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P9WK20

- MAP11_MYCTO

UniProt

P9WK20 - MAP11_MYCTO

Protein

Methionine aminopeptidase 1

Gene

map-1

Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 6 (01 Oct 2014)
      Sequence version 1 (16 Apr 2014)
      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 sitei88 – 881SubstrateUniRule annotation
    Metal bindingi106 – 1061Divalent metal cation 1UniRule annotation
    Metal bindingi117 – 1171Divalent metal cation 1UniRule annotation
    Metal bindingi117 – 1171Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi186 – 1861Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei193 – 1931SubstrateUniRule annotation
    Metal bindingi219 – 2191Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi250 – 2501Divalent metal cation 1UniRule annotation
    Metal bindingi250 – 2501Divalent 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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 1UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 1UniRule annotation
    Short name:
    MetAP 1UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Name:map-1UniRule annotation
    Synonyms:mapA
    Ordered Locus Names:MT0758
    OrganismiMycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
    Taxonomic identifieri83331 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001020: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 266266Methionine aminopeptidase 1PRO_0000427730Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP9WK20.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01265.

    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.

    Sequencei

    Sequence statusi: Complete.

    P9WK20-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPLARLRGR RVVPQRSAGE LDAMAAAGAV VAAALRAIRA AAAPGTSSLS    50
    LDEIAESVIR ESGATPSFLG YHGYPASICA SINDRVVHGI PSTAEVLAPG 100
    DLVSIDCGAV LDGWHGDAAI TFGVGALSDA DEALSEATRE SLQAGIAAMV 150
    VGNRLTDVAH AIETGTRAAE LRYGRSFGIV AGYGGHGIGR QMHMDPFLPN 200
    EGAPGRGPLL AAGSVLAIEP MLTLGTTKTV VLDDKWTVTT ADGSRAAHWE 250
    HTVAVTDDGP RILTLG 266
    Length:266
    Mass (Da):27,277
    Last modified:April 16, 2014 - v1
    Checksum:iA187BD61E62449E1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000516 Genomic DNA. Translation: AAK44992.1.
    RefSeqiNP_335178.1. NC_002755.2.

    Genome annotation databases

    GeneIDi926052.
    KEGGimtc:MT0758.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000516 Genomic DNA. Translation: AAK44992.1 .
    RefSeqi NP_335178.1. NC_002755.2.

    3D structure databases

    ProteinModelPortali P9WK20.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 926052.
    KEGGi mtc:MT0758.

    Phylogenomic databases

    KOi K01265.

    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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CDC 1551 / Oshkosh.

    Entry informationi

    Entry nameiMAP11_MYCTO
    AccessioniPrimary (citable) accession number: P9WK20
    Secondary accession number(s): L0T6B7, Q79FX0, Q7D9D5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: October 1, 2014
    This is version 6 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

    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