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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.

Pathwayi: 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)
  2. Acetylglutamate kinase (argB)
  3. N-acetyl-gamma-glutamyl-phosphate reductase (argC)
  4. 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)DescriptionActionsGraphical viewLength
Sitei8Transition state stabilizer1
Binding sitei66Substrate2 Publications1
Binding sitei158Substrate2 Publications1
Sitei217Transition state stabilizer1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi181 – 186ATP1 Publication6
Nucleotide bindingi209 – 211ATP1 Publication3

GO - Molecular functioni

  • acetylglutamate kinase activity Source: EcoCyc
  • arginine binding Source: GO_Central
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 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)DescriptionActionsGraphical viewLength
Mutagenesisi8K → R: Reduces activity 50-fold. Increases KM for N-acetyl-L-glutamate and ATP about 10-fold. 1 Publication1
Mutagenesisi66R → K: Increases KM for N-acetyl-L-glutamate over 1000-fold. Increases KM for ATP nearly 20-fold. 1 Publication1
Mutagenesisi158N → Q: Increases KM for N-acetyl-L-glutamate over 1000-fold. Increases KM for ATP over 20-fold. 1 Publication1
Mutagenesisi162D → E: Reduces activity over 99%. No effect on KM for N-acetyl-L-glutamate and ATP. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001126141 – 258Acetylglutamate kinaseAdd BLAST258

Proteomic databases

EPDiP0A6C8.
PaxDbiP0A6C8.
PRIDEiP0A6C8.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi4261889. 6 interactors.
DIPiDIP-9136N.
IntActiP0A6C8. 2 interactors.
MINTiMINT-1309378.
STRINGi511145.b3959.

Structurei

Secondary structure

1258
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Helixi11 – 15Combined sources5
Helixi17 – 31Combined sources15
Beta strandi38 – 42Combined sources5
Helixi45 – 55Combined sources11
Helixi70 – 81Combined sources12
Helixi83 – 94Combined sources12
Beta strandi99 – 102Combined sources4
Helixi106 – 108Combined sources3
Beta strandi110 – 114Combined sources5
Helixi117 – 119Combined sources3
Beta strandi120 – 127Combined sources8
Helixi131 – 138Combined sources8
Beta strandi142 – 145Combined sources4
Beta strandi147 – 150Combined sources4
Beta strandi156 – 158Combined sources3
Helixi161 – 172Combined sources12
Beta strandi175 – 184Combined sources10
Helixi198 – 206Combined sources9
Helixi213 – 228Combined sources16
Beta strandi232 – 238Combined sources7
Helixi240 – 242Combined sources3
Helixi243 – 247Combined sources5
Beta strandi252 – 256Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6C8.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni44 – 45Substrate binding2

Sequence similaritiesi

Belongs to the acetylglutamate kinase family.Curated

Phylogenomic databases

eggNOGiENOG4105CAS. Bacteria.
COG0548. LUCA.
HOGENOMiHOG000233260.
InParanoidiP0A6C8.
KOiK00930.
OMAiLVHGGGC.
PhylomeDBiP0A6C8.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
HAMAPiMF_00082_B. ArgB_B. 1 hit.
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 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:JW5553.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261889. 6 interactors.
DIPiDIP-9136N.
IntActiP0A6C8. 2 interactors.
MINTiMINT-1309378.
STRINGi511145.b3959.

Proteomic databases

EPDiP0A6C8.
PaxDbiP0A6C8.
PRIDEiP0A6C8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76941; AAC76941; b3959.
BAE77352; BAE77352; BAE77352.
GeneIDi948464.
KEGGiecj:JW5553.
eco:b3959.
PATRICi32123439. VBIEscCol129921_4080.

Organism-specific databases

EchoBASEiEB0062.
EcoGeneiEG10064. argB.

Phylogenomic databases

eggNOGiENOG4105CAS. Bacteria.
COG0548. LUCA.
HOGENOMiHOG000233260.
InParanoidiP0A6C8.
KOiK00930.
OMAiLVHGGGC.
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. 1 hit.
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...

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: November 2, 2016
This is version 105 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

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 one 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.