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O52353

- MAP1_MYCGA

UniProt

O52353 - MAP1_MYCGA

Protein

Methionine aminopeptidase

Gene

map

Organism
Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (15 Aug 2003)
      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 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

    BioCyciMGAL710127:GC09-73-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:MYCGA0720
    ORF Names:MGA_0745
    OrganismiMycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
    Taxonomic identifieri710127 [NCBI]
    Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
    ProteomesiUP000001418: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 250250Methionine aminopeptidasePRO_0000148945Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi233150.MGA_0745.

    Structurei

    3D structure databases

    ProteinModelPortaliO52353.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030426.
    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.

    O52353-1 [UniParc]FASTAAdd to Basket

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    MIYIKNPNEI QKIKNAAQIY KKIVKQFNFD YIKNKSLKEI DQMLRDFVSQ    50
    HHANSCYHGY LGFKGYHCLS LNQTIIHGLA NDEIFTSKDK LTIDIGIELD 100
    NYYCDSAFTI LGPDVNPRQK LLSEVTHNCI FELVKKIVPN QTTTNDLGIW 150
    TEEYAKKYGY SVIKDFGGHG CGIKIHEDPI ILNYGTKKSS ELLTPNMVIC 200
    IEPMFFEKDN RYYIDPDDSW SVKPVNKNQY VCHWEHMVLI KEDQAEILTL 250
    Length:250
    Mass (Da):29,026
    Last modified:August 15, 2003 - v2
    Checksum:iF7EE9B91D4779F76
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731Q → K in AAB95408. (PubMed:10867916)Curated
    Sequence conflicti83 – 831E → D in AAB95408. (PubMed:10867916)Curated
    Sequence conflicti117 – 1171P → L in AAB95408. (PubMed:10867916)Curated
    Sequence conflicti132 – 1321E → D in AAB95408. (PubMed:10867916)Curated
    Sequence conflicti158 – 1581Y → H in AAB95408. (PubMed:10867916)Curated
    Sequence conflicti161 – 1611S → N in AAB95408. (PubMed:10867916)Curated
    Sequence conflicti189 – 1902SS → PG in AAB95408. (PubMed:10867916)Curated
    Sequence conflicti217 – 2171D → V in AAB95408. (PubMed:10867916)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036708 Genomic DNA. Translation: AAB95408.1.
    AE015450 Genomic DNA. Translation: AAP56422.1.
    RefSeqiNP_852854.1. NC_004829.2.

    Genome annotation databases

    EnsemblBacteriaiAAP56422; AAP56422; MGA_0745.
    GeneIDi1090121.
    KEGGimga:MGA_0745.
    PATRICi20007816. VBIMycGal115357_0076.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036708 Genomic DNA. Translation: AAB95408.1 .
    AE015450 Genomic DNA. Translation: AAP56422.1 .
    RefSeqi NP_852854.1. NC_004829.2.

    3D structure databases

    ProteinModelPortali O52353.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 233150.MGA_0745.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP56422 ; AAP56422 ; MGA_0745 .
    GeneIDi 1090121.
    KEGGi mga:MGA_0745.
    PATRICi 20007816. VBIMycGal115357_0076.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci MGAL710127:GC09-73-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. "Determination and analysis of the nucleotide sequence of a segment of a Mycoplasma gallisepticum strain A5969 chromosome, containing operons S10 and rrn23-5."
      Skamrov A.V., Gol'dman M.A., Feoktistova E.S., Bibilashvili R.S.
      Mol. Biol. (Mosk.) 34:390-396(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: A5969Var.B.
    2. "The complete genome sequence of the avian pathogen Mycoplasma gallisepticum strain R(low)."
      Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F., Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.
      Microbiology 149:2307-2316(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: R(low / passage 15 / clone 2).

    Entry informationi

    Entry nameiMAP1_MYCGA
    AccessioniPrimary (citable) accession number: O52353
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: August 15, 2003
    Last modified: October 1, 2014
    This is version 107 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