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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)DescriptionActionsGraphical viewLength
    Sitei91Transition state stabilizerUniRule annotation1
    Active sitei95Proton acceptor1
    Metal bindingi263Iron (heme axial ligand)1

    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 lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
    Proteomesi
    • UP000002717 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00003450952 – 720Catalase-peroxidaseAdd BLAST719

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    1720
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi22 – 25Combined sources4
    Helixi32 – 35Combined sources4
    Turni40 – 42Combined sources3
    Helixi51 – 55Combined sources5
    Helixi60 – 71Combined sources12
    Helixi81 – 83Combined sources3
    Helixi86 – 97Combined sources12
    Turni102 – 104Combined sources3
    Helixi109 – 111Combined sources3
    Helixi113 – 115Combined sources3
    Helixi119 – 121Combined sources3
    Helixi123 – 125Combined sources3
    Helixi128 – 134Combined sources7
    Helixi136 – 142Combined sources7
    Helixi143 – 145Combined sources3
    Helixi148 – 163Combined sources16
    Beta strandi190 – 193Combined sources4
    Beta strandi196 – 198Combined sources3
    Beta strandi202 – 204Combined sources3
    Turni205 – 207Combined sources3
    Beta strandi215 – 217Combined sources3
    Beta strandi221 – 223Combined sources3
    Helixi234 – 247Combined sources14
    Helixi252 – 263Combined sources12
    Helixi274 – 276Combined sources3
    Helixi281 – 283Combined sources3
    Helixi286 – 288Combined sources3
    Beta strandi295 – 298Combined sources4
    Helixi302 – 304Combined sources3
    Beta strandi306 – 309Combined sources4
    Beta strandi312 – 316Combined sources5
    Helixi324 – 331Combined sources8
    Beta strandi334 – 338Combined sources5
    Beta strandi344 – 350Combined sources7
    Helixi353 – 355Combined sources3
    Beta strandi363 – 366Combined sources4
    Helixi373 – 380Combined sources8
    Helixi382 – 393Combined sources12
    Helixi395 – 411Combined sources17
    Helixi417 – 419Combined sources3
    Helixi431 – 433Combined sources3
    Helixi445 – 454Combined sources10
    Helixi459 – 470Combined sources12
    Turni475 – 478Combined sources4
    Helixi486 – 488Combined sources3
    Helixi492 – 494Combined sources3
    Helixi496 – 498Combined sources3
    Helixi500 – 517Combined sources18
    Helixi521 – 539Combined sources19
    Helixi557 – 559Combined sources3
    Helixi563 – 568Combined sources6
    Beta strandi571 – 573Combined sources3
    Helixi574 – 576Combined sources3
    Beta strandi578 – 581Combined sources4
    Helixi587 – 598Combined sources12
    Helixi602 – 615Combined sources14
    Helixi619 – 621Combined sources3
    Helixi637 – 642Combined sources6
    Beta strandi647 – 651Combined sources5
    Beta strandi657 – 661Combined sources5
    Turni662 – 664Combined sources3
    Beta strandi667 – 671Combined sources5
    Helixi673 – 676Combined sources4
    Helixi677 – 679Combined sources3
    Helixi682 – 692Combined sources11
    Helixi694 – 696Combined sources3
    Helixi697 – 712Combined sources16
    Turni713 – 715Combined sources3
    Turni717 – 719Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    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.
    OrthoDBiPOG091H05R1.

    Family and domain databases

    HAMAPiMF_01961. Catal_peroxid. 1 hit.
    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 differs from that shown. Reason: Frameshift at positions 574 and 594.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti56K → Q in BAA09601 (PubMed:8645214).Curated1
    Sequence conflicti60Missing in BAA09601 (PubMed:8645214).Curated1
    Sequence conflicti193V → F in BAA09601 (PubMed:8645214).Curated1
    Sequence conflicti327 – 329RML → AVCS in BAA09601 (PubMed:8645214).Curated3
    Sequence conflicti339S → N in BAA09601 (PubMed:8645214).Curated1
    Sequence conflicti504A → P in BAA09601 (PubMed:8645214).Curated1
    Sequence conflicti514A → S in BAA09601 (PubMed:8645214).Curated1
    Sequence conflicti520S → T in BAA09601 (PubMed:8645214).Curated1
    Sequence conflicti536A → K in BAA09601 (PubMed:8645214).Curated1
    Sequence conflicti625G → V in BAA09601 (PubMed:8645214).Curated1

    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
    PDB 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.
    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.
    OrthoDBiPOG091H05R1.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ31MN3.

    Family and domain databases

    HAMAPiMF_01961. Catal_peroxid. 1 hit.
    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...

    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 2, 2016
    This is version 72 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.