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P69000

- MAP1_CLOAB

UniProt

P69000 - MAP1_CLOAB

Protein

Methionine aminopeptidase

Gene

map

Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (01 Feb 2005)
      Previous versions | rss
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    • Comment

    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 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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei77 – 771SubstrateUniRule annotation
    Metal bindingi95 – 951Divalent metal cation 1UniRule annotation
    Metal bindingi106 – 1061Divalent metal cation 1UniRule annotation
    Metal bindingi106 – 1061Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi169 – 1691Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei176 – 1761SubstrateUniRule annotation
    Metal bindingi202 – 2021Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi233 – 2331Divalent metal cation 1UniRule annotation
    Metal bindingi233 – 2331Divalent metal cation 2; catalyticUniRule annotation

    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 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:CA_C3111
    OrganismiClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
    Taxonomic identifieri272562 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000000814: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 250250Methionine aminopeptidasePRO_0000148935Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP69000.
    SMRiP69000. Positions 1-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    OMAiNYGKPGR.

    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.

    P69000-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIIIKNDTEI EYMRQAGKIV GETLNMLEKA AKPGVTTADL DRLAEDFIKK    50
    YNAIPSFKGY GGFPASICTS INEEVIHGIP SKHRVLHEGD IISVDCGAIL 100
    NGYQGDAART FAIGEISEEA AKLIKVTKES FFKGVEKAVI GNRLTDISHS 150
    IQEYVESFGY GVVRDYVGHG IGKEMHEDPE VPNYGRPGRG PKLVHGMVLA 200
    IEPMVDVGTY MVKTQSNDWT VVTQDGSLAA HYENTVAILD NGPEILTLCE 250
    Length:250
    Mass (Da):27,301
    Last modified:February 1, 2005 - v1
    Checksum:iFE811B9E55B0584B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001437 Genomic DNA. No translation available.
    RefSeqiYP_008920787.1. NC_003030.1.

    Genome annotation databases

    GeneIDi1119294.
    KEGGicac:CA_C3111.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001437 Genomic DNA. No translation available.
    RefSeqi YP_008920787.1. NC_003030.1.

    3D structure databases

    ProteinModelPortali P69000.
    SMRi P69000. Positions 1-248.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1119294.
    KEGGi cac:CA_C3111.

    Phylogenomic databases

    OMAi NYGKPGR.

    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 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
    2. "Improving genome annotations using phylogenetic profile anomaly detection."
      Mikkelsen T.S., Galagan J.E., Mesirov J.P.
      Bioinformatics 21:464-470(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiMAP1_CLOAB
    AccessioniPrimary (citable) accession number: P69000
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 65 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3