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Q89AP3

- MAP1_BUCBP

UniProt

Q89AP3 - MAP1_BUCBP

Protein

Methionine aminopeptidase

Gene

map

Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    • Comment

    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 sitei80 – 801SubstrateUniRule annotation
    Metal bindingi98 – 981Divalent metal cation 1UniRule annotation
    Metal bindingi109 – 1091Divalent metal cation 1UniRule annotation
    Metal bindingi109 – 1091Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi172 – 1721Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei179 – 1791SubstrateUniRule 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

    BioCyciBAPH224915:GJ9D-212-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:bbp_212
    OrganismiBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
    Taxonomic identifieri224915 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
    ProteomesiUP000000601: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 266266Methionine aminopeptidasePRO_0000148931Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi224915.bbp212.

    Structurei

    3D structure databases

    ProteinModelPortaliQ89AP3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    KOiK01265.
    OMAiEGMCFTI.
    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.

    Q89AP3-1 [UniParc]FASTAAdd to Basket

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    MTCIFIKNIN EINKMRLVGK LVADVLDMIK EYIVPGITTE ELNNICHNYI    50
    TYKQHAKPAC LGYQGFPKSI CTSINDIVCH GIPNKNSILK NGDIINIDVA 100
    ILKDKYYSDA SKMFFVGKPT ELGKKLCYVA KKSLYLALYT IRPGINLQKL 150
    GKVIQNYVKK QNFSIVKEYC GHGIGRSFHE PPQILHHNYY KSNTTILQSG 200
    MTFTVEPMIN SGSCEVQCTN DGWTVKTKDK SLSAQYEHTI LVNEEGCEIL 250
    TLQKGEQISR ILKNLT 266
    Length:266
    Mass (Da):30,049
    Last modified:June 1, 2003 - v1
    Checksum:i564C2FC926EEBCA6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016826 Genomic DNA. Translation: AAO26944.1.
    RefSeqiNP_777839.1. NC_004545.1.
    WP_011091345.1. NC_004545.1.

    Genome annotation databases

    EnsemblBacteriaiAAO26944; AAO26944; bbp_212.
    GeneIDi1058483.
    KEGGibab:bbp212.
    PATRICi21245199. VBIBucAph80364_0206.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016826 Genomic DNA. Translation: AAO26944.1 .
    RefSeqi NP_777839.1. NC_004545.1.
    WP_011091345.1. NC_004545.1.

    3D structure databases

    ProteinModelPortali Q89AP3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224915.bbp212.

    Protein family/group databases

    MEROPSi M24.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO26944 ; AAO26944 ; bbp_212 .
    GeneIDi 1058483.
    KEGGi bab:bbp212.
    PATRICi 21245199. VBIBucAph80364_0206.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BAPH224915:GJ9D-212-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: Bp.

    Entry informationi

    Entry nameiMAP1_BUCBP
    AccessioniPrimary (citable) accession number: Q89AP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 14, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 84 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