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P28617

- MAP1_GEOSE

UniProt

P28617 - MAP1_GEOSE

Protein

Methionine aminopeptidase

Gene

map

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
  1. 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 By similarity.By similarity

    Catalytic activityi

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

    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 By similarity.By similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase (EC:3.4.11.18)
    Short name:
    MAP
    Short name:
    MetAP
    Alternative name(s):
    Peptidase M
    Gene namesi
    Name:map
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›51›51Methionine aminopeptidasePRO_0000148926Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP28617.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.90.230.10. 1 hit.
    InterProiIPR000994. Pept_M24_structural-domain.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    SUPFAMiSSF55920. SSF55920. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

    P28617-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIICKTAHEI TLMREAGKIV SATLEELKNH IRPGVTTKEL DAIAEEVIRS   50
    H 51
    Length:51
    Mass (Da):5,698
    Last modified:December 1, 1992 - v1
    Checksum:i1E270FB8C42489D8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei51 – 511

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88104 Genomic DNA. Translation: AAA22206.1.
    PIRiC42196.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88104 Genomic DNA. Translation: AAA22206.1 .
    PIRi C42196.

    3D structure databases

    ProteinModelPortali P28617.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.90.230.10. 1 hit.
    InterProi IPR000994. Pept_M24_structural-domain.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55920. SSF55920. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Zinc, a novel structural element found in the family of bacterial adenylate kinases."
      Glaser P., Presecan E., Delepierre M., Surewicz W.K., Mantsch H.H., Barzu O., Gilles A.M.
      Biochemistry 31:3038-3043(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiMAP1_GEOSE
    AccessioniPrimary (citable) accession number: P28617
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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