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Protein

Methionine aminopeptidase

Gene

map

Organism
Thermococcus onnurineus (strain NA1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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).UniRule annotation1 Publication

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation1 Publication

Cofactori

Fe2+By similarity1 Publication, Co2+By similarity1 Publication, Ni2+By similarity1 Publication, Mn2+By similarity1 PublicationNote: 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. The enzyme is active with cobalt, nickel, manganese and 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

    GO - Biological processi

    Complete GO annotation...

    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 Componenti: 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.
    OMAiIRASCIY.

    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

            10         20         30         40         50
    MDEREALIKA GEIARQVKKE VISLIKPGTK LYDIAEFVER RIIELGGKPA
    60 70 80 90 100
    FPCNLSINEI AAHYTPYKGD ETVLKEGDYL KVDIGVHVDG YIADTALTFR
    110 120 130 140 150
    VGMEEDDLVT AAREALENAI KVIRAGIKIN EIGKAIEETI RGYGFNPIVN
    160 170 180 190 200
    LSGHKIERYK LHAGISIPNI YRPADSYVLK EGDVIAIEPF ATTGAGQVIE
    210 220 230 240 250
    VPPALIFMYL RDRPVRMAQA RRVLMHIKRE YNGLPFAYRW LQGFMPEGQL
    260 270 280 290
    KLALAQLDRV GAIYSYPILR EVRGGLVAQF EHTVIVEKEG AYITT
    Length:295
    Mass (Da):33,013
    Last modified:January 20, 2009 - v1
    Checksum:i743CE50ECD2622D2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

    STRINGi523850.TON_0362.

    Protein family/group databases

    MEROPSiM24.035.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226277.
    KOiK01265.
    OMAiIRASCIY.

    Enzyme and pathway databases

    BioCyciTONN523850:GC7X-382-MONOMER.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: July 22, 2015
    This is version 47 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.