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P53579

- MAP11_SYNY3

UniProt

P53579 - MAP11_SYNY3

Protein

Methionine aminopeptidase A

Gene

slr0918

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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 sitei80 – 801SubstrateUniRule annotation
    Metal bindingi98 – 981Divalent metal cation 1UniRule annotation
    Metal bindingi109 – 1091Divalent metal cation 1UniRule annotation
    Metal bindingi109 – 1091Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi172 – 1721Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei179 – 1791SubstrateUniRule annotation
    Metal bindingi205 – 2051Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi236 – 2361Divalent metal cation 1UniRule annotation
    Metal bindingi236 – 2361Divalent 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

    Protein family/group databases

    MEROPSiM24.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase AUniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP AUniRule annotation
    Short name:
    MetAP AUniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Ordered Locus Names:slr0918
    OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
    Taxonomic identifieri1111708 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
    ProteomesiUP000001425: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 253253Methionine aminopeptidase APRO_0000148963Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi1148.slr0918.

    Structurei

    3D structure databases

    ProteinModelPortaliP53579.
    SMRiP53579. Positions 4-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030426.
    KOiK01265.
    OMAiVEASYDV.
    OrthoDBiEOG6MWNDS.
    PhylomeDBiP53579.

    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.

    P53579-1 [UniParc]FASTAAdd to Basket

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    MGDTITLLSR REIEKMRQAG QLAAALLDHL APMVQPGITT LELNDEAEKW    50
    TKAHGAISAP LGYNGFPKSI CTSINEVICH GIPHRKRVLQ AGDIINVDVT 100
    PIVDGYHGDC SRTFFVGTPS PVAEKLVKVT EECLRLGIEA VKPGGKIGDI 150
    GAAIQSHAEA QGFSVVRDFV GHGISKIFHT APQIPHYGKA GKGKRLRPGM 200
    VFTIEPMINE GTWEAVLLDD GWTAITKDGK LSAQFEHTIA VTEDGVEILT 250
    LGE 253
    Length:253
    Mass (Da):27,235
    Last modified:October 1, 1996 - v1
    Checksum:iBABEA87651501D72
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000022 Genomic DNA. Translation: BAA10466.1.
    PIRiS75731.
    RefSeqiNP_442396.1. NC_000911.1.
    YP_005652456.1. NC_017277.1.
    YP_007452272.1. NC_020286.1.

    Genome annotation databases

    EnsemblBacteriaiBAA10466; BAA10466; BAA10466.
    GeneIDi954962.
    KEGGisyn:slr0918.
    syy:SYNGTS_2503.
    syz:MYO_125280.
    PATRICi23842480. VBISynSp132158_2780.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000022 Genomic DNA. Translation: BAA10466.1 .
    PIRi S75731.
    RefSeqi NP_442396.1. NC_000911.1.
    YP_005652456.1. NC_017277.1.
    YP_007452272.1. NC_020286.1.

    3D structure databases

    ProteinModelPortali P53579.
    SMRi P53579. Positions 4-252.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 1148.slr0918.

    Protein family/group databases

    MEROPSi M24.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAA10466 ; BAA10466 ; BAA10466 .
    GeneIDi 954962.
    KEGGi syn:slr0918.
    syy:SYNGTS_2503.
    syz:MYO_125280.
    PATRICi 23842480. VBISynSp132158_2780.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030426.
    KOi K01265.
    OMAi VEASYDV.
    OrthoDBi EOG6MWNDS.
    PhylomeDBi P53579.

    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 the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
      Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
      DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27184 / PCC 6803 / N-1.
    2. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
      Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
      , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PCC 6803 / Kazusa.

    Entry informationi

    Entry nameiMAP11_SYNY3
    AccessioniPrimary (citable) accession number: P53579
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 101 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
    3. Synechocystis PCC 6803
      Synechocystis (strain PCC 6803): entries and gene names

    External Data

    Dasty 3