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P44421

- MAP1_HAEIN

UniProt

P44421 - MAP1_HAEIN

Protein

Methionine aminopeptidase

Gene

map

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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 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 bindingi172 – 1721Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei179 – 1791SubstrateUniRule annotation
    Metal bindingi205 – 2051Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi236 – 2361Divalent metal cation 1UniRule annotation
    Metal bindingi236 – 2361Divalent 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

    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:HI_1722
    OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
    Taxonomic identifieri71421 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000000579: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 268268Methionine aminopeptidasePRO_0000148940Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi71421.HI1722.

    Structurei

    3D structure databases

    ProteinModelPortaliP44421.
    SMRiP44421. Positions 2-262.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    KOiK01265.
    OMAiEGMCFTI.
    OrthoDBiEOG6MWNDS.
    PhylomeDBiP44421.

    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.

    P44421-1 [UniParc]FASTAAdd to Basket

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    MAIPIRTEKE IVKLREACKL ASDVLVMIEP YVKAGVTTGE LDRICHEYMV    50
    NEQKVIPACL NYHGFPKATC ISINEVVCHG IPSDDKVLKN GDIVNIDVTV 100
    IKDGYFGDNS KMYIVGGETN IRSKKLVEAA QEALYVGIRT VKPDIRLNEI 150
    GKAVQKYTES QTFSVVREYC GHGVGTEFHC EPQVLHYYAD DGGVILKPGM 200
    VFTIEPMINA GKKEVRVMGD GWTVKTKDRS HSAQYEHQLI VTETGCEVMT 250
    IRDEEIAEGR ISRIMVNV 268
    Length:268
    Mass (Da):29,896
    Last modified:November 1, 1995 - v1
    Checksum:iC71DEA15BB5E732B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC23368.1.
    PIRiC64138.
    RefSeqiNP_439863.1. NC_000907.1.

    Genome annotation databases

    EnsemblBacteriaiAAC23368; AAC23368; HI_1722.
    GeneIDi950876.
    KEGGihin:HI1722.
    PATRICi20192197. VBIHaeInf48452_1801.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC23368.1 .
    PIRi C64138.
    RefSeqi NP_439863.1. NC_000907.1.

    3D structure databases

    ProteinModelPortali P44421.
    SMRi P44421. Positions 2-262.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 71421.HI1722.

    Protein family/group databases

    MEROPSi M24.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC23368 ; AAC23368 ; HI_1722 .
    GeneIDi 950876.
    KEGGi hin:HI1722.
    PATRICi 20192197. VBIHaeInf48452_1801.

    Phylogenomic databases

    eggNOGi COG0024.
    KOi K01265.
    OMAi EGMCFTI.
    OrthoDBi EOG6MWNDS.
    PhylomeDBi P44421.

    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 51907 / DSM 11121 / KW20 / Rd.

    Entry informationi

    Entry nameiMAP1_HAEIN
    AccessioniPrimary (citable) accession number: P44421
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 105 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. Haemophilus influenzae
      Haemophilus influenzae (strain Rd): 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