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Protein

Methionine aminopeptidase 1

Gene

map-1

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 annotation1 Publication

Catalytic activityi

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

Cofactori

Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: 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 various metalloform-selective inhibitors.1 Publication

Kineticsi

  1. KM=18 µM for Met-Ala-Ser (at pH 7.5 and at 37 degrees Celsius)2 Publications
  2. KM=328 µM for Met-Gly-Met-Met (at pH 7.5 and at 37 degrees Celsius)2 Publications

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius. It retained half of its activity after 10 min of incubation at 55 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei88 – 881SubstrateUniRule annotation
    Metal bindingi106 – 1061Divalent metal cation 1UniRule annotation
    Metal bindingi117 – 1171Divalent metal cation 1UniRule annotation
    Metal bindingi117 – 1171Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi186 – 1861Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei193 – 1931SubstrateUniRule annotation
    Metal bindingi219 – 2191Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi250 – 2501Divalent metal cation 1UniRule annotation
    Metal bindingi250 – 2501Divalent metal cation 2; catalyticUniRule annotation

    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 1UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 1UniRule annotation
    Short name:
    MetAP 1UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Name:map-1UniRule annotation
    Synonyms:mapA
    Ordered Locus Names:Rv0734
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001584 Componenti: Chromosome

    Organism-specific databases

    TubercuListiRv0734.

    Subcellular locationi

    GO - Cellular componenti

    • plasma membrane Source: MTBBASE
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 266266Methionine aminopeptidase 1PRO_0000414588Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi83332.Rv0734.

    Structurei

    3D structure databases

    ProteinModelPortaliP9WK21.
    SMRiP9WK21. Positions 10-265.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01265.
    OMAiEESMWAG.
    PhylomeDBiP9WK21.

    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.

    Sequencei

    Sequence statusi: Complete.

    P9WK21-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRPLARLRGR RVVPQRSAGE LDAMAAAGAV VAAALRAIRA AAAPGTSSLS
    60 70 80 90 100
    LDEIAESVIR ESGATPSFLG YHGYPASICA SINDRVVHGI PSTAEVLAPG
    110 120 130 140 150
    DLVSIDCGAV LDGWHGDAAI TFGVGALSDA DEALSEATRE SLQAGIAAMV
    160 170 180 190 200
    VGNRLTDVAH AIETGTRAAE LRYGRSFGIV AGYGGHGIGR QMHMDPFLPN
    210 220 230 240 250
    EGAPGRGPLL AAGSVLAIEP MLTLGTTKTV VLDDKWTVTT ADGSRAAHWE
    260
    HTVAVTDDGP RILTLG
    Length:266
    Mass (Da):27,277
    Last modified:April 16, 2014 - v1
    Checksum:iA187BD61E62449E1
    GO

    Mass spectrometryi

    Molecular mass is 28812 Da from positions 1 - 266. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP43479.1.
    RefSeqiWP_003403728.1. NZ_KK339370.1.
    YP_177748.1. NC_000962.3.

    Genome annotation databases

    EnsemblBacteriaiCCP43479; CCP43479; Rv0734.
    GeneIDi888564.
    KEGGimtu:Rv0734.
    mtv:RVBD_0734.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP43479.1.
    RefSeqiWP_003403728.1. NZ_KK339370.1.
    YP_177748.1. NC_000962.3.

    3D structure databases

    ProteinModelPortaliP9WK21.
    SMRiP9WK21. Positions 10-265.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv0734.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCCP43479; CCP43479; Rv0734.
    GeneIDi888564.
    KEGGimtu:Rv0734.
    mtv:RVBD_0734.

    Organism-specific databases

    TubercuListiRv0734.

    Phylogenomic databases

    KOiK01265.
    OMAiEESMWAG.
    PhylomeDBiP9WK21.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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. "Expression and characterization of Mycobacterium tuberculosis methionine aminopeptidase type 1a."
      Lu J.P., Ye Q.Z.
      Bioorg. Med. Chem. Lett. 20:2776-2779(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 25618 / H37Rv.

    Entry informationi

    Entry nameiMAP11_MYCTU
    AccessioniPrimary (citable) accession number: P9WK21
    Secondary accession number(s): L0T6B7, Q79FX0, Q7D9D5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: July 22, 2015
    This is version 14 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

    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. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.