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Protein

Methionine aminopeptidase

Gene

map

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: -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

    Keywordsi

    Molecular functionAminopeptidase, Hydrolase, Protease
    LigandMetal-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
    OMAiHTVLLMP
    OrthoDBiPOG093Z06FJ

    Family and domain databases

    CDDicd01088 MetAP2, 1 hit
    Gene3Di1.10.10.10, 1 hit
    HAMAPiMF_01975 MetAP_2_arc, 1 hit
    InterProiView protein in InterPro
    IPR036005 Creatinase/aminopeptidase-like
    IPR028595 MetAP_archaeal
    IPR000994 Pept_M24
    IPR001714 Pept_M24_MAP
    IPR002468 Pept_M24A_MAP2
    IPR018349 Pept_M24A_MAP2_BS
    IPR036388 WH-like_DNA-bd_sf
    IPR036390 WH_DNA-bd_sf
    PfamiView protein in Pfam
    PF00557 Peptidase_M24, 1 hit
    PRINTSiPR00599 MAPEPTIDASE
    SUPFAMiSSF46785 SSF46785, 1 hit
    SSF55920 SSF55920, 2 hits
    TIGRFAMsiTIGR00501 met_pdase_II, 1 hit
    PROSITEiView protein in PROSITE
    PS01202 MAP_2, 1 hit

    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
    PATRICifig|186497.12.peg.569

    Similar proteinsi

    Entry informationi

    Entry nameiMAP2_PYRFU
    AccessioniPrimary (citable) accession number: P56218
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 15, 1998
    Last modified: March 28, 2018
    This is version 139 of the entry and version 1 of the sequence. See 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

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