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Protein

Catalase-related peroxidase

Gene

MAP_2744c

Organism
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has an organic peroxide-dependent peroxidase activity. Exhibits strong peroxidase activity using organic hydroperoxides as cosubstrates, weak peroxidase activity using hydrogen peroxide and negligible catalase activity. May have a role in elimination of reactive oxygen species, in particular by deactivating hydroperoxides.1 Publication

Cofactori

heme2 Publications

Kineticsi

Kcat is 13 sec(-1) for H2O2. Kcat is 320 sec(-1) for t-butyl hydroperoxide. Kcat is 330 sec(-1) for cumene hydroperoxide. Kcat is 529 sec(-1) for 9S-HPODE.1 Publication

  1. KM=30 mM for H2O2 in 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS) oxidation assay (at pH 7.0)1 Publication
  2. KM=22 mM for t-butyl hydroperoxide in ABTS oxidation assay (at pH 7.0)1 Publication
  3. KM=3 mM for cumene hydroperoxide in ABTS oxidation assay (at pH 7.0)1 Publication
  4. KM=49 µM for 9S-hydroperoxy-octadecadienoic acid (9S-HPODE) used as a cosubstrate with ABTS (at pH 7.0)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei28 – 281By similarity
    Metal bindingi294 – 2941Iron (heme axial ligand)

    GO - Molecular functioni

    • catalase activity Source: InterPro
    • heme binding Source: UniProtKB
    • iron ion binding Source: UniProtKB
    • peroxidase activity Source: UniProtKB

    GO - Biological processi

    • hydrogen peroxide metabolic process Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    • regulation of reactive oxygen species metabolic process Source: UniProtKB
    • response to oxidative stress Source: InterPro
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMAVI262316:GCQR-2780-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catalase-related peroxidase1 Publication (EC:1.11.1.-1 Publication)
    Gene namesi
    Ordered Locus Names:MAP_2744c
    OrganismiMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
    Taxonomic identifieri262316 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)
    ProteomesiUP000000580 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 313313Catalase-related peroxidasePRO_0000424152Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi262316.MAP2744c.

    Structurei

    Secondary structure

    1
    313
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 1610Combined sources
    Beta strandi26 – 283Combined sources
    Beta strandi30 – 4011Combined sources
    Helixi44 – 463Combined sources
    Helixi51 – 533Combined sources
    Beta strandi57 – 6913Combined sources
    Beta strandi81 – 888Combined sources
    Beta strandi94 – 1018Combined sources
    Helixi110 – 11910Combined sources
    Beta strandi121 – 1233Combined sources
    Helixi126 – 13611Combined sources
    Helixi138 – 1414Combined sources
    Helixi144 – 1507Combined sources
    Beta strandi153 – 1553Combined sources
    Helixi157 – 1593Combined sources
    Beta strandi162 – 17110Combined sources
    Beta strandi177 – 18812Combined sources
    Helixi195 – 1995Combined sources
    Helixi205 – 21612Combined sources
    Beta strandi219 – 2279Combined sources
    Beta strandi246 – 25712Combined sources
    Beta strandi260 – 2634Combined sources
    Beta strandi279 – 2813Combined sources
    Helixi285 – 30218Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3E4WX-ray1.80A/B1-313[»]
    3E4YX-ray2.60A1-313[»]
    ProteinModelPortaliQ73WB6.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ73WB6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the catalase family.Sequence Analysis

    Phylogenomic databases

    KOiK03781.
    OMAiKRTPFRY.
    OrthoDBiEOG6742T3.

