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Q9ZJT0

- MAP1_HELPJ

UniProt

Q9ZJT0 - MAP1_HELPJ

Protein

Methionine aminopeptidase

Gene

map

Organism
Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
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 May 1999)
      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 sitei78 – 781SubstrateUniRule annotation
    Metal bindingi95 – 951Divalent metal cation 1UniRule annotation
    Metal bindingi106 – 1061Divalent metal cation 1UniRule annotation
    Metal bindingi106 – 1061Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi169 – 1691Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei176 – 1761SubstrateUniRule annotation
    Metal bindingi206 – 2061Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi237 – 2371Divalent metal cation 1UniRule annotation
    Metal bindingi237 – 2371Divalent 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

    BioCyciHPYL85963:GJB9-1255-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:jhp_1219
    OrganismiHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
    Taxonomic identifieri85963 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
    ProteomesiUP000000804: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 253253Methionine aminopeptidasePRO_0000148942Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi85963.jhp1219.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ZJT0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    KOiK01265.
    OMAiHICQTHA.
    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.

    Q9ZJT0-1 [UniParc]FASTAAdd to Basket

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    MAISIKSPKE IKALRKAGEL TAQALALLER EVRPGVSLLE LDKMAEDFIK    50
    SSHARPAFKG LYGFPNSVCM SLNEVVIHGI PTDYVLQEGD IIGLDLGVEV 100
    DGYYGDSALT LPIGAISPQD EKLLACSKES LMHAISSIRV GMHFKELSQI 150
    LEGAITERGF VPLKGFCGHG IGKKPHEEPE IPNYLEKGVK ANSGPKIKEG 200
    MVFCLEPMVC QKQGEPKILA DKWSVVSVDG LNTSHHEHTI AIVGNKAVIL 250
    TER 253
    Length:253
    Mass (Da):27,464
    Last modified:May 1, 1999 - v1
    Checksum:iD588885F32C34150
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001439 Genomic DNA. Translation: AAD06803.1.
    PIRiC71833.
    RefSeqiNP_223937.1. NC_000921.1.

    Genome annotation databases

    EnsemblBacteriaiAAD06803; AAD06803; jhp_1219.
    GeneIDi889835.
    KEGGihpj:jhp1219.
    PATRICi20607280. VBIHelPyl98156_1321.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001439 Genomic DNA. Translation: AAD06803.1 .
    PIRi C71833.
    RefSeqi NP_223937.1. NC_000921.1.

    3D structure databases

    ProteinModelPortali Q9ZJT0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 85963.jhp1219.

    Protein family/group databases

    MEROPSi M24.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD06803 ; AAD06803 ; jhp_1219 .
    GeneIDi 889835.
    KEGGi hpj:jhp1219.
    PATRICi 20607280. VBIHelPyl98156_1321.

    Phylogenomic databases

    eggNOGi COG0024.
    KOi K01265.
    OMAi HICQTHA.
    OrthoDBi EOG6MWNDS.

    Enzyme and pathway databases

    BioCyci HPYL85963:GJB9-1255-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: J99 / ATCC 700824.

    Entry informationi

    Entry nameiMAP1_HELPJ
    AccessioniPrimary (citable) accession number: Q9ZJT0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 1999
    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

    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