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Protein

Methionine aminopeptidase

Gene

map

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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).UniRule annotation1 Publication

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation1 Publication

Cofactori

Co2+UniRule annotation1 Publication, Zn2+UniRule annotation1 Publication, Mn2+UniRule annotation1 Publication, Fe2+UniRule annotation1 PublicationNote: 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 annotation1 Publication

Kineticsi

  1. KM=9.2 mM for a Met-Ala-Ser peptide (for the Fe2+-complexed enzyme)2 Publications
  2. KM=11.8 mM for a Met-Ala-Ser peptide (for the Co2+-complexed enzyme)2 Publications
  3. KM=5.0 mM for a Met-Gly-Met-Met peptide (for the Fe2+-complexed enzyme)2 Publications
  4. KM=5.1 mM for a Met-Gly-Met-Met peptide (for the Co2+-complexed enzyme)2 Publications
  5. KM=1.3 mM for a Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Fe2+-complexed enzyme)2 Publications
  6. KM=2.0 mM for a Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Co2+-complexed enzyme)2 Publications

    pH dependencei

    Optimum pH is 7-8.2 Publications

    Temperature dependencei

    Optimum temperature is about 90 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei62SubstrateUniRule annotation1
    Metal bindingi82Divalent metal cation 11
    Metal bindingi93Divalent metal cation 11
    Metal bindingi93Divalent metal cation 2; catalytic1
    Metal bindingi153Divalent metal cation 2; catalytic; via tele nitrogen1
    Binding sitei161Substrate1
    Metal bindingi187Divalent metal cation 2; catalytic1
    Metal bindingi280Divalent metal cation 11
    Metal bindingi280Divalent metal cation 2; catalytic1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BRENDAi3.4.11.18. 5243.

    Protein family/group databases

    MEROPSiM24.035.

    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:PF0541
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    Proteomesi
    • UP000001013 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi161H → A: Reduces enzymatic activity by 96% at 37 degrees Celsius and by 88% at 87 degrees Celsius; when associated with A-173. 1 Publication1
    Mutagenesisi173H → A: Reduces enzymatic activity by 96% at 37 degrees Celsius and by 88% at 87 degrees Celsius; when associated with A-161. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL4857.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001489781 – 295Methionine aminopeptidaseAdd BLAST295

    Proteomic databases

    PRIDEiP56218.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation2 Publications

    Protein-protein interaction databases

    STRINGi186497.PF0541.

    Structurei

    Secondary structure

    1295
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 23Combined sources21
    Helixi30 – 43Combined sources14
    Beta strandi47 – 50Combined sources4
    Beta strandi53 – 56Combined sources4
    Beta strandi59 – 61Combined sources3
    Beta strandi78 – 87Combined sources10
    Beta strandi90 – 99Combined sources10
    Helixi106 – 121Combined sources16
    Helixi129 – 140Combined sources12
    Turni141 – 143Combined sources3
    Beta strandi148 – 150Combined sources3
    Beta strandi152 – 154Combined sources3
    Beta strandi159 – 161Combined sources3
    Beta strandi165 – 169Combined sources5
    Beta strandi183 – 186Combined sources4
    Beta strandi189 – 193Combined sources5
    Beta strandi197 – 208Combined sources12
    Helixi217 – 229Combined sources13
    Turni230 – 232Combined sources3
    Beta strandi235 – 237Combined sources3
    Helixi238 – 240Combined sources3
    Turni241 – 243Combined sources3
    Helixi246 – 258Combined sources13
    Beta strandi261 – 270Combined sources10
    Beta strandi276 – 278Combined sources3
    Beta strandi280 – 285Combined sources6
    Beta strandi287 – 292Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1WKMX-ray2.30A/B1-295[»]
    1XGMX-ray2.80A/B1-295[»]
    1XGNX-ray2.90A/B1-295[»]
    1XGOX-ray3.50A1-295[»]
    1XGSX-ray1.75A/B1-295[»]
    2DFIX-ray2.10A/B1-292[»]
    ProteinModelPortaliP56218.
    SMRiP56218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56218.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiarCOG01001. Archaea.
    COG0024. LUCA.
    HOGENOMiHOG000226277.
    KOiK01265.
    OMAiERYKLHA.

