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O66489

- MAP1_AQUAE

UniProt

O66489 - MAP1_AQUAE

Protein

Methionine aminopeptidase

Gene

map

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.UniRule annotation

    Catalytic activityi

    Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule 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. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. 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.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei84 – 841SubstrateUniRule annotation
    Metal bindingi102 – 1021Divalent metal cation 1UniRule annotation
    Metal bindingi113 – 1131Divalent metal cation 1UniRule annotation
    Metal bindingi113 – 1131Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi176 – 1761Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei183 – 1831SubstrateUniRule annotation
    Metal bindingi211 – 2111Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi242 – 2421Divalent metal cation 1UniRule annotation
    Metal bindingi242 – 2421Divalent 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

    BioCyciAAEO224324:GJBH-64-MONOMER.

    Protein family/group databases

    MEROPSiM24.001.

    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:aq_076
    OrganismiAquifex aeolicus (strain VF5)
    Taxonomic identifieri224324 [NCBI]
    Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
    ProteomesiUP000000798: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 258258Methionine aminopeptidasePRO_0000148924Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi224324.aq_076.

    Structurei

    3D structure databases

    ProteinModelPortaliO66489.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030426.
    KOiK01265.
    OMAiMPGDRPL.
    OrthoDBiEOG6MWNDS.

    Family and domain databases

    Gene3Di3.90.230.10. 1 hit.
    HAMAPiMF_01974. MetAP_1.
    InterProiIPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 1 hit.
    TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
    PROSITEiPS00680. MAP_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O66489-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIELYSQRE IEKIRKASQI VAEVLHIVAE NVKPGVSTWD LEMIARKETE    50
    KRGAKPAFLG YKPPFSDVRY PAALCISIND EVVHGLPKKE KVIKEGDVVS 100
    IDFGAIYDGY AGDSAITVIA GKGSPEAQKL LEATKEALYN AIEKALPGKK 150
    VGDITKAIHE TAEKYGFKTI LRYGGHGVGR KVHQEPFVPN NVKDIGKKNP 200
    RLRQGMVIAI EPMLSIGTEE TVEDGDGWTV KTKDGSLAAH FEHTVAITKK 250
    GPVILTEL 258
    Length:258
    Mass (Da):28,185
    Last modified:August 1, 1998 - v1
    Checksum:iD2EE530C81D09C07
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000657 Genomic DNA. Translation: AAC06448.1.
    PIRiF70307.
    RefSeqiNP_213049.1. NC_000918.1.

    Genome annotation databases

    EnsemblBacteriaiAAC06448; AAC06448; aq_076.
    GeneIDi1192502.
    KEGGiaae:aq_076.
    PATRICi20957853. VBIAquAeo85532_0067.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000657 Genomic DNA. Translation: AAC06448.1 .
    PIRi F70307.
    RefSeqi NP_213049.1. NC_000918.1.

    3D structure databases

    ProteinModelPortali O66489.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224324.aq_076.

    Protein family/group databases

    MEROPSi M24.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC06448 ; AAC06448 ; aq_076 .
    GeneIDi 1192502.
    KEGGi aae:aq_076.
    PATRICi 20957853. VBIAquAeo85532_0067.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030426.
    KOi K01265.
    OMAi MPGDRPL.
    OrthoDBi EOG6MWNDS.

    Enzyme and pathway databases

    BioCyci AAEO224324:GJBH-64-MONOMER.

    Family and domain databases

    Gene3Di 3.90.230.10. 1 hit.
    HAMAPi MF_01974. MetAP_1.
    InterProi IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 1 hit.
    TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
    PROSITEi PS00680. MAP_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: VF5.

    Entry informationi

    Entry nameiMAP1_AQUAE
    AccessioniPrimary (citable) accession number: O66489
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 100 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