    Family and domain databases

    Gene3Di2.40.180.10. 1 hit.
    InterProiIPR018028. Catalase.
    IPR020835. Catalase-like_dom.
    IPR011614. Catalase_core.
    IPR024168. Catalase_SrpA-type_pred.
    [Graphical view]
    PANTHERiPTHR11465. PTHR11465. 1 hit.
    PfamiPF00199. Catalase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000296. SrpA. 1 hit.
    PRINTSiPR00067. CATALASE.
    SMARTiSM01060. Catalase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56634. SSF56634. 1 hit.
    PROSITEiPS51402. CATALASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q73WB6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSGGLTPDQA IDAIRGTGGA QPGCRALHAK GTLYRGTFTA TRDAVMLSAA
    60 70 80 90 100
    PHLDGSTVPA LIRFSNGSGN PKQRDGAPGV RGMAVKFTLP DGSTTDVSAQ
    110 120 130 140 150
    TARLLVSSTP EGFIDLLKAM RPGLTTPLRL ATHLLTHPRL LGALPLLREA
    160 170 180 190 200
    NRIPASYATT EYHGLHAFRW IAADGSARFV RYHLVPTAAE EYLSASDARG
    210 220 230 240 250
    KDPDFLTDEL AARLQDGPVR FDFRVQIAGP TDSTVDPSSA WQSTQIVTVG
    260 270 280 290 300
    TVTITGPDTE REHGGDIVVF DPMRVTDGIE PSDDPVLRFR TLVYSASVKL
    310
    RTGVDRGAQA PPV
    Length:313
    Mass (Da):33,321
    Last modified:July 5, 2004 - v1
    Checksum:i7EE2BE95125CD14E
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE016958 Genomic DNA. Translation: AAS05061.1.
    RefSeqiWP_003875322.1. NC_002944.2.

    Genome annotation databases

    EnsemblBacteriaiAAS05061; AAS05061; MAP_2744c.
    GeneIDi2720786.
    KEGGimpa:MAP2744c.
    PATRICi17998202. VBIMycAvi108102_2915.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE016958 Genomic DNA. Translation: AAS05061.1.
    RefSeqiWP_003875322.1. NC_002944.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3E4WX-ray1.80A/B1-313[»]
    3E4YX-ray2.60A1-313[»]
    ProteinModelPortaliQ73WB6.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi262316.MAP2744c.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAS05061; AAS05061; MAP_2744c.
    GeneIDi2720786.
    KEGGimpa:MAP2744c.
    PATRICi17998202. VBIMycAvi108102_2915.

    Phylogenomic databases

    KOiK03781.
    OMAiKRTPFRY.
    OrthoDBiEOG6742T3.

    Enzyme and pathway databases

    BioCyciMAVI262316:GCQR-2780-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiQ73WB6.

    Family and domain databases

    Gene3Di2.40.180.10. 1 hit.
    InterProiIPR018028. Catalase.
    IPR020835. Catalase-like_dom.
    IPR011614. Catalase_core.
    IPR024168. Catalase_SrpA-type_pred.
    [Graphical view]
    PANTHERiPTHR11465. PTHR11465. 1 hit.
    PfamiPF00199. Catalase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000296. SrpA. 1 hit.
    PRINTSiPR00067. CATALASE.
    SMARTiSM01060. Catalase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56634. SSF56634. 1 hit.
    PROSITEiPS51402. CATALASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
      Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
      Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-968 / K-10.
    2. "Coordination modes of tyrosinate-ligated catalase-type heme enzymes: magnetic circular dichroism studies of Plexaura homomalla allene oxide synthase, Mycobacterium avium ssp. paratuberculosis protein-2744c, and bovine liver catalase in their ferric and ferrous states."
      Bandara D.M., Sono M., Bruce G.S., Brash A.R., Dawson J.H.
      J. Inorg. Biochem. 105:1786-1794(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: MAGNETIC CIRCULAR DICHROISM, COFACTOR.
    3. "The structure and peroxidase activity of a 33-kDa catalase-related protein from Mycobacterium avium ssp. paratuberculosis."
      Pakhomova S., Gao B., Boeglin W.E., Brash A.R., Newcomer M.E.
      Protein Sci. 18:2559-2568(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiCRPE_MYCPA
    AccessioniPrimary (citable) accession number: Q73WB6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 16, 2013
    Last sequence update: July 5, 2004
    Last modified: July 22, 2015
    This is version 74 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, Complete proteome, Reference proteome

    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

    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.