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P9WK19

- MAP12_MYCTU

UniProt

P9WK19 - MAP12_MYCTU

Protein

Methionine aminopeptidase 2

Gene

map

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 6 (01 Oct 2014)
      Sequence version 1 (16 Apr 2014)
      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.2 PublicationsUniRule 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

    Enzyme regulationi

    Inhibited by bengamide derivatives and by various metalloform-selective inhibitors.2 Publications

    Kineticsi

    1. KM=58 µM for Met-Gly-Met-Met (at pH 7.5 and at 37 degrees Celsius)2 Publications
    2. KM=394 µM for Met-Ala-Ser (at pH 7.5 and at 37 degrees Celsius)2 Publications

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius. It lost all its activities at 55 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei114 – 1141Substrate
    Metal bindingi131 – 1311Divalent metal cation 1
    Metal bindingi142 – 1421Divalent metal cation 1
    Metal bindingi142 – 1421Divalent metal cation 2; catalytic
    Metal bindingi205 – 2051Divalent metal cation 2; catalytic; via tele nitrogen
    Binding sitei212 – 2121Substrate
    Metal bindingi238 – 2381Divalent metal cation 2; catalytic
    Metal bindingi269 – 2691Divalent metal cation 1
    Metal bindingi269 – 2691Divalent 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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 2UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2UniRule annotation
    Short name:
    MetAP 2UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Name:mapUniRule annotation
    Synonyms:mapB
    Ordered Locus Names:Rv2861c
    ORF Names:MTV003.07c
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001584: Chromosome

    Organism-specific databases

    TubercuListiRv2861c.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 285285Methionine aminopeptidase 2PRO_0000148948Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Structurei

    Secondary structure

    1
    285
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni26 – 294
    Beta strandi30 – 323
    Beta strandi36 – 383
    Helixi44 – 6623
    Helixi74 – 8714
    Turni93 – 964
    Helixi97 – 993
    Beta strandi102 – 1087
    Beta strandi111 – 1133
    Beta strandi127 – 13610
    Beta strandi139 – 14810
    Helixi154 – 17219
    Helixi182 – 19211
    Turni193 – 1953
    Beta strandi200 – 2023
    Beta strandi204 – 2063
    Beta strandi208 – 2125
    Beta strandi233 – 2375
    Beta strandi240 – 2445
    Beta strandi248 – 2503
    Beta strandi257 – 2593
    Beta strandi265 – 2673
    Beta strandi269 – 2746
    Beta strandi276 – 2838

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y1NX-ray1.51A1-285[»]
    1YJ3X-ray1.60A1-285[»]
    3IU7X-ray1.40A1-285[»]
    3IU8X-ray1.85A1-285[»]
    3IU9X-ray1.75A1-285[»]
    3PKAX-ray1.25A1-285[»]
    3PKBX-ray1.25A1-285[»]
    3PKCX-ray1.47A1-285[»]
    3PKDX-ray1.47A1-285[»]
    3PKEX-ray1.60A1-285[»]
    3RORX-ray2.00A1-285[»]
    4IDYX-ray2.00A1-285[»]
    4IECX-ray2.00A1-285[»]
    4IF7X-ray2.00A1-285[»]
    ProteinModelPortaliP9WK19.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01265.
    PhylomeDBiP9WK19.

    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.

    P9WK19-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSRTALSPG VLSPTRPVPN WIARPEYVGK PAAQEGSEPW VQTPEVIEKM    50
    RVAGRIAAGA LAEAGKAVAP GVTTDELDRI AHEYLVDNGA YPSTLGYKGF 100
    PKSCCTSLNE VICHGIPDST VITDGDIVNI DVTAYIGGVH GDTNATFPAG 150
    DVADEHRLLV DRTREATMRA INTVKPGRAL SVIGRVIESY ANRFGYNVVR 200
    DFTGHGIGTT FHNGLVVLHY DQPAVETIMQ PGMTFTIEPM INLGALDYEI 250
    WDDGWTVVTK DRKWTAQFEH TLLVTDTGVE ILTCL 285
    Length:285
    Mass (Da):30,891
    Last modified:April 16, 2014 - v1
    Checksum:iE69831250E6C6130
    GO

    Mass spectrometryi

    Molecular mass is 32516 Da from positions 1 - 285. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP45662.1.
    PIRiG70885.
    RefSeqiYP_006516313.1. NC_018143.2.
    YP_177911.1. NC_000962.3.

    Genome annotation databases

    GeneIDi13317652.
    888596.
    KEGGimtu:Rv2861c.
    mtv:RVBD_2861c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP45662.1 .
    PIRi G70885.
    RefSeqi YP_006516313.1. NC_018143.2.
    YP_177911.1. NC_000962.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Y1N X-ray 1.51 A 1-285 [» ]
    1YJ3 X-ray 1.60 A 1-285 [» ]
    3IU7 X-ray 1.40 A 1-285 [» ]
    3IU8 X-ray 1.85 A 1-285 [» ]
    3IU9 X-ray 1.75 A 1-285 [» ]
    3PKA X-ray 1.25 A 1-285 [» ]
    3PKB X-ray 1.25 A 1-285 [» ]
    3PKC X-ray 1.47 A 1-285 [» ]
    3PKD X-ray 1.47 A 1-285 [» ]
    3PKE X-ray 1.60 A 1-285 [» ]
    3ROR X-ray 2.00 A 1-285 [» ]
    4IDY X-ray 2.00 A 1-285 [» ]
    4IEC X-ray 2.00 A 1-285 [» ]
    4IF7 X-ray 2.00 A 1-285 [» ]
    ProteinModelPortali P9WK19.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 13317652.
    888596.
    KEGGi mtu:Rv2861c.
    mtv:RVBD_2861c.

    Organism-specific databases

    TubercuListi Rv2861c.

    Phylogenomic databases

    KOi K01265.
    PhylomeDBi P9WK19.

    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 25618 / H37Rv.
    2. "Expression and characterization of two functional methionine aminopeptidases from Mycobacterium tuberculosis H37Rv."
      Zhang X., Chen S., Hu Z., Zhang L., Wang H.
      Curr. Microbiol. 59:520-525(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A METHIONINE AMINOPEPTIDASE, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MASS SPECTROMETRY.
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 25618 / H37Rv.
    4. "Identification of an SH3-binding motif in a new class of methionine aminopeptidases from Mycobacterium tuberculosis suggests a mode of interaction with the ribosome."
      Addlagatta A., Quillin M.L., Omotoso O., Liu J.O., Matthews B.W.
      Biochemistry 44:7166-7174(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) IN COMPLEXES WITH COBALT IONS AND METHIONINE.
    5. "Catalysis and inhibition of Mycobacterium tuberculosis methionine aminopeptidase."
      Lu J.P., Chai S.C., Ye Q.Z.
      J. Med. Chem. 53:1329-1337(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, FUNCTION AS A METHIONINE AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR.
    6. "Inhibition of Mycobacterium tuberculosis methionine aminopeptidases by bengamide derivatives."
      Lu J.P., Yuan X.H., Yuan H., Wang W.L., Wan B., Franzblau S.G., Ye Q.Z.
      ChemMedChem 6:1041-1048(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MANGANESE IONS, COFACTOR, ENZYME REGULATION.

    Entry informationi

    Entry nameiMAP12_MYCTU
    AccessioniPrimary (citable) accession number: P9WK19
    Secondary accession number(s): L0TDS5, O33343, P0A5J2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: October 1, 2014
    This is version 6 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, Reference proteome

    Documents

    1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3