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B6YTG0

- MAP2_THEON

UniProt

B6YTG0 - MAP2_THEON

Protein

Methionine aminopeptidase

Gene

map

Organism
Thermococcus onnurineus (strain NA1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (20 Jan 2009)
      Previous versions | rss
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    Functioni

    Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).1 PublicationUniRule annotation

    Catalytic activityi

    Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.1 PublicationUniRule annotation

    Cofactori

    Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site By similarity. The enzyme is active with cobalt, nickel, manganese or divalent iron ions.By similarity1 Publication

    Kineticsi

    kcat is 168 min(-1) with L-Met-p-nitroanilide as substrate.

    1. KM=0.68 mM for L-Met-p-nitroanilide1 Publication

    pH dependencei

    Optimum pH is 7.1 Publication

    Temperature dependencei

    Optimum temperature is 80-90 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei63 – 631SubstrateUniRule annotation
    Metal bindingi83 – 831Divalent metal cation 1UniRule annotation
    Metal bindingi94 – 941Divalent metal cation 1UniRule annotation
    Metal bindingi94 – 941Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi154 – 1541Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei162 – 1621SubstrateUniRule annotation
    Metal bindingi188 – 1881Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi281 – 2811Divalent metal cation 1UniRule annotation
    Metal bindingi281 – 2811Divalent metal cation 2; catalyticUniRule annotation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-HAMAP
    2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. protein initiator methionine removal Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BioCyciTONN523850:GC7X-382-MONOMER.

    Protein family/group databases

    MEROPSiM24.035.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidaseUniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAPUniRule annotation
    Short name:
    MetAPUniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Name:mapUniRule annotation
    Ordered Locus Names:TON_0362
    OrganismiThermococcus onnurineus (strain NA1)
    Taxonomic identifieri523850 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
    ProteomesiUP000002727: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 295295Methionine aminopeptidasePRO_0000428826Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi523850.TON_0362.

    Structurei

    3D structure databases

    ProteinModelPortaliB6YTG0.
    SMRiB6YTG0. Positions 3-295.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226277.
    KOiK01265.
    OMAiERYKLHA.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPiMF_01975. MetAP_2_arc.
    InterProiIPR028595. MetAP_archaeal.
    IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 2 hits.
    TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
    PROSITEiPS01202. MAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B6YTG0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDEREALIKA GEIARQVKKE VISLIKPGTK LYDIAEFVER RIIELGGKPA    50
    FPCNLSINEI AAHYTPYKGD ETVLKEGDYL KVDIGVHVDG YIADTALTFR 100
    VGMEEDDLVT AAREALENAI KVIRAGIKIN EIGKAIEETI RGYGFNPIVN 150
    LSGHKIERYK LHAGISIPNI YRPADSYVLK EGDVIAIEPF ATTGAGQVIE 200
    VPPALIFMYL RDRPVRMAQA RRVLMHIKRE YNGLPFAYRW LQGFMPEGQL 250
    KLALAQLDRV GAIYSYPILR EVRGGLVAQF EHTVIVEKEG AYITT 295
    Length:295
    Mass (Da):33,013
    Last modified:January 20, 2009 - v1
    Checksum:i743CE50ECD2622D2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ144133 Genomic DNA. Translation: ABA26945.1.
    CP000855 Genomic DNA. Translation: ACJ15847.1.
    RefSeqiWP_012571319.1. NC_011529.1.
    YP_002306744.1. NC_011529.1.

    Genome annotation databases

    EnsemblBacteriaiACJ15847; ACJ15847; TON_0362.
    GeneIDi7018028.
    KEGGiton:TON_0362.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ144133 Genomic DNA. Translation: ABA26945.1 .
    CP000855 Genomic DNA. Translation: ACJ15847.1 .
    RefSeqi WP_012571319.1. NC_011529.1.
    YP_002306744.1. NC_011529.1.

    3D structure databases

    ProteinModelPortali B6YTG0.
    SMRi B6YTG0. Positions 3-295.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 523850.TON_0362.

    Protein family/group databases

    MEROPSi M24.035.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACJ15847 ; ACJ15847 ; TON_0362 .
    GeneIDi 7018028.
    KEGGi ton:TON_0362.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226277.
    KOi K01265.
    OMAi ERYKLHA.

    Enzyme and pathway databases

    BioCyci TONN523850:GC7X-382-MONOMER.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPi MF_01975. MetAP_2_arc.
    InterProi IPR028595. MetAP_archaeal.
    IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10804:SF9. PTHR10804:SF9. 1 hit.
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 2 hits.
    TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
    PROSITEi PS01202. MAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, and characterization of a methionyl aminopeptidase from a hyperthermophilic archaeon Thermococcus sp. NA1."
      Lee H.S., Kim Y.J., Bae S.S., Jeon J.H., Lim J.K., Jeong B.C., Kang S.G., Lee J.H.
      Mar. Biotechnol. 8:425-432(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
      Strain: NA1.
    2. "The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism."
      Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H., Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J., Colwell R.R., Kim S.-J., Lee J.-H.
      J. Bacteriol. 190:7491-7499(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NA1.

    Entry informationi

    Entry nameiMAP2_THEON
    AccessioniPrimary (citable) accession number: B6YTG0
    Secondary accession number(s): Q2QC91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2014
    Last sequence update: January 20, 2009
    Last modified: October 1, 2014
    This is version 43 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, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3