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P27142

- KAD_GEOSE

UniProt

P27142 - KAD_GEOSE

Protein

Adenylate kinase

Gene

adk

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    • Comment

    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

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius. Thermal denaturation midpoint (Tm) is 74.5 degrees Celsius.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei31 – 311AMP
    Binding sitei36 – 361AMP
    Binding sitei92 – 921AMP
    Binding sitei127 – 1271ATP
    Metal bindingi130 – 1301Zinc; structural
    Metal bindingi133 – 1331Zinc; structural
    Metal bindingi150 – 1501Zinc; structural
    Metal bindingi153 – 1531Zinc; structural
    Binding sitei160 – 1601AMP
    Binding sitei171 – 1711AMP
    Binding sitei199 – 1991ATP; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 156ATP
    Nucleotide bindingi57 – 593AMP
    Nucleotide bindingi85 – 884AMP
    Nucleotide bindingi136 – 1372ATP

    GO - Molecular functioni

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

    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

    SABIO-RKP27142.
    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
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 217217Adenylate kinasePRO_0000158729Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    217
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Helixi13 – 2412
    Beta strandi28 – 303
    Helixi31 – 4111
    Helixi44 – 5512
    Helixi61 – 7212
    Helixi75 – 773
    Beta strandi81 – 855
    Helixi90 – 10213
    Beta strandi109 – 1146
    Helixi117 – 1259
    Beta strandi127 – 1304
    Turni131 – 1333
    Beta strandi136 – 1383
    Turni139 – 1413
    Turni151 – 1533
    Beta strandi156 – 1583
    Helixi161 – 1633
    Helixi165 – 17915
    Helixi181 – 1888
    Beta strandi192 – 1965
    Helixi201 – 21616

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZINX-ray1.60A1-217[»]
    1ZIOX-ray1.96A1-217[»]
    1ZIPX-ray1.85A1-217[»]
    ProteinModelPortaliP27142.
    SMRiP27142. Positions 1-217.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27142.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 5930NMPbindAdd
    BLAST
    Regioni126 – 16338LIDAdd
    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.

    Sequence similaritiesi

    Belongs to the adenylate kinase family.UniRule annotation

    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.

    P27142-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNLVLMGLPG AGKGTQAEKI VAAYGIPHIS TGDMFRAAMK EGTPLGLQAK    50
    QYMDRGDLVP DEVTIGIVRE RLSKDDCQNG FLLDGFPRTV AQAEALETML 100
    ADIGRKLDYV IHIDVRQDVL MERLTGRRIC RNCGATYHLI FHPPAKPGVC 150
    DKCGGELYQR ADDNEATVAN RLEVNMKQMK PLVDFYEQKG YLRNINGEQD 200
    MEKVFADIRE LLGGLAR 217
    Length:217
    Mass (Da):24,143
    Last modified:August 1, 1992 - v1
    Checksum:iD8701931117C53CF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88104 Genomic DNA. Translation: AAA22205.1.
    PIRiB42196. KIBSAF.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88104 Genomic DNA. Translation: AAA22205.1 .
    PIRi B42196. KIBSAF.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZIN X-ray 1.60 A 1-217 [» ]
    1ZIO X-ray 1.96 A 1-217 [» ]
    1ZIP X-ray 1.85 A 1-217 [» ]
    ProteinModelPortali P27142.
    SMRi P27142. Positions 1-217.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00588 ; UER00649 .
    SABIO-RK P27142.

    Miscellaneous databases

    EvolutionaryTracei P27142.

    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. "Zinc, a novel structural element found in the family of bacterial adenylate kinases."
      Glaser P., Presecan E., Delepierre M., Surewicz W.K., Mantsch H.H., Barzu O., Gilles A.M.
      Biochemistry 31:3038-3043(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ZINC ION.
    2. Schiltz E., Buerkle S., Stiehle H., Mader B., Schulz G.E.
      Submitted (APR-1992) to the PIR data bank
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Crystal structures of Bacillus stearothermophilus adenylate kinase with bound Ap5A, Mg2+ Ap5A, and Mn2+ Ap5A reveal an intermediate lid position and six coordinate octahedral geometry for bound Mg2+ and Mn2+."
      Berry M.B., Phillips G.N. Jr.
      Proteins 32:276-288(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF COMPLEX WITH BI-SUBSTRATE ANALOG AP5A AND ZINC.

    Entry informationi

    Entry nameiKAD_GEOSE
    AccessioniPrimary (citable) accession number: P27142
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 97 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3