Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Catalase-peroxidase

Gene

katG

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
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.

Catalytic activityi

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

Cofactori

heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.

Kineticsi

  1. KM=4.2 mM for H2O2 for catalase activity1 Publication

    pH dependencei

    Optimum pH is 6.5 for catalase activity. Active from pH 4.5 to 8.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei91 – 911Transition state stabilizerUniRule annotation
    Active sitei95 – 951Proton acceptor
    Metal bindingi263 – 2631Iron (heme axial ligand)

    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

    BioCyciSYNEL:SYNPCC7942_1656-MONOMER.
    BRENDAi1.11.1.21. 7781.

    Protein family/group databases

    PeroxiBasei2426. SeCP01_PCC7942.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catalase-peroxidaseUniRule annotation (EC:1.11.1.21UniRule annotation)
    Short name:
    CPUniRule annotation
    Alternative name(s):
    Peroxidase/catalaseUniRule annotation
    Gene namesi
    Name:katGUniRule annotation
    Ordered Locus Names:Synpcc7942_1656
    OrganismiSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
    Taxonomic identifieri1140 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
    Proteomesi
    • UP000002717 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 720719Catalase-peroxidasePRO_0000345095Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki94 ↔ 222Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-248)
    Cross-linki222 ↔ 248Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-94)

    Post-translational modificationi

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

    Proteomic databases

    PRIDEiQ31MN3.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    STRINGi1140.Synpcc7942_1656.

    Structurei

    Secondary structure

    1
    720
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 254Combined sources
    Helixi32 – 354Combined sources
    Turni40 – 423Combined sources
    Helixi51 – 555Combined sources
    Helixi60 – 7112Combined sources
    Helixi81 – 833Combined sources
    Helixi86 – 9712Combined sources
    Turni102 – 1043Combined sources
    Helixi109 – 1113Combined sources
    Helixi113 – 1153Combined sources
    Helixi119 – 1213Combined sources
    Helixi123 – 1253Combined sources
    Helixi128 – 1347Combined sources
    Helixi136 – 1427Combined sources
    Helixi143 – 1453Combined sources
    Helixi148 – 16316Combined sources
    Beta strandi190 – 1934Combined sources
    Beta strandi196 – 1983Combined sources
    Beta strandi202 – 2043Combined sources
    Turni205 – 2073Combined sources
    Beta strandi215 – 2173Combined sources
    Beta strandi221 – 2233Combined sources
    Helixi234 – 24714Combined sources
    Helixi252 – 26312Combined sources
    Helixi274 – 2763Combined sources
    Helixi281 – 2833Combined sources
    Helixi286 – 2883Combined sources
    Beta strandi295 – 2984Combined sources
    Helixi302 – 3043Combined sources
    Beta strandi306 – 3094Combined sources
    Beta strandi312 – 3165Combined sources
    Helixi324 – 3318Combined sources
    Beta strandi334 – 3385Combined sources
    Beta strandi344 – 3507Combined sources
    Helixi353 – 3553Combined sources
    Beta strandi363 – 3664Combined sources
    Helixi373 – 3808Combined sources
    Helixi382 – 39312Combined sources
    Helixi395 – 41117Combined sources
    Helixi417 – 4193Combined sources
    Helixi431 – 4333Combined sources
    Helixi445 – 45410Combined sources
    Helixi459 – 47012Combined sources
    Turni475 – 4784Combined sources
    Helixi486 – 4883Combined sources
    Helixi492 – 4943Combined sources
    Helixi496 – 4983Combined sources
    Helixi500 – 51718Combined sources
    Helixi521 – 53919Combined sources
    Helixi557 – 5593Combined sources
    Helixi563 – 5686Combined sources
    Beta strandi571 – 5733Combined sources
    Helixi574 – 5763Combined sources
    Beta strandi578 – 5814Combined sources
    Helixi587 – 59812Combined sources
    Helixi602 – 61514Combined sources
    Helixi619 – 6213Combined sources
    Helixi637 – 6426Combined sources
    Beta strandi647 – 6515Combined sources
    Beta strandi657 – 6615Combined sources
    Turni662 – 6643Combined sources
    Beta strandi667 – 6715Combined sources
    Helixi673 – 6764Combined sources
    Helixi677 – 6793Combined sources
    Helixi682 – 69211Combined sources
    Helixi694 – 6963Combined sources
    Helixi697 – 71216Combined sources
    Turni713 – 7153Combined sources
    Turni717 – 7193Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UB2X-ray2.40A1-720[»]
    3WNUX-ray2.20A1-720[»]
    3WXOX-ray2.12A11-720[»]
    3X16X-ray2.65A1-720[»]
    4PAEX-ray3.21A1-720[»]
    ProteinModelPortaliQ31MN3.
    SMRiQ31MN3. Positions 21-720.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ31MN3.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

