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O51132

- MAP1_BORBU

UniProt

O51132 - MAP1_BORBU

Protein

Methionine aminopeptidase

Gene

map

Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      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 sitei79 – 791SubstrateUniRule annotation
    Metal bindingi96 – 961Divalent metal cation 1UniRule annotation
    Metal bindingi107 – 1071Divalent metal cation 1UniRule annotation
    Metal bindingi107 – 1071Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi170 – 1701Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei177 – 1771SubstrateUniRule annotation
    Metal bindingi204 – 2041Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi235 – 2351Divalent metal cation 1UniRule annotation
    Metal bindingi235 – 2351Divalent 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

    BioCyciBBUR224326:G9SO-104-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:BB_0105
    OrganismiBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
    Taxonomic identifieri224326 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group
    ProteomesiUP000001807: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 251251Methionine aminopeptidasePRO_0000148928Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi224326.BB0105.

    Structurei

    3D structure databases

    ProteinModelPortaliO51132.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    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.

    O51132-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKLRLKSKD EIKKIKASAS LLALTLLEVE RNIVPGISTK ELDLIAYDFI    50
    IKNRAKPAFK GYRGFKGTIC ASVNEEVIHG IPGKRKLADG DIVSIDCGVI 100
    LDGFYSDMAK TFKVGNVDSS IDKLLEVTNA SLYKGIAEMK VGNRILNISK 150
    AIEDYIKPFG FGIVREYTGH GVGFELHEEP SVPNYYAPFF KNIRIQEGMV 200
    LAIEPMVNLR GHKVSIKSDG WTVFASDLSY SAHFEHTVAV VDGLPLILSE 250
    V 251
    Length:251
    Mass (Da):27,711
    Last modified:June 1, 1998 - v1
    Checksum:i807996A2B082BC1C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000783 Genomic DNA. Translation: AAC66499.1.
    PIRiA70113.
    RefSeqiNP_212239.1. NC_001318.1.
    WP_010889683.1. NC_001318.1.

    Genome annotation databases

    EnsemblBacteriaiAAC66499; AAC66499; BB_0105.
    GeneIDi1194941.
    KEGGibbu:BB_0105.
    PATRICi20556816. VBIBorBur75917_0503.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000783 Genomic DNA. Translation: AAC66499.1 .
    PIRi A70113.
    RefSeqi NP_212239.1. NC_001318.1.
    WP_010889683.1. NC_001318.1.

    3D structure databases

    ProteinModelPortali O51132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224326.BB0105.

    Protein family/group databases

    MEROPSi M24.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC66499 ; AAC66499 ; BB_0105 .
    GeneIDi 1194941.
    KEGGi bbu:BB_0105.
    PATRICi 20556816. VBIBorBur75917_0503.

    Phylogenomic databases

    eggNOGi COG0024.
    OMAi MPGDRPL.
    OrthoDBi EOG6MWNDS.

    Enzyme and pathway databases

    BioCyci BBUR224326:G9SO-104-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: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

    Entry informationi

    Entry nameiMAP1_BORBU
    AccessioniPrimary (citable) accession number: O51132
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 105 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