Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

C6C5B9

- C6C5B9_DICDC

UniProt

C6C5B9 - C6C5B9_DICDC

Protein

Glycerol kinase

Gene

glpK

Organism
Dickeya dadantii (strain Ech703)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (01 Sep 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.UniRule annotation

    Catalytic activityi

    ATP + glycerol = ADP + sn-glycerol 3-phosphate.UniRule annotationSAAS annotation

    Enzyme regulationi

    Activity of this regulatory enzyme is affected by several metabolites. Allosterically and non-competitively inhibited by fructose 1,6-bisphosphate (FBP) and unphosphorylated phosphocarrier protein EIIA-Glc (III-Glc), an integral component of the bacterial phosphotransferase (PTS) system.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei15 – 151SubstrateUniRule annotation
    Binding sitei19 – 191ATPUniRule annotation
    Binding sitei137 – 1371SubstrateUniRule annotation
    Binding sitei269 – 2691ATPUniRule annotation
    Binding sitei312 – 3121ATP; via carbonyl oxygenUniRule annotation
    Binding sitei316 – 3161ATP; via amide nitrogenUniRule annotation
    Binding sitei331 – 3311ATPUniRule annotation
    Metal bindingi480 – 4801Zinc; shared with EIIA-GlcUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 173ATPUniRule annotation
    Nucleotide bindingi413 – 4175ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. glycerol kinase activity Source: UniProtKB-HAMAP
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. glycerol-3-phosphate metabolic process Source: UniProtKB-HAMAP
    2. glycerol catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    KinaseUniRule annotationSAAS annotationImported, Transferase

    Keywords - Biological processi

    Glycerol metabolismUniRule annotationSAAS annotation

    Keywords - Ligandi

    ATP-bindingUniRule annotationSAAS annotation, Metal-bindingUniRule annotation, Nucleotide-binding, ZincUniRule annotation

    Enzyme and pathway databases

    BioCyciDDAD579405:GHJU-3897-MONOMER.
    UniPathwayiUPA00618; UER00672.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycerol kinaseUniRule annotation (EC:2.7.1.30UniRule annotation)
    Alternative name(s):
    ATP:glycerol 3-phosphotransferaseUniRule annotation
    GlycerokinaseUniRule annotation
    Gene namesi
    Name:glpKUniRule annotation
    Ordered Locus Names:Dd703_3803Imported
    OrganismiDickeya dadantii (strain Ech703)Imported
    Taxonomic identifieri579405 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya
    ProteomesiUP000002734: Chromosome

    Interactioni

    Subunit structurei

    Homotetramer and homodimer (in equilibrium). Heterodimer with EIIA-Glc. Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.UniRule annotation

    Protein-protein interaction databases

    STRINGi579405.Dd703_3803.

    Structurei

    3D structure databases

    ProteinModelPortaliC6C5B9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni85 – 862Substrate bindingUniRule annotation
    Regioni235 – 2373Allosteric FBP inhibitor bindingUniRule annotation
    Regioni247 – 2482Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the FGGY kinase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0554.
    HOGENOMiHOG000222134.
    KOiK00864.
    OMAiHFFGVEV.
    OrthoDBiEOG6RZB46.

    Family and domain databases

    HAMAPiMF_00186. Glycerol_kin.
    InterProiIPR018485. Carb_kinase_FGGY_C.
    IPR018483. Carb_kinase_FGGY_CS.
    IPR018484. Carb_kinase_FGGY_N.
    IPR005999. Glycerol_kin.
    [Graphical view]
    PfamiPF02782. FGGY_C. 1 hit.
    PF00370. FGGY_N. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01311. glycerol_kin. 1 hit.
    PROSITEiPS00933. FGGY_KINASES_1. 1 hit.
    PS00445. FGGY_KINASES_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    C6C5B9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQEKKYIVA LDQGTTSSRA VVLDHDANIV SVSQREFPQI YPKPGWVEHD    50
    PMEIWASQSS TLVEALAKAG ISSDEVAGIG ITNQRETVVV WEKETGKPIY 100
    NAIVWQCRRT ADICEKLKKD GLEEYIRANT GLVVDPYFSG TKVKWILDHV 150
    DGARDRANRG ELLLGTIDTW LIWKMTQGRV HVTDYTNASR TMLFNIHKLD 200
    WDERMLEALD IPRSMLPQVR PSSEMYGQTN IGGKGGTRIP ICGIAGDQQA 250
    ALYGQLCVQP GMAKNTYGTG CFLLMNTGTE AVASRHGLLT TIACGPRGEV 300
    NYALEGAVFI GGASIQWLRD ELKLINDAAD SEYFATKVKD TNGVYVVPAF 350
    TGLGAPYWDP YARGAIFGLT RGANANHIIR ATLESIAFQT RDVLDAMQAD 400
    ADTRLQSLRV DGGAVANNFL MQFQSDILGT RVERPQVRES TALGAAFLAG 450
    LATGFWNDLD EVKSKTAIER EFRPSIETVE RNFRYRGWQK AVERARNWED 500
    HDA 503
    Length:503
    Mass (Da):55,776
    Last modified:September 1, 2009 - v1
    Checksum:i5825E56251D1F4B5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001654 Genomic DNA. Translation: ACS87556.1.
    RefSeqiYP_002989378.1. NC_012880.1.

    Genome annotation databases

    EnsemblBacteriaiACS87556; ACS87556; Dd703_3803.
    GeneIDi8087188.
    KEGGidda:Dd703_3803.
    PATRICi21795313. VBIDicDad95084_4030.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001654 Genomic DNA. Translation: ACS87556.1 .
    RefSeqi YP_002989378.1. NC_012880.1.

    3D structure databases

    ProteinModelPortali C6C5B9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 579405.Dd703_3803.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACS87556 ; ACS87556 ; Dd703_3803 .
    GeneIDi 8087188.
    KEGGi dda:Dd703_3803.
    PATRICi 21795313. VBIDicDad95084_4030.

    Phylogenomic databases

    eggNOGi COG0554.
    HOGENOMi HOG000222134.
    KOi K00864.
    OMAi HFFGVEV.
    OrthoDBi EOG6RZB46.

    Enzyme and pathway databases

    UniPathwayi UPA00618 ; UER00672 .
    BioCyci DDAD579405:GHJU-3897-MONOMER.

    Family and domain databases

    HAMAPi MF_00186. Glycerol_kin.
    InterProi IPR018485. Carb_kinase_FGGY_C.
    IPR018483. Carb_kinase_FGGY_CS.
    IPR018484. Carb_kinase_FGGY_N.
    IPR005999. Glycerol_kin.
    [Graphical view ]
    Pfami PF02782. FGGY_C. 1 hit.
    PF00370. FGGY_N. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01311. glycerol_kin. 1 hit.
    PROSITEi PS00933. FGGY_KINASES_1. 1 hit.
    PS00445. FGGY_KINASES_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ech703Imported.

    Entry informationi

    Entry nameiC6C5B9_DICDC
    AccessioniPrimary (citable) accession number: C6C5B9
    Entry historyi
    Integrated into UniProtKB/TrEMBL: September 1, 2009
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 38 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzymeUniRule annotation, Complete proteomeImported

    External Data

    Dasty 3