    Family and domain databases

    CDDicd01088. MetAP2. 1 hit.
    Gene3Di1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPiMF_01975. MetAP_2_arc. 1 hit.
    InterProiIPR028595. MetAP_archaeal.
    IPR000994. Pept_M24.
    IPR001714. Pept_M24_MAP.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF46785. SSF46785. 1 hit.
    SSF55920. SSF55920. 2 hits.
    TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
    PROSITEiPS01202. MAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P56218-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDTEKLMKAG EIAKKVREKA IKLARPGMLL LELAESIEKM IMELGGKPAF
    60 70 80 90 100
    PVNLSINEIA AHYTPYKGDT TVLKEGDYLK IDVGVHIDGF IADTAVTVRV
    110 120 130 140 150
    GMEEDELMEA AKEALNAAIS VARAGVEIKE LGKAIENEIR KRGFKPIVNL
    160 170 180 190 200
    SGHKIERYKL HAGISIPNIY RPHDNYVLKE GDVFAIEPFA TIGAGQVIEV
    210 220 230 240 250
    PPTLIYMYVR DVPVRVAQAR FLLAKIKREY GTLPFAYRWL QNDMPEGQLK
    260 270 280 290
    LALKTLEKAG AIYGYPVLKE IRNGIVAQFE HTIIVEKDSV IVTTE
    Length:295
    Mass (Da):32,842
    Last modified:July 15, 1998 - v1
    Checksum:i9739BC55F812E65B
    GO

    Mass spectrometryi

    Molecular mass is 32848 Da from positions 1 - 295. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009950 Genomic DNA. Translation: AAL80665.1.
    PIRiJC5671.
    RefSeqiWP_011011659.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL80665; AAL80665; PF0541.
    GeneIDi1468383.
    KEGGipfu:PF0541.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009950 Genomic DNA. Translation: AAL80665.1.
    PIRiJC5671.
    RefSeqiWP_011011659.1. NC_003413.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1WKMX-ray2.30A/B1-295[»]
    1XGMX-ray2.80A/B1-295[»]
    1XGNX-ray2.90A/B1-295[»]
    1XGOX-ray3.50A1-295[»]
    1XGSX-ray1.75A/B1-295[»]
    2DFIX-ray2.10A/B1-292[»]
    ProteinModelPortaliP56218.
    SMRiP56218.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi186497.PF0541.

    Chemistry databases

    ChEMBLiCHEMBL4857.

    Protein family/group databases

    MEROPSiM24.035.

    Proteomic databases

    PRIDEiP56218.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL80665; AAL80665; PF0541.
    GeneIDi1468383.
    KEGGipfu:PF0541.

    Phylogenomic databases

    eggNOGiarCOG01001. Archaea.
    COG0024. LUCA.
    HOGENOMiHOG000226277.
    KOiK01265.
    OMAiERYKLHA.

    Enzyme and pathway databases

    BRENDAi3.4.11.18. 5243.

    Miscellaneous databases

    EvolutionaryTraceiP56218.

    Family and domain databases

    CDDicd01088. MetAP2. 1 hit.
    Gene3Di1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPiMF_01975. MetAP_2_arc. 1 hit.
    InterProiIPR028595. MetAP_archaeal.
    IPR000994. Pept_M24.
    IPR001714. Pept_M24_MAP.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF46785. SSF46785. 1 hit.
    SSF55920. SSF55920. 2 hits.
    TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
    PROSITEiPS01202. MAP_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMAP2_PYRFU
    AccessioniPrimary (citable) accession number: P56218
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 15, 1998
    Last modified: November 30, 2016
    This is version 131 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.