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P47418

- MAP1_MYCGE

UniProt

P47418 - MAP1_MYCGE

Protein

Methionine aminopeptidase

Gene

map

Organism
Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      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 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 bindingi169 – 1691Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei176 – 1761SubstrateUniRule annotation
    Metal bindingi202 – 2021Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi233 – 2331Divalent metal cation 1UniRule annotation
    Metal bindingi233 – 2331Divalent 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

    BioCyciMGEN243273:GH2R-181-MONOMER.

    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:MG172
    OrganismiMycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
    Taxonomic identifieri243273 [NCBI]
    Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
    ProteomesiUP000000807: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 248248Methionine aminopeptidasePRO_0000148946Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi243273.MG_172.

    Structurei

    3D structure databases

    ProteinModelPortaliP47418.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    KOiK01265.
    OMAiNIIQTHA.
    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.

    P47418-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIYLKSANEV AGIKKACAIF KAVKAYFTIE KLLGKKLVTI DRLIKQFIEQ    50
    KQAKCAFHGY LGFPGFNCLS LNQTVIHGVA DQTVFKDSDK LTLDIGIDYH 100
    GYLCDAAFTL LGNKADPKAV KLLNDVEQAF SKVIEPELFV NNPIGNLSNA 150
    IQTYFENKGY FLVKEFGGHG CGIKIHEDPL ILNWGEKNQG VRLQEGMVIC 200
    IEPMVMTDSS EITMAANNWN VLTLKSKFNC HVEQMYHITN NGFECLTN 248
    Length:248
    Mass (Da):27,738
    Last modified:February 1, 1996 - v1
    Checksum:iEE3E965632AD7E76
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L43967 Genomic DNA. Translation: AAC71390.1.
    PIRiA64219.
    RefSeqiNP_072835.1. NC_000908.2.

    Genome annotation databases

    EnsemblBacteriaiAAC71390; AAC71390; MG_172.
    GeneIDi875255.
    KEGGimge:MG_172.
    PATRICi20009776. VBIMycGen98045_0194.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L43967 Genomic DNA. Translation: AAC71390.1 .
    PIRi A64219.
    RefSeqi NP_072835.1. NC_000908.2.

    3D structure databases

    ProteinModelPortali P47418.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243273.MG_172.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC71390 ; AAC71390 ; MG_172 .
    GeneIDi 875255.
    KEGGi mge:MG_172.
    PATRICi 20009776. VBIMycGen98045_0194.

    Phylogenomic databases

    eggNOGi COG0024.
    KOi K01265.
    OMAi NIIQTHA.
    OrthoDBi EOG6MWNDS.

    Enzyme and pathway databases

    BioCyci MGEN243273:GH2R-181-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: ATCC 33530 / G-37 / NCTC 10195.

    Entry informationi

    Entry nameiMAP1_MYCGE
    AccessioniPrimary (citable) accession number: P47418
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 101 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. Mycoplasma genitalium
      Mycoplasma genitalium (strain G-37): 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