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Protein

Methionine aminopeptidase 2

Gene

map

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.UniRule annotation2 Publications

Catalytic activityi

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

Cofactori

Co2+UniRule annotation2 Publications, Zn2+UniRule annotation, Mn2+UniRule annotation2 Publications, 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

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)DescriptionActionsGraphical viewLength
    Binding sitei114SubstrateUniRule annotation3 Publications1
    Metal bindingi131Divalent metal cation 1UniRule annotation3 Publications1
    Metal bindingi142Divalent metal cation 1UniRule annotation3 Publications1
    Metal bindingi142Divalent metal cation 2; catalyticUniRule annotation3 Publications1
    Metal bindingi205Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation3 Publications1
    Binding sitei212SubstrateUniRule annotation3 Publications1
    Metal bindingi238Divalent metal cation 2; catalyticUniRule annotation3 Publications1
    Metal bindingi269Divalent metal cation 1UniRule annotation3 Publications1
    Metal bindingi269Divalent metal cation 2; catalyticUniRule annotation3 Publications1

    GO - Molecular functioni

    • cobalt ion binding Source: MTBBASE
    • iron ion binding Source: MTBBASE
    • manganese ion binding Source: MTBBASE
    • metalloaminopeptidase activity Source: MTBBASE
    • nickel cation binding Source: MTBBASE

    GO - Biological processi

    • methionine metabolic process Source: MTBBASE
    • protein initiator methionine removal involved in protein maturation Source: MTBBASE
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BioCyciMTBH37RV:G185E-7112-MONOMER.

    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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    Proteomesi
    • UP000001584 Componenti: Chromosome

    Organism-specific databases

    TubercuListiRv2861c.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001489481 – 285Methionine aminopeptidase 2Add BLAST285

    Proteomic databases

    PaxDbiP9WK19.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi83332.Rv2861c.

    Structurei

    Secondary structure

    1285
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni26 – 29Combined sources4
    Beta strandi30 – 32Combined sources3
    Beta strandi36 – 38Combined sources3
    Helixi44 – 66Combined sources23
    Helixi74 – 87Combined sources14
    Turni93 – 96Combined sources4
    Helixi97 – 99Combined sources3
    Beta strandi102 – 108Combined sources7
    Beta strandi111 – 113Combined sources3
    Beta strandi127 – 136Combined sources10
    Beta strandi139 – 148Combined sources10
    Helixi154 – 172Combined sources19
    Helixi182 – 192Combined sources11
    Turni193 – 195Combined sources3
    Beta strandi200 – 202Combined sources3
    Beta strandi204 – 206Combined sources3
    Beta strandi208 – 212Combined sources5
    Beta strandi233 – 237Combined sources5
    Beta strandi240 – 244Combined sources5
    Beta strandi248 – 250Combined sources3
    Beta strandi257 – 259Combined sources3
    Beta strandi265 – 267Combined sources3
    Beta strandi269 – 274Combined sources6
    Beta strandi276 – 283Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    4OOKX-ray1.90A1-283[»]
    ProteinModelPortaliP9WK19.
    SMRiP9WK19.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG4105CA1. Bacteria.
    COG0024. LUCA.
    KOiK01265.
    OMAiVIKDEYH.
    PhylomeDBiP9WK19.

    Family and domain databases

    CDDicd01086. MetAP1. 1 hit.
    Gene3Di3.90.230.10. 1 hit.
    HAMAPiMF_01974. MetAP_1. 1 hit.
    InterProiIPR000994. Pept_M24.
    IPR001714. Pept_M24_MAP.
    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

            10         20         30         40         50
    MPSRTALSPG VLSPTRPVPN WIARPEYVGK PAAQEGSEPW VQTPEVIEKM
    60 70 80 90 100
    RVAGRIAAGA LAEAGKAVAP GVTTDELDRI AHEYLVDNGA YPSTLGYKGF
    110 120 130 140 150
    PKSCCTSLNE VICHGIPDST VITDGDIVNI DVTAYIGGVH GDTNATFPAG
    160 170 180 190 200
    DVADEHRLLV DRTREATMRA INTVKPGRAL SVIGRVIESY ANRFGYNVVR
    210 220 230 240 250
    DFTGHGIGTT FHNGLVVLHY DQPAVETIMQ PGMTFTIEPM INLGALDYEI
    260 270 280
    WDDGWTVVTK DRKWTAQFEH TLLVTDTGVE ILTCL
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP45662.1.
    PIRiG70885.
    RefSeqiWP_003899513.1. NZ_KK339370.1.
    YP_177911.1. NC_000962.3.

    Genome annotation databases

    EnsemblBacteriaiCCP45662; CCP45662; Rv2861c.
    GeneIDi888596.
    KEGGimtu:Rv2861c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP45662.1.
    PIRiG70885.
    RefSeqiWP_003899513.1. NZ_KK339370.1.
    YP_177911.1. NC_000962.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    4OOKX-ray1.90A1-283[»]
    ProteinModelPortaliP9WK19.
    SMRiP9WK19.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv2861c.

    Proteomic databases

    PaxDbiP9WK19.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCCP45662; CCP45662; Rv2861c.
    GeneIDi888596.
    KEGGimtu:Rv2861c.

    Organism-specific databases

    TubercuListiRv2861c.

    Phylogenomic databases

    eggNOGiENOG4105CA1. Bacteria.
    COG0024. LUCA.
    KOiK01265.
    OMAiVIKDEYH.
    PhylomeDBiP9WK19.

    Enzyme and pathway databases

    BioCyciMTBH37RV:G185E-7112-MONOMER.

    Miscellaneous databases

    PROiP9WK19.

    Family and domain databases

    CDDicd01086. MetAP1. 1 hit.
    Gene3Di3.90.230.10. 1 hit.
    HAMAPiMF_01974. MetAP_1. 1 hit.
    InterProiIPR000994. Pept_M24.
    IPR001714. Pept_M24_MAP.
    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]
    ProtoNetiSearch...

    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: November 30, 2016
    This is version 22 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

    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.