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P57324

- MAP1_BUCAI

UniProt

P57324 - MAP1_BUCAI

Protein

Methionine aminopeptidase

Gene

map

Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Dec 2000)
      Previous versions | rss
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    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 bindingi97 – 971Divalent metal cation 1UniRule annotation
    Metal bindingi108 – 1081Divalent metal cation 1UniRule annotation
    Metal bindingi108 – 1081Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi171 – 1711Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei178 – 1781SubstrateUniRule 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

    BioCyciBAPH107806:GBZJ-230-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:BU230
    OrganismiBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)
    Taxonomic identifieri107806 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
    ProteomesiUP000001806: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 264264Methionine aminopeptidasePRO_0000148929Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP57324.
    SMRiP57324. Positions 5-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030427.
    KOiK01265.
    OMAiVEASYDV.
    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.

    P57324-1 [UniParc]FASTAAdd to Basket

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    MSCIIKTESE IKKMRISGKL AAEVLEMIKE HLQPKISTED INQICHDYIV    50
    YKKKAISACL GYHGFPKSIC ISINDVVCHG IPSKNQVFKE GDIVNIDIAI 100
    IKDGYHGDTS KMFYIGKTSI LSKRLCQVAR ESLYLSLKLV KPGIPLYKIG 150
    EIIQNYVESN NFSVVKEYCG HGIGRNFHEE PHVLHYKNKK NNIILKKGMI 200
    FTIEPMINSG NPEVKCMKDG WTVKTKDRSL SAQYEHTVLV TEYGCDILTW 250
    QKDEDISQKL VNIN 264
    Length:264
    Mass (Da):30,012
    Last modified:December 1, 2000 - v1
    Checksum:i4FCCFAE8AC9FFF3D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000003 Genomic DNA. Translation: BAB12945.1.
    RefSeqiNP_240059.1. NC_002528.1.

    Genome annotation databases

    EnsemblBacteriaiBAB12945; BAB12945; BAB12945.
    GeneIDi1109673.
    KEGGibuc:BU230.
    PATRICi21243982. VBIBucAph127364_0243.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000003 Genomic DNA. Translation: BAB12945.1 .
    RefSeqi NP_240059.1. NC_002528.1.

    3D structure databases

    ProteinModelPortali P57324.
    SMRi P57324. Positions 5-256.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M24.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB12945 ; BAB12945 ; BAB12945 .
    GeneIDi 1109673.
    KEGGi buc:BU230.
    PATRICi 21243982. VBIBucAph127364_0243.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030427.
    KOi K01265.
    OMAi VEASYDV.
    OrthoDBi EOG6MWNDS.

    Enzyme and pathway databases

    BioCyci BAPH107806:GBZJ-230-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. "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
      Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
      Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: APS.

    Entry informationi

    Entry nameiMAP1_BUCAI
    AccessioniPrimary (citable) accession number: P57324
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 92 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. Buchnera aphidicola (subsp. Acyrthosiphon pisum)
      Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3