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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

Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.UniRule annotation2 Publications

Catalytic activityi

ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate.UniRule annotation2 Publications

Kineticsi

  1. KM=0.20 mM for N-acetyl-L-glutamate1 Publication
  2. KM=0.29 mM for ATP1 Publication

    Pathwayi: L-arginine biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.UniRule annotationCurated
    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 stabilizerUniRule annotation1 Publication1
    Binding sitei66SubstrateUniRule annotation2 Publications1
    Binding sitei158SubstrateUniRule annotation2 Publications1
    Sitei217Transition state stabilizerUniRule annotation1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi181 – 186ATPUniRule annotation1 Publication6
    Nucleotide bindingi209 – 211ATPUniRule annotation1 Publication3

    GO - Molecular functioni

    • acetylglutamate kinase activity Source: EcoCyc
    • arginine binding Source: GO_Central
    • ATP binding Source: UniProtKB-KW

    GO - Biological processi

    • arginine biosynthetic process Source: EcoCyc
    • cellular response to DNA damage stimulus Source: EcoliWiki

    Keywordsi

    Molecular functionKinase, Transferase
    Biological processAmino-acid biosynthesis, Arginine biosynthesis
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:ACETYLGLUTKIN-MONOMER.
    MetaCyc:ACETYLGLUTKIN-MONOMER.
    BRENDAi2.7.2.8. 2026.
    SABIO-RKiP0A6C8.
    UniPathwayiUPA00068; UER00107.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetylglutamate kinaseUniRule annotationCurated (EC:2.7.2.8UniRule annotation2 Publications)
    Alternative name(s):
    N-acetyl-L-glutamate 5-phosphotransferaseUniRule annotationCurated
    NAG kinaseUniRule annotationCurated
    Short name:
    NAGK1 PublicationUniRule annotation
    Gene namesi
    Name:argB1 PublicationUniRule annotation
    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

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    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

    Chemistry databases

    DrugBankiDB04075. N-Acetyl-L-Glutamate.
    DB04395. Phosphoaminophosphonic Acid-Adenylate Ester.
    DB04444. Tetrafluoroaluminate Ion.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001126142 – 258Acetylglutamate kinaseAdd BLAST257

    Proteomic databases

    EPDiP0A6C8.
    PaxDbiP0A6C8.
    PRIDEiP0A6C8.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation3 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 bindingUniRule annotation2 Publications2

    Sequence similaritiesi

    Belongs to the acetylglutamate kinase family. ArgB subfamily.UniRule annotationCurated

    Phylogenomic databases

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

    Family and domain databases

    HAMAPiMF_00082. ArgB. 1 hit.
    InterProiView protein in InterPro
    IPR004662. AcgluKinase.
    IPR001048. Asp/Glu/Uridylate_kinase.
    PfamiView protein in Pfam
    PF00696. AA_kinase. 1 hit.
    PIRSFiPIRSF000728. NAGK. 1 hit.
    SUPFAMiSSF53633. SSF53633. 1 hit.
    TIGRFAMsiTIGR00761. argB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    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. Translation N-terminally extended.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.
    WP_001302318.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76941; AAC76941; b3959.
    BAE77352; BAE77352; BAE77352.
    GeneIDi948464.
    KEGGiecj:JW5553.
    eco:b3959.
    PATRICifig|1411691.4.peg.2746.

    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.
    WP_001302318.1. NZ_LN832404.1.

    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.

    Chemistry databases

    DrugBankiDB04075. N-Acetyl-L-Glutamate.
    DB04395. Phosphoaminophosphonic Acid-Adenylate Ester.
    DB04444. Tetrafluoroaluminate Ion.

    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.
    PATRICifig|1411691.4.peg.2746.

    Organism-specific databases

    EchoBASEiEB0062.
    EcoGeneiEG10064. argB.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayiUPA00068; UER00107.
    BioCyciEcoCyc:ACETYLGLUTKIN-MONOMER.
    MetaCyc:ACETYLGLUTKIN-MONOMER.
    BRENDAi2.7.2.8. 2026.
    SABIO-RKiP0A6C8.

    Miscellaneous databases

    EvolutionaryTraceiP0A6C8.
    PROiPR:P0A6C8.

    Family and domain databases

    HAMAPiMF_00082. ArgB. 1 hit.
    InterProiView protein in InterPro
    IPR004662. AcgluKinase.
    IPR001048. Asp/Glu/Uridylate_kinase.
    PfamiView protein in Pfam
    PF00696. AA_kinase. 1 hit.
    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 historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: June 7, 2017
    This is version 109 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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.