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Protein

Catalase-peroxidase 2

Gene

katG2

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May play a role in the intracellular survival of mycobacteria.

Catalytic activityi

Donor + H2O2 = oxidized donor + 2 H2O.UniRule annotation
2 H2O2 = O2 + 2 H2O.UniRule annotation

Cofactori

heme bNote: Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer.

Kineticsi

  1. KM=1.4 mM for H2O2 for the catalase reaction1 Publication
  2. KM=0.19 mM for o-dianisidine for the peroxidase reaction1 Publication
  3. KM=0.17 mM for NADPH for the peroxidase reaction1 Publication
  4. KM=0.23 mM for NADH for the peroxidase reaction1 Publication
  5. KM=0.31 mM for pyrogallol for the peroxidase reaction1 Publication
  6. KM=0.11 mM for 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) for the peroxidase reaction1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei110 – 1101Transition state stabilizerUniRule annotation
    Active sitei114 – 1141Proton acceptorUniRule annotation
    Metal bindingi279 – 2791Iron (heme axial ligand)UniRule annotation

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMSME246196:GJ4Y-3461-MONOMER.

    Protein family/group databases

    PeroxiBasei3570. MsmCP02_mc2155.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catalase-peroxidase 2UniRule annotation (EC:1.11.1.21UniRule annotation)
    Short name:
    CP 2UniRule annotation
    Alternative name(s):
    Peroxidase/catalase 2UniRule annotation
    Gene namesi
    Name:katG2UniRule annotation
    Synonyms:katH
    Ordered Locus Names:MSMEG_3461, MSMEI_3380
    OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
    Taxonomic identifieri246196 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
    Proteomesi
    • UP000006158 Componenti: Chromosome
    • UP000000757 Componenti: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    Defects cause isoniazid (INH) resistance.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved2 Publications
    Chaini2 – 748747Catalase-peroxidase 2PRO_0000345094Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki113 ↔ 238Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-264)UniRule annotation
    Cross-linki238 ↔ 264Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-113)UniRule annotation

    Post-translational modificationi

    The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme.UniRule annotation

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi246196.MSMEG_3461.

    Structurei

    3D structure databases

    ProteinModelPortaliA0QXX7.
    SMRiA0QXX7. Positions 41-748.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peroxidase family. Peroxidase/catalase subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105C1X. Bacteria.
    COG0376. LUCA.
    HOGENOMiHOG000218110.
    KOiK03782.
    OMAiVVWTPTP.
    OrthoDBiEOG6RRKKM.

    Family and domain databases

    HAMAPiMF_01961. Catal_peroxid.
    InterProiIPR000763. Catalase_peroxidase.
    IPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view]
    PfamiPF00141. peroxidase. 2 hits.
    [Graphical view]
    PRINTSiPR00460. BPEROXIDASE.
    PR00458. PEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 2 hits.
    TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
    PROSITEiPS00435. PEROXIDASE_1. 1 hit.
    PS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A0QXX7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSDTSDSRP PNPDTKTAST SESENPAIPS PKPKSGAPLR NQDWWPNQID
    60 70 80 90 100
    VSRLHPHPPQ GNPLGEDFDY AEEFAKLDVN ALKADLTALM TQSQDWWPAD
    110 120 130 140 150
    YGHYGGLFIR MSWHSAGTYR IHDGRGGGGQ GAQRFAPINS WPDNVSLDKA
    160 170 180 190 200
    RRLLWPIKQK YGNKISWADL LVFTGNVALE SMGFKTFGFG FGREDIWEPE
    210 220 230 240 250
    EILFGEEDEW LGTDKRYGGG EQRQLAEPYG ATTMGLIYVN PEGPEGQPDP
    260 270 280 290 300
    LAAAHDIRET FGRMAMNDEE TAALIVGGHT FGKTHGAGDA SLVGPEPEAA
    310 320 330 340 350
    PIEQQGLGWK SSYGTGKGPD TITSGLEVVW TNTPTKWDNS FLEILYGYEW
    360 370 380 390 400
    ELTKSPAGAW QFTAKDGAGA GTIPDPFGGP GRNPTMLVTD ISMRVDPIYG
    410 420 430 440 450
    KITRRWLDHP EELSEAFAKA WYKLLHRDMG PISRYLGPWV AEPQLWQDPV
    460 470 480 490 500
    PAVDHPLVDD QDIAALKSTV LDSGLSTGQL IKTAWASAAS YRNTDKRGGA
    510 520 530 540 550
    NGARVRLEPQ KNWDVNEPAE LATVLPVLER IQQDFNASAS GGKKVSLADL
    560 570 580 590 600
    IVLAGSAAIE KAAKDGGYNV TVPFAPGRTD ASQENTDVES FAVLEPRADG
    610 620 630 640 650
    FRNYVRPGEK VQLEKMLLER AYFLGVTAPQ LTALVGGLRA LDVNHGGTKH
    660 670 680 690 700
    GVFTDRPGAL TNDFFVNLLD MGTEWKTSET TENVYEGVDR KTGQLKWTAT
    710 720 730 740
    ANDLVFGSHS VLRAVAEVYA QSDNGERFVN DFVKAWVKVM NNDRFDLK
    Length:748
    Mass (Da):81,998
    Last modified:January 9, 2007 - v1
    Checksum:i73E44205C96B2FD3
    GO

