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P56218

- MAP2_PYRFU

UniProt

P56218 - MAP2_PYRFU

Protein

Methionine aminopeptidase

Gene

map

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (15 Jul 1998)
      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).1 PublicationUniRule annotation

    Catalytic activityi

    Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.1 PublicationUniRule 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.1 PublicationUniRule annotation

    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei62 – 621SubstrateUniRule annotation
    Metal bindingi82 – 821Divalent metal cation 1
    Metal bindingi93 – 931Divalent metal cation 1
    Metal bindingi93 – 931Divalent metal cation 2; catalytic
    Metal bindingi153 – 1531Divalent metal cation 2; catalytic; via tele nitrogen
    Binding sitei161 – 1611Substrate
    Metal bindingi187 – 1871Divalent metal cation 2; catalytic
    Metal bindingi280 – 2801Divalent metal cation 1
    Metal bindingi280 – 2801Divalent metal cation 2; catalytic

    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

    MEROPSiM24.035.

    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
    ProteomesiUP000001013: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi161 – 1611H → A: Reduces enzymatic activity by 96% at 37 degrees Celsius and by 88% at 87 degrees Celsius; when associated with A-173. 1 Publication
    Mutagenesisi173 – 1731H → A: Reduces enzymatic activity by 96% at 37 degrees Celsius and by 88% at 87 degrees Celsius; when associated with A-161. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 295295Methionine aminopeptidasePRO_0000148978Add
    BLAST

    Proteomic databases

    PRIDEiP56218.

    Interactioni

    Subunit structurei

    Monomer.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    STRINGi186497.PF0541.

    Structurei

    Secondary structure

    1
    295
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 2321
    Helixi30 – 4314
    Beta strandi47 – 504
    Beta strandi53 – 564
    Beta strandi59 – 613
    Beta strandi78 – 8710
    Beta strandi90 – 9910
    Helixi106 – 12116
    Helixi129 – 14012
    Turni141 – 1433
    Beta strandi148 – 1503
    Beta strandi152 – 1543
    Beta strandi159 – 1613
    Beta strandi165 – 1695
    Beta strandi183 – 1864
    Beta strandi189 – 1935
    Beta strandi197 – 20812
    Helixi217 – 22913
    Turni230 – 2323
    Beta strandi235 – 2373
    Helixi238 – 2403
    Turni241 – 2433
    Helixi246 – 25813
    Beta strandi261 – 27010
    Beta strandi276 – 2783
    Beta strandi280 – 2856
    Beta strandi287 – 2926

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 1-295.
    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

    eggNOGiCOG0024.
    HOGENOMiHOG000226277.
    KOiK01265.
    OMAiERYKLHA.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPiMF_01975. MetAP_2_arc.
    InterProiIPR028595. MetAP_archaeal.
    IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    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.
    SUPFAMiSSF55920. 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

    MDTEKLMKAG EIAKKVREKA IKLARPGMLL LELAESIEKM IMELGGKPAF    50
    PVNLSINEIA AHYTPYKGDT TVLKEGDYLK IDVGVHIDGF IADTAVTVRV 100
    GMEEDELMEA AKEALNAAIS VARAGVEIKE LGKAIENEIR KRGFKPIVNL 150
    SGHKIERYKL HAGISIPNIY RPHDNYVLKE GDVFAIEPFA TIGAGQVIEV 200
    PPTLIYMYVR DVPVRVAQAR FLLAKIKREY GTLPFAYRWL QNDMPEGQLK 250
    LALKTLEKAG AIYGYPVLKE IRNGIVAQFE HTIIVEKDSV IVTTE 295
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009950 Genomic DNA. Translation: AAL80665.1.
    PIRiJC5671.
    RefSeqiNP_578270.1. NC_003413.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009950 Genomic DNA. Translation: AAL80665.1 .
    PIRi JC5671.
    RefSeqi NP_578270.1. NC_003413.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WKM X-ray 2.30 A/B 1-295 [» ]
    1XGM X-ray 2.80 A/B 1-295 [» ]
    1XGN X-ray 2.90 A/B 1-295 [» ]
    1XGO X-ray 3.50 A 1-295 [» ]
    1XGS X-ray 1.75 A/B 1-295 [» ]
    2DFI X-ray 2.10 A/B 1-292 [» ]
    ProteinModelPortali P56218.
    SMRi P56218. Positions 1-295.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 186497.PF0541.

    Chemistry

    ChEMBLi CHEMBL4857.

    Protein family/group databases

    MEROPSi M24.035.

    Proteomic databases

    PRIDEi P56218.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL80665 ; AAL80665 ; PF0541 .
    GeneIDi 1468383.
    KEGGi pfu:PF0541.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226277.
    KOi K01265.
    OMAi ERYKLHA.

    Miscellaneous databases

    EvolutionaryTracei P56218.
    PROi P56218.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPi MF_01975. MetAP_2_arc.
    InterProi IPR028595. MetAP_archaeal.
    IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10804:SF9. PTHR10804:SF9. 1 hit.
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 2 hits.
    TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
    PROSITEi PS01202. MAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
      Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
      Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    2. "Methionine aminopeptidase from the hyperthermophilic Archaeon Pyrococcus furiosus: molecular cloning and overexpression in Escherichia coli of the gene, and characteristics of the enzyme."
      Tsunasawa S., Izu Y., Miyagi M., Kato I.
      J. Biochem. 122:843-850(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-35, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    3. "Overexpression and divalent metal binding properties of the methionyl aminopeptidase from Pyrococcus furiosus."
      Meng L., Ruebush S., D'souza V.M., Copik A.J., Tsunasawa S., Holz R.C.
      Biochemistry 41:7199-7208(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    4. "Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus."
      Tahirov T.H., Oki H., Tsukihara T., Ogasahara K., Yutani K., Ogata K., Izu Y., Tsunasawa S., Kato I.
      J. Mol. Biol. 284:101-124(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH COBALT, MUTAGENESIS OF HIS-161 AND HIS-173.
    5. "EPR and X-ray crystallographic characterization of the product-bound form of the MnII-loaded methionyl aminopeptidase from Pyrococcus furiosus."
      Copik A.J., Nocek B.P., Swierczek S.I., Ruebush S., Jang S.B., Meng L., D'souza V.M., Peters J.W., Bennett B., Holz R.C.
      Biochemistry 44:121-129(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MANGANESE AND METHIONINE.

    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: October 1, 2014
    This is version 116 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

    External Data

    Dasty 3