCOG0548.
HOGENOMiHOG000233260.
InParanoidiP0A6C8.
KOiK00930.
OMAiGIESKMV.
OrthoDBiEOG6JB13D.
PhylomeDBiP0A6C8.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00107.
BioCyciEcoCyc:ACETYLGLUTKIN-MONOMER.
ECOL316407:JW5553-MONOMER.
MetaCyc:ACETYLGLUTKIN-MONOMER.
BRENDAi2.7.2.8. 2026.
SABIO-RKP0A6C8.

Miscellaneous databases

EvolutionaryTraceiP0A6C8.
PROiP0A6C8.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
HAMAPiMF_00082_B. ArgB_B.
InterProiIPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000728. NAGK. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00761. argB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of Escherichia coli argB and argC genes: comparison of N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde dehydrogenase with homologous and analogous enzymes."
    Parsot C., Boyen A., Cohen G.N., Glansdorff N.
    Gene 68:275-283(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modelling of aspartokinase."
    Marco-Marin C., Ramon-Maiques S., Tavarez S., Rubio V.
    J. Mol. Biol. 334:459-476(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-8; ARG-66; ASN-158 AND ASP-162.
  6. "N-acetyl-L-glutamate kinase from Escherichia coli: cloning of the gene, purification and crystallization of the recombinant enzyme and preliminary X-ray analysis of the free and ligand-bound forms."
    Gil F., Ramon-Maiques S., Marina A., Fita I., Rubio V.
    Acta Crystallogr. D 55:1350-1352(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  7. "Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis."
    Ramon-Maiques S., Marina A., Gil-Ortiz F., Fita I., Rubio V.
    Structure 10:329-342(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ATP ANALOG, SUBUNIT.
  8. "The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF(4)(-) transition state mimic."
    Gil-Ortiz F., Ramon-Maiques S., Fita I., Rubio V.
    J. Mol. Biol. 331:231-244(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; ATP AND TRANSITION STATE ANALOG.

Entry informationi

Entry nameiARGB_ECOLI
AccessioniPrimary (citable) accession number: P0A6C8
Secondary accession number(s): P11445, Q2M8Q4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: June 24, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.