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Q9Z9J4

- MAP1_BACHD

UniProt

Q9Z9J4 - MAP1_BACHD

Protein

Methionine aminopeptidase

Gene

map

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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.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 bindingi94 – 941Divalent metal cation 1UniRule annotation
    Metal bindingi105 – 1051Divalent metal cation 1UniRule annotation
    Metal bindingi105 – 1051Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi168 – 1681Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei175 – 1751SubstrateUniRule annotation
    Metal bindingi201 – 2011Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi232 – 2321Divalent metal cation 1UniRule annotation
    Metal bindingi232 – 2321Divalent 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

    Enzyme and pathway databases

    BioCyciBHAL272558:GJC5-181-MONOMER.

    Protein family/group databases

    MEROPSiM24.001.

    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:BH0156
    OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
    Taxonomic identifieri272558 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001258: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 248248Methionine aminopeptidasePRO_0000148925Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272558.BH0156.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z9J4.
    SMRiQ9Z9J4. Positions 1-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030426.
    KOiK01265.
    OMAiNIIQTHA.
    OrthoDBiEOG6MWNDS.

    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.

    Q9Z9J4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIICKTEREL EIMREAGRIV ALTHQEIKLH IQPGITTKKL DEIAETFIRS    50
    HGATPSFKGY NGFTGSICAS VNEELVHGIP GNRVLKEGDI ISVDIGAKYN 100
    GYHGDSAWTY AVGNISDEDQ DLLDVTETSL YKGLEQAKAG ARLSDISHAI 150
    QSYAEPRGYA IVREYVGHGV GQNLHEDPQI PHYGPPGKGP RLKPGMVLAI 200
    EPMVNAGSRY VRTLSDNWTV VTVDGKKCAH FEHTIAITET GYEILTKA 248
    Length:248
    Mass (Da):27,155
    Last modified:May 1, 1999 - v1
    Checksum:iC2295A5147447327
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017508 Genomic DNA. Translation: BAA75293.1.
    BA000004 Genomic DNA. Translation: BAB03875.1.
    PIRiT44405.
    RefSeqiNP_241022.1. NC_002570.2.
    WP_010896339.1. NC_002570.2.

    Genome annotation databases

    EnsemblBacteriaiBAB03875; BAB03875; BAB03875.
    GeneIDi893603.
    KEGGibha:BH0156.
    PATRICi18937186. VBIBacHal18977_0165.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017508 Genomic DNA. Translation: BAA75293.1 .
    BA000004 Genomic DNA. Translation: BAB03875.1 .
    PIRi T44405.
    RefSeqi NP_241022.1. NC_002570.2.
    WP_010896339.1. NC_002570.2.

    3D structure databases

    ProteinModelPortali Q9Z9J4.
    SMRi Q9Z9J4. Positions 1-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272558.BH0156.

    Protein family/group databases

    MEROPSi M24.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB03875 ; BAB03875 ; BAB03875 .
    GeneIDi 893603.
    KEGGi bha:BH0156.
    PATRICi 18937186. VBIBacHal18977_0165.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030426.
    KOi K01265.
    OMAi NIIQTHA.
    OrthoDBi EOG6MWNDS.

    Enzyme and pathway databases

    BioCyci BHAL272558:GJC5-181-MONOMER.

    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. "Sequence analysis of a 32-kb region including the major ribosomal protein gene clusters from alkaliphilic Bacillus sp. strain C-125."
      Takami H., Takaki Y., Nakasone K., Hirama C., Inoue A., Horikoshi K.
      Biosci. Biotechnol. Biochem. 63:452-455(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
    2. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
      Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
      Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

    Entry informationi

    Entry nameiMAP1_BACHD
    AccessioniPrimary (citable) accession number: Q9Z9J4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 105 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