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P0A6C8

- ARGB_ECOLI

UniProt

P0A6C8 - ARGB_ECOLI

Protein

Acetylglutamate kinase

Gene

argB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    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

    1. acetylglutamate kinase activity Source: EcoCyc
    2. ATP binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. arginine biosynthetic process Source: EcoCyc
    2. cellular response to DNA damage stimulus Source: EcoliWiki

    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.
    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10064. argB.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A6C8.

    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 – 95
    Helixi11 – 155
    Helixi17 – 3115
    Beta strandi38 – 425
    Helixi45 – 5410
    Turni70 – 723
    Helixi73 – 819
    Helixi83 – 9412
    Beta strandi99 – 1024
    Helixi106 – 1083
    Beta strandi110 – 1145
    Turni117 – 1193
    Beta strandi120 – 1278
    Helixi131 – 1388
    Beta strandi142 – 1509
    Beta strandi156 – 1583
    Helixi161 – 17212
    Beta strandi175 – 18410
    Helixi198 – 2069
    Helixi212 – 22817
    Beta strandi232 – 2387
    Helixi240 – 2423
    Helixi243 – 2486
    Beta strandi253 – 2564

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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.
    KOiK00930.
    OMAiWRDAEQL.
    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

    MMNPLIIKLG GVLLDSEEAL ERLFSALVNY RESHQRPLVI VHGGGCVVDE    50
    LMKGLNLPVK KKNGLRVTPA DQIDIITGAL AGTANKTLLA WAKKHQIAAV 100
    GLFLGDGDSV KVTQLDEELG HVGLAQPGSP KLINSLLENG YLPVVSSIGV 150
    TDEGQLMNVN ADQAATALAA TLGADLILLS DVSGILDGKG QRIAEMTAAK 200
    AEQLIEQGII TDGMIVKVNA ALDAARTLGR PVDIASWRHA EQLPALFNGM 250
    PMGTRILA 258
    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.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_491493.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76941; AAC76941; b3959.
    BAE77352; BAE77352; BAE77352.
    GeneIDi12932895.
    948464.
    KEGGiecj:Y75_p3229.
    eco:b3959.
    PATRICi32123439. VBIEscCol129921_4080.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    PIRi JT0331. KIECAE.
    RefSeqi NP_418394.3. NC_000913.3.
    YP_491493.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GS5 X-ray 1.50 A 1-258 [» ]
    1GSJ X-ray 1.85 A 1-258 [» ]
    1OH9 X-ray 1.91 A 1-258 [» ]
    1OHA X-ray 1.90 A 1-258 [» ]
    1OHB X-ray 1.90 A 1-258 [» ]
    2WXB X-ray 2.00 A/B 1-258 [» ]
    2X2W X-ray 2.00 A/B 1-258 [» ]
    ProteinModelPortali P0A6C8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9136N.
    IntActi P0A6C8. 2 interactions.
    MINTi MINT-1309378.
    STRINGi 511145.b3959.

    Proteomic databases

    PaxDbi P0A6C8.
    PRIDEi P0A6C8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76941 ; AAC76941 ; b3959 .
    BAE77352 ; BAE77352 ; BAE77352 .
    GeneIDi 12932895.
    948464.
    KEGGi ecj:Y75_p3229.
    eco:b3959.
    PATRICi 32123439. VBIEscCol129921_4080.

    Organism-specific databases

    EchoBASEi EB0062.
    EcoGenei EG10064. argB.

    Phylogenomic databases

    eggNOGi COG0548.
    HOGENOMi HOG000233260.
    KOi K00930.
    OMAi WRDAEQL.
    OrthoDBi EOG6JB13D.
    PhylomeDBi P0A6C8.

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00107 .
    BioCyci EcoCyc:ACETYLGLUTKIN-MONOMER.
    ECOL316407:JW5553-MONOMER.
    MetaCyc:ACETYLGLUTKIN-MONOMER.
    SABIO-RK P0A6C8.

    Miscellaneous databases

    EvolutionaryTracei P0A6C8.
    PROi P0A6C8.

    Gene expression databases

    Genevestigatori P0A6C8.

    Family and domain databases

    Gene3Di 3.40.1160.10. 1 hit.
    HAMAPi MF_00082_B. ArgB_B.
    InterProi IPR004662. AcgluKinase.
    IPR001048. Asp/Glu/Uridylate_kinase.
    [Graphical view ]
    Pfami PF00696. AA_kinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000728. NAGK. 1 hit.
    SUPFAMi SSF53633. SSF53633. 1 hit.
    TIGRFAMsi TIGR00761. argB. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 91 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