    Mass spectrometryi

    Molecular mass is 81889 Da from positions 2 - 748. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ311851 Genomic DNA. Translation: CAC44462.1.
    CP000480 Genomic DNA. Translation: ABK73887.1.
    CP001663 Genomic DNA. Translation: AFP39843.1.
    RefSeqiWP_011729086.1. NZ_CP009494.1.
    YP_887765.1. NC_008596.1.

    Genome annotation databases

    EnsemblBacteriaiABK73887; ABK73887; MSMEG_3461.
    AFP39843; AFP39843; MSMEI_3380.
    GeneIDi4536428.
    KEGGimsb:LJ00_17220.
    msg:MSMEI_3380.
    msm:MSMEG_3461.
    PATRICi18079343. VBIMycSme59918_3418.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ311851 Genomic DNA. Translation: CAC44462.1.
    CP000480 Genomic DNA. Translation: ABK73887.1.
    CP001663 Genomic DNA. Translation: AFP39843.1.
    RefSeqiWP_011729086.1. NZ_CP009494.1.
    YP_887765.1. NC_008596.1.

    3D structure databases

    ProteinModelPortaliA0QXX7.
    SMRiA0QXX7. Positions 41-748.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi246196.MSMEG_3461.

    Protein family/group databases

    PeroxiBasei3570. MsmCP02_mc2155.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABK73887; ABK73887; MSMEG_3461.
    AFP39843; AFP39843; MSMEI_3380.
    GeneIDi4536428.
    KEGGimsb:LJ00_17220.
    msg:MSMEI_3380.
    msm:MSMEG_3461.
    PATRICi18079343. VBIMycSme59918_3418.

    Phylogenomic databases

    eggNOGiENOG4105C1X. Bacteria.
    COG0376. LUCA.
    HOGENOMiHOG000218110.
    KOiK03782.
    OMAiVVWTPTP.
    OrthoDBiEOG6RRKKM.

    Enzyme and pathway databases

    BioCyciMSME246196:GJ4Y-3461-MONOMER.

    Family and domain databases

    HAMAPiMF_01961. Catal_peroxid.
    InterProiIPR000763. Catalase_peroxidase.
    IPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view]
    PfamiPF00141. peroxidase. 2 hits.
    [Graphical view]
    PRINTSiPR00460. BPEROXIDASE.
    PR00458. PEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 2 hits.
    TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
    PROSITEiPS00435. PEROXIDASE_1. 1 hit.
    PS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The catalase-peroxidase of Mycobacterium smegmatis."
      Honore N.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
      Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    3. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
      Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
      Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    4. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
      Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
      Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE.
      Strain: ATCC 700084 / mc(2)155.
    5. "Purification and characterization of the Mycobacterium smegmatis catalase-peroxidase involved in isoniazid activation."
      Marcinkeviciene J.A., Magliozzo R.S., Blanchard J.S.
      J. Biol. Chem. 270:22290-22295(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-20, BIOPHYSICOCHEMICAL PROPERTIES, HEME-BINDING, SUBUNIT, MASS SPECTROMETRY, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiKATG2_MYCS2
    AccessioniPrimary (citable) accession number: A0QXX7
    Secondary accession number(s): I7FMA5, Q93JZ3, Q9R4J9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 22, 2008
    Last sequence update: January 9, 2007
    Last modified: November 11, 2015
    This is version 69 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    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 one 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.