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Q92GY7

- KAD_RICCN

UniProt

Q92GY7 - KAD_RICCN

Protein

Adenylate kinase

Gene

adk

Organism
Rickettsia conorii (strain ATCC VR-613 / Malish 7)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.UniRule annotation

    Catalytic activityi

    ATP + AMP = 2 ADP.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361AMPUniRule annotation
    Binding sitei92 – 921AMPUniRule annotation
    Binding sitei123 – 1231ATPUniRule annotation
    Metal bindingi126 – 1261Zinc; structuralUniRule annotation
    Metal bindingi129 – 1291Zinc; structuralUniRule annotation
    Metal bindingi146 – 1461Zinc; structuralUniRule annotation
    Metal bindingi149 – 1491Zinc; structuralUniRule annotation
    Binding sitei157 – 1571AMPUniRule annotation
    Binding sitei168 – 1681AMPUniRule annotation
    Binding sitei196 – 1961ATP; via carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 156ATPUniRule annotation
    Nucleotide bindingi57 – 593AMPUniRule annotation
    Nucleotide bindingi85 – 884AMPUniRule annotation
    Nucleotide bindingi132 – 1332ATPUniRule annotation

    GO - Molecular functioni

    1. adenylate kinase activity Source: UniProtKB-HAMAP
    2. ATP binding Source: UniProtKB-HAMAP
    3. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. AMP salvage Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Nucleotide biosynthesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00588; UER00649.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylate kinaseUniRule annotation (EC:2.7.4.3UniRule annotation)
    Short name:
    AKUniRule annotation
    Alternative name(s):
    ATP-AMP transphosphorylaseUniRule annotation
    ATP:AMP phosphotransferaseUniRule annotation
    Adenylate monophosphate kinaseUniRule annotation
    Gene namesi
    Name:adkUniRule annotation
    Ordered Locus Names:RC0985
    OrganismiRickettsia conorii (strain ATCC VR-613 / Malish 7)
    Taxonomic identifieri272944 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group
    ProteomesiUP000000816: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 212212Adenylate kinasePRO_0000158838Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272944.RC0985.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92GY7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 5930NMPbindUniRule annotationAdd
    BLAST
    Regioni122 – 16039LIDUniRule annotationAdd
    BLAST

    Domaini

    Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.UniRule annotation

    Sequence similaritiesi

    Belongs to the adenylate kinase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0563.
    HOGENOMiHOG000238772.
    KOiK00939.
    OMAiQAKFIME.
    OrthoDBiEOG679TH4.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00235. Adenylate_kinase_Adk.
    InterProiIPR006259. Adenyl_kin_sub.
    IPR000850. Adenylat/UMP-CMP_kin.
    IPR007862. Adenylate_kinase_lid-dom.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR23359. PTHR23359. 1 hit.
    PfamiPF05191. ADK_lid. 1 hit.
    [Graphical view]
    PRINTSiPR00094. ADENYLTKNASE.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01351. adk. 1 hit.
    PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q92GY7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMVIFLGPPG AGKGTQGKKI AKKIDLPHIA IGDIFRTIIK TSTSEAELIN    50
    NYVKQGELIP NEIVNQVIKN FLLSSEYKNG YILDGYPRNL EQAKFFESFI 100
    KEKIKIIYFD VSDELLIKRI LGRYSCKNCG KIYNRYFVQP KTDNVCDVCG 150
    SSTFDYRKDD NEEVIKKRIE VYKTETYPLI DYYKNSGNFY IVNGSKNEQE 200
    IEIDIQKILK IN 212
    Length:212
    Mass (Da):24,497
    Last modified:December 1, 2001 - v1
    Checksum:iBF785765826527A4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006914 Genomic DNA. Translation: AAL03523.1.
    PIRiA97823.
    RefSeqiNP_360622.1. NC_003103.1.
    WP_010977577.1. NC_003103.1.

    Genome annotation databases

    EnsemblBacteriaiAAL03523; AAL03523; RC0985.
    GeneIDi928128.
    KEGGirco:RC0985.
    PATRICi17889376. VBIRicCon45613_1125.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006914 Genomic DNA. Translation: AAL03523.1 .
    PIRi A97823.
    RefSeqi NP_360622.1. NC_003103.1.
    WP_010977577.1. NC_003103.1.

    3D structure databases

    ProteinModelPortali Q92GY7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272944.RC0985.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL03523 ; AAL03523 ; RC0985 .
    GeneIDi 928128.
    KEGGi rco:RC0985.
    PATRICi 17889376. VBIRicCon45613_1125.

    Phylogenomic databases

    eggNOGi COG0563.
    HOGENOMi HOG000238772.
    KOi K00939.
    OMAi QAKFIME.
    OrthoDBi EOG679TH4.

    Enzyme and pathway databases

    UniPathwayi UPA00588 ; UER00649 .

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_00235. Adenylate_kinase_Adk.
    InterProi IPR006259. Adenyl_kin_sub.
    IPR000850. Adenylat/UMP-CMP_kin.
    IPR007862. Adenylate_kinase_lid-dom.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR23359. PTHR23359. 1 hit.
    Pfami PF05191. ADK_lid. 1 hit.
    [Graphical view ]
    PRINTSi PR00094. ADENYLTKNASE.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR01351. adk. 1 hit.
    PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC VR-613 / Malish 7.

    Entry informationi

    Entry nameiKAD_RICCN
    AccessioniPrimary (citable) accession number: Q92GY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 84 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

    Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Rickettsia conorii
      (strain Malish 7): entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3