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P0A6C8 (ARGB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylglutamate kinase

EC=2.7.2.8
Alternative name(s):
N-acetyl-L-glutamate 5-phosphotransferase
NAG kinase
Short name=AGK
Gene names
Name:argB
Ordered Locus Names:b3959, JW5553
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. HAMAP-Rule MF_00082_B

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. HAMAP-Rule MF_00082_B

Subunit structure

Homodimer. Ref.7

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_00082_B.

Sequence similarities

Belongs to the acetylglutamate kinase family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 258258Acetylglutamate kinase HAMAP-Rule MF_00082_B
PRO_0000112614

Regions

Nucleotide binding181 – 1866ATP HAMAP-Rule MF_00082_B
Nucleotide binding209 – 2113ATP HAMAP-Rule MF_00082_B
Region44 – 452Substrate binding HAMAP-Rule MF_00082_B

Sites

Binding site661Substrate
Binding site1581Substrate
Site81Transition state stabilizer
Site2171Transition state stabilizer

Experimental info

Mutagenesis81K → R: Reduces activity 50-fold. Increases KM for N-acetyl-L-glutamate and ATP about 10-fold. Ref.5
Mutagenesis661R → K: Increases KM for N-acetyl-L-glutamate over 1000-fold. Increases KM for ATP nearly 20-fold. Ref.5
Mutagenesis1581N → Q: Increases KM for N-acetyl-L-glutamate over 1000-fold. Increases KM for ATP over 20-fold. Ref.5
Mutagenesis1621D → E: Reduces activity over 99%. No effect on KM for N-acetyl-L-glutamate and ATP. Ref.5

Secondary structure

.............................................. 258
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6C8 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 8B916B8CBC143738

FASTA25827,160
        10         20         30         40         50         60 
MMNPLIIKLG GVLLDSEEAL ERLFSALVNY RESHQRPLVI VHGGGCVVDE LMKGLNLPVK 

        70         80         90        100        110        120 
KKNGLRVTPA DQIDIITGAL AGTANKTLLA WAKKHQIAAV GLFLGDGDSV KVTQLDEELG 

       130        140        150        160        170        180 
HVGLAQPGSP KLINSLLENG YLPVVSSIGV TDEGQLMNVN ADQAATALAA TLGADLILLS 

       190        200        210        220        230        240 
DVSGILDGKG QRIAEMTAAK AEQLIEQGII TDGMIVKVNA ALDAARTLGR PVDIASWRHA 

       250 
EQLPALFNGM PMGTRILA 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRKIECAE. JT0331.
RefSeqNP_418394.3. NC_000913.3.
YP_491493.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP0A6C8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9136N.
IntActP0A6C8. 2 interactions.
MINTMINT-1309378.
STRING511145.b3959.

Proteomic databases

PaxDbP0A6C8.
PRIDEP0A6C8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76941; AAC76941; b3959.
BAE77352; BAE77352; BAE77352.
GeneID12932895.
948464.
KEGGecj:Y75_p3229.
eco:b3959.
PATRIC32123439. VBIEscCol129921_4080.

Organism-specific databases

EchoBASEEB0062.
EcoGeneEG10064. argB.

Phylogenomic databases

eggNOGCOG0548.
HOGENOMHOG000233260.
KOK00930.
OMAWRDAEQL.
OrthoDBEOG6JB13D.
PhylomeDBP0A6C8.

Enzyme and pathway databases

BioCycEcoCyc:ACETYLGLUTKIN-MONOMER.
ECOL316407:JW5553-MONOMER.
MetaCyc:ACETYLGLUTKIN-MONOMER.
SABIO-RKP0A6C8.
UniPathwayUPA00068; UER00107.

Gene expression databases

GenevestigatorP0A6C8.

Family and domain databases

Gene3D3.40.1160.10. 1 hit.
HAMAPMF_00082_B. ArgB_B.
InterProIPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF000728. NAGK. 1 hit.
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR00761. argB. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A6C8.
PROP0A6C8.

Entry information

Entry nameARGB_ECOLI
AccessionPrimary (citable) accession number: P0A6C8
Secondary accession number(s): P11445, Q2M8Q4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: June 11, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene