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P50614

- MAP1_CLOPE

UniProt

P50614 - MAP1_CLOPE

Protein

Methionine aminopeptidase

Gene

map

Organism
Clostridium perfringens (strain 13 / Type A)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (31 Jan 2002)
      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 sitei77 – 771SubstrateUniRule annotation
    Metal bindingi94 – 941Divalent metal cation 1UniRule annotation
    Metal bindingi105 – 1051Divalent metal cation 1UniRule annotation
    Metal bindingi105 – 1051Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi168 – 1681Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei175 – 1751SubstrateUniRule annotation
    Metal bindingi201 – 2011Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi232 – 2321Divalent metal cation 1UniRule annotation
    Metal bindingi232 – 2321Divalent 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

    BioCyciCPER195102:GJFM-2485-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:CPE2383
    OrganismiClostridium perfringens (strain 13 / Type A)
    Taxonomic identifieri195102 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000000818: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 249249Methionine aminopeptidasePRO_0000148936Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi195102.CPE2383.

    Structurei

    3D structure databases

    ProteinModelPortaliP50614.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030426.
    KOiK01265.
    OMAiAEREMEW.
    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.

    P50614-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIILKNENEI DLMRKAGKIL GETLNLLKEK VRPGITTTEL DRIAEEFITK    50
    HGATPSFKGL YGFPASLCIS VNNQVIHGFP GSYELKDGDI VSIDCGVCLN 100
    GFHSDAARTF GVGNISEEAE KLIRITEESF FKGIEKAYVD NRLTDISNEI 150
    QQYVEANGFS VVRDFVGHGI GRKVHEDPEV PNFGRPGRGP KLMAGMVLAI 200
    EPMVNMGSYR VKTLDDGWTV VTADGKLSAH YENTVAILPN GPEILTLIK 249
    Length:249
    Mass (Da):27,323
    Last modified:January 31, 2002 - v2
    Checksum:i7FDC5CD82CEAFAC7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301K → Q in CAA60211. (PubMed:7559358)Curated
    Sequence conflicti104 – 1041S → R in CAA60211. (PubMed:7559358)Curated
    Sequence conflicti148 – 1481N → K in CAA60211. (PubMed:7559358)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000016 Genomic DNA. Translation: BAB82089.1.
    X86486 Genomic DNA. Translation: CAA60211.1.
    RefSeqiNP_563299.1. NC_003366.1.

    Genome annotation databases

    EnsemblBacteriaiBAB82089; BAB82089; BAB82089.
    GeneIDi990744.
    KEGGicpe:CPE2383.
    PATRICi19498821. VBICloPer59675_2453.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000016 Genomic DNA. Translation: BAB82089.1 .
    X86486 Genomic DNA. Translation: CAA60211.1 .
    RefSeqi NP_563299.1. NC_003366.1.

    3D structure databases

    ProteinModelPortali P50614.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 195102.CPE2383.

    Protein family/group databases

    MEROPSi M24.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB82089 ; BAB82089 ; BAB82089 .
    GeneIDi 990744.
    KEGGi cpe:CPE2383.
    PATRICi 19498821. VBICloPer59675_2453.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030426.
    KOi K01265.
    OMAi AEREMEW.
    OrthoDBi EOG6MWNDS.

    Enzyme and pathway databases

    BioCyci CPER195102:GJFM-2485-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: 13 / Type A.
    2. "Rapid expansion of the physical and genetic map of the chromosome of Clostridium perfringens CPN50."
      Katayama S., Dupuy B., Garnier T., Cole S.T.
      J. Bacteriol. 177:5680-5685(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-148.
      Strain: CPN50.

    Entry informationi

    Entry nameiMAP1_CLOPE
    AccessioniPrimary (citable) accession number: P50614
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 31, 2002
    Last modified: October 1, 2014
    This is version 104 of the entry and version 2 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