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

    Family and domain databases

    HAMAPiMF_01961. Catal_peroxid.
    InterProiIPR000763. Catalase_peroxidase.
    IPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR019794. Peroxidases_AS.
    [Graphical view]
    PfamiPF00141. peroxidase. 2 hits.
    [Graphical view]
    PRINTSiPR00460. BPEROXIDASE.
    PR00458. PEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 2 hits.
    TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
    PROSITEiPS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q31MN3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTATQGKCPV MHGGATTVNI STAEWWPKAL NLDILSQHDR KTNPMGPDFN
    60 70 80 90 100
    YQEEVKKLDV AALKQDLQAL MTDSQDWWPA DWGHYGGLMI RLTWHAAGTY
    110 120 130 140 150
    RIADGRGGAG TGNQRFAPLN SWPDNTNLDK ARRLLWPIKQ KYGNKLSWAD
    160 170 180 190 200
    LIAYAGTIAY ESMGLKTFGF AFGREDIWHP EKDIYWGPEK EWVPPSTNPN
    210 220 230 240 250
    SRYTGDRELE NPLAAVTMGL IYVNPEGVDG NPDPLKTAHD VRVTFARMAM
    260 270 280 290 300
    NDEETVALTA GGHTVGKCHG NGNAALLGPE PEGADVEDQG LGWINKTQSG
    310 320 330 340 350
    IGRNAVTSGL EGAWTPHPTQ WDNGYFRMLL NYDWELKKSP AGAWQWEPIN
    360 370 380 390 400
    PREEDLPVDV EDPSIRRNLV MTDADMAMKM DPEYRKISER FYQDPAYFAD
    410 420 430 440 450
    VFARAWFKLT HRDMGPKARY IGPDVPQEDL IWQDPIPAGN RNYDVQAVKD
    460 470 480 490 500
    RIAASGLSIS ELVSTAWDSA RTYRNSDKRG GANGARIRLA PQKDWEGNEP
    510 520 530 540 550
    DRLAKVLAVL EGIAAATGAS VADVIVLAGN VGVEQAARAA GVEIVLPFAP
    560 570 580 590 600
    GRGDATAEQT DTESFAVLEP IHDGYRNWLK QDYAATPEEL LLDRTQLLGL
    610 620 630 640 650
    TAPEMTVLIG GLRVLGTNHG GTKHGVFTDR EGVLTNDFFV NLTDMNYLWK
    660 670 680 690 700
    PAGKNLYEIC DRKTNQVKWT ATRVDLVFGS NSILRAYSEL YAQDDNKEKF
    710 720
    VRDFVAAWTK VMNADRFDLD
    Length:720
    Mass (Da):80,078
    Last modified:December 6, 2005 - v1
    Checksum:i93A4C2E9990F1A2F
    GO

    Sequence cautioni

    The sequence BAA09601.1 differs from that shown. Reason: Frameshift at positions 574 and 594. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 561K → Q in BAA09601 (PubMed:8645214).Curated
    Sequence conflicti60 – 601Missing in BAA09601 (PubMed:8645214).Curated
    Sequence conflicti193 – 1931V → F in BAA09601 (PubMed:8645214).Curated
    Sequence conflicti327 – 3293RML → AVCS in BAA09601 (PubMed:8645214).Curated
    Sequence conflicti339 – 3391S → N in BAA09601 (PubMed:8645214).Curated
    Sequence conflicti504 – 5041A → P in BAA09601 (PubMed:8645214).Curated
    Sequence conflicti514 – 5141A → S in BAA09601 (PubMed:8645214).Curated
    Sequence conflicti520 – 5201S → T in BAA09601 (PubMed:8645214).Curated
    Sequence conflicti536 – 5361A → K in BAA09601 (PubMed:8645214).Curated
    Sequence conflicti625 – 6251G → V in BAA09601 (PubMed:8645214).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D61378 Genomic DNA. Translation: BAA09601.1. Frameshift.
    CP000100 Genomic DNA. Translation: ABB57686.1.
    PIRiS71130.
    RefSeqiWP_011244741.1. NC_007604.1.

    Genome annotation databases

    EnsemblBacteriaiABB57686; ABB57686; Synpcc7942_1656.
    KEGGisyf:Synpcc7942_1656.
    PATRICi23788713. VBISynElo51371_1880.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D61378 Genomic DNA. Translation: BAA09601.1. Frameshift.
    CP000100 Genomic DNA. Translation: ABB57686.1.
    PIRiS71130.
    RefSeqiWP_011244741.1. NC_007604.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UB2X-ray2.40A1-720[»]
    3WNUX-ray2.20A1-720[»]
    3WXOX-ray2.12A11-720[»]
    3X16X-ray2.65A1-720[»]
    4PAEX-ray3.21A1-720[»]
    ProteinModelPortaliQ31MN3.
    SMRiQ31MN3. Positions 21-720.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi1140.Synpcc7942_1656.

    Protein family/group databases

    PeroxiBasei2426. SeCP01_PCC7942.

    Proteomic databases

    PRIDEiQ31MN3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABB57686; ABB57686; Synpcc7942_1656.
    KEGGisyf:Synpcc7942_1656.
    PATRICi23788713. VBISynElo51371_1880.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyciSYNEL:SYNPCC7942_1656-MONOMER.
    BRENDAi1.11.1.21. 7781.

    Miscellaneous databases

    EvolutionaryTraceiQ31MN3.

    Family and domain databases

    HAMAPiMF_01961. Catal_peroxid.
    InterProiIPR000763. Catalase_peroxidase.
    IPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR019794. Peroxidases_AS.
    [Graphical view]
    PfamiPF00141. peroxidase. 2 hits.
    [Graphical view]
    PRINTSiPR00460. BPEROXIDASE.
    PR00458. PEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 2 hits.
    TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
    PROSITEiPS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 2 hits.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The catalase-peroxidase of Synechococcus PCC 7942: purification, nucleotide sequence analysis and expression in Escherichia coli."
      Mutsuda M., Ishikawa T., Takeda T., Shigeoka S.
      Biochem. J. 316:251-257(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-15, BIOPHYSICOCHEMICAL PROPERTIES, HEME-BINDING, SUBUNIT.
    2. "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PCC 7942.
    3. "Crystal structure of catalase-peroxidase from Synechococcus PCC 7942."
      Wada K., Tada T.
      Submitted (MAR-2004) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH HEME.

    Entry informationi

    Entry nameiKATG_SYNE7
    AccessioniPrimary (citable) accession number: Q31MN3
    Secondary accession number(s): Q55110
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 22, 2008
    Last sequence update: December 6, 2005
    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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.