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P60355

- MCAT_LACPN

UniProt

P60355 - MCAT_LACPN

Protein

Manganese catalase

Gene
N/A
Organism
Lactobacillus plantarum
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (16 Feb 2004)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    2 H2O2 = O2 + 2 H2O.

    Cofactori

    Binds 1 calcium ion per subunit.
    Binds 2 manganese ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi35 – 351Manganese 1
    Metal bindingi57 – 571Calcium
    Metal bindingi61 – 611Calcium
    Metal bindingi66 – 661Manganese 1
    Metal bindingi66 – 661Manganese 2
    Metal bindingi69 – 691Manganese 1
    Metal bindingi148 – 1481Manganese 2
    Metal bindingi181 – 1811Manganese 2
    Metal bindingi218 – 2181Calcium
    Metal bindingi220 – 2201Calcium; via carbonyl oxygen
    Metal bindingi222 – 2221Calcium; via carbonyl oxygen

    GO - Molecular functioni

    1. catalase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Ligandi

    Calcium, Manganese, Metal-binding

    Protein family/group databases

    PeroxiBasei3978. LplMnCat01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Manganese catalase (EC:1.11.1.6)
    Alternative name(s):
    Pseudocatalase
    OrganismiLactobacillus plantarum
    Taxonomic identifieri1590 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi42 – 421Y → F: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 266266Manganese catalasePRO_0000096155Add
    BLAST

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Structurei

    Secondary structure

    1
    266
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 43
    Helixi19 – 3012
    Helixi35 – 4814
    Helixi53 – 8028
    Turni81 – 833
    Helixi88 – 936
    Helixi97 – 1037
    Helixi106 – 1105
    Beta strandi113 – 1153
    Helixi128 – 1303
    Helixi137 – 15923
    Helixi165 – 19632
    Beta strandi198 – 2014
    Turni205 – 2073
    Helixi210 – 2123
    Beta strandi215 – 2173
    Helixi224 – 2285
    Beta strandi240 – 2445
    Helixi259 – 2613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JKUX-ray1.84A/B/C/D/E/F1-266[»]
    1JKVX-ray1.39A/B/C/D/E/F1-266[»]
    1O9IX-ray1.33A/B/C/D/E/F1-266[»]
    ProteinModelPortaliP60355.
    SMRiP60355. Positions 1-266.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60355.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the manganese catalase family.Curated

    Family and domain databases

    Gene3Di1.20.1260.10. 1 hit.
    3.30.1530.10. 1 hit.
    InterProiIPR009078. Ferritin-like_SF.
    IPR012347. Ferritin-rel.
    IPR007760. Mn_catalase.
    IPR027407. Mn_catalase_dom2.
    [Graphical view]
    PfamiPF05067. Mn_catalase. 1 hit.
    [Graphical view]
    SUPFAMiSSF47240. SSF47240. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P60355-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFKHTRKLQY NAKPDRSDPI MARRLQESLG GQWGETTGMM SYLSQGWAST    50
    GAEKYKDLLL DTGTEEMAHV EMISTMIGYL LEDAPFGPED LKRDPSLATT 100
    MAGMDPEHSL VHGLNASLNN PNGAAWNAGY VTSSGNLVAD MRFNVVRESE 150
    ARLQVSRLYS MTEDEGVRDM LKFLLARETQ HQLQFMKAQE ELEEKYGIIV 200
    PGDMKEIEHS EFSHVLMNFS DGDGSKAFEG QVAKDGEKFT YQENPEAMGG 250
    IPHIKPGDPR LHNHQG 266
    Length:266
    Mass (Da):29,743
    Last modified:February 16, 2004 - v1
    Checksum:i2943A15DD7A60CB1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87070 Genomic DNA. Translation: BAA13239.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87070 Genomic DNA. Translation: BAA13239.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JKU X-ray 1.84 A/B/C/D/E/F 1-266 [» ]
    1JKV X-ray 1.39 A/B/C/D/E/F 1-266 [» ]
    1O9I X-ray 1.33 A/B/C/D/E/F 1-266 [» ]
    ProteinModelPortali P60355.
    SMRi P60355. Positions 1-266.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    PeroxiBasei 3978. LplMnCat01.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P60355.

    Family and domain databases

    Gene3Di 1.20.1260.10. 1 hit.
    3.30.1530.10. 1 hit.
    InterProi IPR009078. Ferritin-like_SF.
    IPR012347. Ferritin-rel.
    IPR007760. Mn_catalase.
    IPR027407. Mn_catalase_dom2.
    [Graphical view ]
    Pfami PF05067. Mn_catalase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47240. SSF47240. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of manganese catalase from Lactobacillus plantarum."
      Igarashi T., Kono Y., Tanaka K.
      J. Biol. Chem. 271:29521-29524(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-32 AND 67-86.
      Strain: ATCC 14431 / T-1043-5.
    2. Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS), SUBUNIT.
    3. "Outer sphere mutagenesis of Lactobacillus plantarum manganese catalase disrupts the cluster core. Mechanistic implications."
      Whittaker M.M., Barynin V.V., Igarashi T., Whittaker J.W.
      Eur. J. Biochem. 270:1102-1116(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS), MUTAGENESIS OF TYR-42.

    Entry informationi

    Entry nameiMCAT_LACPN
    AccessioniPrimary (citable) accession number: P60355
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: February 16, 2004
    Last modified: October 1, 2014
    This is version 55 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, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3