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P41392

- MAP1_KLEOX

UniProt

P41392 - MAP1_KLEOX

Protein

Methionine aminopeptidase

Gene

map

Organism
Klebsiella oxytoca
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
    OrganismiKlebsiella oxytoca
    Taxonomic identifieri571 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 43›43Methionine aminopeptidasePRO_0000148943Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP41392.
    SMRiP41392. Positions 1-41.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

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

    Sequencei

    Sequence statusi: Fragment.

    P41392-1 [UniParc]FASTAAdd to Basket

    « Hide

    TVKTKDRSLS AQYEHTIVVT DNGCEILTLR KDDTIPAIIS HNE          43
    Length:43
    Mass (Da):4,826
    Last modified:November 1, 1995 - v1
    Checksum:i5E030E6D4A3049E1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78685 Genomic DNA. Translation: CAA55352.1.
    PIRiS54755. S43195.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78685 Genomic DNA. Translation: CAA55352.1 .
    PIRi S54755. S43195.

    3D structure databases

    ProteinModelPortali P41392.
    SMRi P41392. Positions 1-41.
    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 ]
    SUPFAMi SSF55920. SSF55920. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The role of uridylyltransferase in the control of Klebsiella pneumoniae nif gene regulation."
      Edwards R.A., Merrick M.J.
      Mol. Gen. Genet. 247:189-198(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: M5a1.

    Entry informationi

    Entry nameiMAP1_KLEOX
    AccessioniPrimary (citable) accession number: P41392
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 79 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