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P38372

- KAD_BACHD

UniProt

P38372 - KAD_BACHD

Protein

Adenylate kinase

Gene

adk

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      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 sitei31 – 311AMPUniRule annotation
    Binding sitei36 – 361AMPUniRule annotation
    Binding sitei92 – 921AMPUniRule annotation
    Binding sitei127 – 1271ATPUniRule annotation
    Binding sitei160 – 1601AMPUniRule annotation
    Binding sitei171 – 1711AMPUniRule annotation
    Binding sitei199 – 1991ATP; via carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 156ATPUniRule annotation
    Nucleotide bindingi57 – 593AMPUniRule annotation
    Nucleotide bindingi85 – 884AMPUniRule annotation
    Nucleotide bindingi136 – 1372ATPUniRule annotation

    GO - Molecular functioni

    1. adenylate kinase activity Source: UniProtKB-HAMAP
    2. ATP 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, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBHAL272558:GJC5-180-MONOMER.
    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:BH0155
    OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
    Taxonomic identifieri272558 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001258: 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 – 217217Adenylate kinasePRO_0000158725Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272558.BH0155.

    Structurei

    3D structure databases

    ProteinModelPortaliP38372.
    SMRiP38372. Positions 1-216.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 5930NMPbindUniRule annotationAdd
    BLAST
    Regioni126 – 16338LIDUniRule 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.UniRule annotation

    Sequence similaritiesi

    Belongs to the adenylate kinase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0563.
    KOiK00939.
    OMAiVLNIEVP.
    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.

    P38372-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNLILMGLPG AGKGTQAEKI IEKYGIPHIS TGDMFRAAMK NETELGLKAK    50
    SYMDAGELVP DEVTIGIVRD RLSQDDCQNG FLLDGFPRTV AQAEALEDIL 100
    ASLDKKLDYV INIDVPEQLL MDRLTGRRVS PTSGRTYHVI FNPPKVEGIC 150
    DVDGSELIQR DDDKPETVKK RLEVNQKQAQ PLIDFYSEKG YLQNINGDQD 200
    ISRVFEDINE LLKGLSS 217
    Length:217
    Mass (Da):24,170
    Last modified:December 1, 2000 - v2
    Checksum:iFD5DF854B3BA3592
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41I → N in BAA01192. (PubMed:1512566)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017508 Genomic DNA. Translation: BAA75292.1.
    BA000004 Genomic DNA. Translation: BAB03874.1.
    D10360 Genomic DNA. Translation: BAA01192.1.
    PIRiC44859.
    T44404.
    RefSeqiNP_241021.1. NC_002570.2.
    WP_010896338.1. NC_002570.2.

    Genome annotation databases

    EnsemblBacteriaiBAB03874; BAB03874; BAB03874.
    GeneIDi892776.
    KEGGibha:BH0155.
    PATRICi18937184. VBIBacHal18977_0164.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017508 Genomic DNA. Translation: BAA75292.1 .
    BA000004 Genomic DNA. Translation: BAB03874.1 .
    D10360 Genomic DNA. Translation: BAA01192.1 .
    PIRi C44859.
    T44404.
    RefSeqi NP_241021.1. NC_002570.2.
    WP_010896338.1. NC_002570.2.

    3D structure databases

    ProteinModelPortali P38372.
    SMRi P38372. Positions 1-216.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272558.BH0155.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB03874 ; BAB03874 ; BAB03874 .
    GeneIDi 892776.
    KEGGi bha:BH0155.
    PATRICi 18937184. VBIBacHal18977_0164.

    Phylogenomic databases

    eggNOGi COG0563.
    KOi K00939.
    OMAi VLNIEVP.
    OrthoDBi EOG679TH4.

    Enzyme and pathway databases

    UniPathwayi UPA00588 ; UER00649 .
    BioCyci BHAL272558:GJC5-180-MONOMER.

    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. "Sequence analysis of a 32-kb region including the major ribosomal protein gene clusters from alkaliphilic Bacillus sp. strain C-125."
      Takami H., Takaki Y., Nakasone K., Hirama C., Inoue A., Horikoshi K.
      Biosci. Biotechnol. Biochem. 63:452-455(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
    2. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
      Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
      Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
    3. "Molecular cloning and characterization of an alkalophilic Bacillus sp. C125 gene homologous to Bacillus subtilis secY."
      Kang S.K., Kudo T., Horikoshi K.
      J. Gen. Microbiol. 138:1365-1370(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107.
      Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

    Entry informationi

    Entry nameiKAD_BACHD
    AccessioniPrimary (citable) accession number: P38372
    Secondary accession number(s): Q9JPW7, Q9WWJ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3