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Protein

Catalase-peroxidase

Gene

katG

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: -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 bUniRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.UniRule annotation

Enzyme regulationi

Inhibited by KCN.1 Publication

Kineticsi

  1. KM=13.2 mM for H2O2 for the catalase reaction1 Publication

    pH dependencei

    Optimum pH is 4.75 for the peroxidase reaction and 6.25 for the catalase reaction.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei87Transition state stabilizerUniRule annotation1
    Active sitei91Proton acceptorUniRule annotation1
    Metal bindingi279Iron (heme axial ligand)UniRule annotation1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionOxidoreductase, Peroxidase
    Biological processHydrogen peroxide
    LigandHeme, Iron, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.11.1.6 3627

    Protein family/group databases

    PeroxiBasei2181 NcCP01

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catalase-peroxidaseUniRule annotation (EC:1.11.1.21UniRule annotation)
    Short name:
    CPUniRule annotation
    Alternative name(s):
    Catalase-2
    Peroxidase/catalaseUniRule annotation
    Gene namesi
    Name:katGUniRule annotation
    Synonyms:cat-2
    ORF Names:NCU05770
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    Proteomesi
    • UP000001805 Componenti: Chromosome 7, Linkage Group VII

    Organism-specific databases

    EuPathDBiFungiDB:NCU05770

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000555821 – 753Catalase-peroxidaseAdd BLAST753

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Cross-linki90 ↔ 238Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-264)UniRule annotation
    Cross-linki238 ↔ 264Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-90)UniRule annotation

    Post-translational modificationi

    Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.UniRule annotation

    Proteomic databases

    PRIDEiQ8X182

    Expressioni

    Inductioni

    Induced in late stationary growth phase.1 Publication

    Interactioni

    Subunit structurei

    Homodimer or homotetramer.UniRule annotation

    Structurei

    Secondary structure

    1753
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi18 – 21Combined sources4
    Helixi29 – 31Combined sources3
    Helixi36 – 38Combined sources3
    Helixi47 – 52Combined sources6
    Helixi56 – 66Combined sources11
    Beta strandi72 – 74Combined sources3
    Helixi77 – 79Combined sources3
    Helixi82 – 89Combined sources8
    Helixi93 – 95Combined sources3
    Turni98 – 100Combined sources3
    Helixi109 – 111Combined sources3
    Helixi115 – 117Combined sources3
    Helixi124 – 130Combined sources7
    Helixi132 – 138Combined sources7
    Helixi139 – 141Combined sources3
    Helixi144 – 158Combined sources15
    Beta strandi166 – 168Combined sources3
    Turni192 – 194Combined sources3
    Beta strandi237 – 239Combined sources3
    Helixi244 – 246Combined sources3
    Helixi250 – 262Combined sources13
    Turni263 – 265Combined sources3
    Helixi268 – 278Combined sources11
    Helixi290 – 292Combined sources3
    Helixi297 – 299Combined sources3
    Helixi302 – 304Combined sources3
    Helixi318 – 320Combined sources3
    Beta strandi322 – 325Combined sources4
    Helixi340 – 347Combined sources8
    Beta strandi348 – 354Combined sources7
    Beta strandi360 – 366Combined sources7
    Helixi387 – 394Combined sources8
    Helixi396 – 407Combined sources12
    Helixi409 – 425Combined sources17
    Turni426 – 428Combined sources3
    Helixi431 – 433Combined sources3
    Beta strandi435 – 438Combined sources4
    Helixi460 – 472Combined sources13
    Helixi477 – 488Combined sources12
    Turni493 – 496Combined sources4
    Helixi504 – 506Combined sources3
    Helixi510 – 512Combined sources3
    Helixi514 – 516Combined sources3
    Helixi518 – 536Combined sources19
    Beta strandi537 – 539Combined sources3
    Helixi546 – 560Combined sources15
    Helixi577 – 579Combined sources3
    Helixi584 – 588Combined sources5
    Helixi594 – 596Combined sources3
    Beta strandi603 – 605Combined sources3
    Helixi607 – 617Combined sources11
    Helixi622 – 634Combined sources13
    Helixi639 – 641Combined sources3
    Helixi657 – 662Combined sources6
    Beta strandi667 – 683Combined sources17
    Turni684 – 686Combined sources3
    Beta strandi689 – 694Combined sources6
    Helixi695 – 702Combined sources8
    Helixi704 – 713Combined sources10
    Beta strandi715 – 717Combined sources3
    Helixi719 – 734Combined sources16
    Turni735 – 737Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5WHQX-ray2.90A/B2-753[»]
    5WHSX-ray2.60A/B7-741[»]
    ProteinModelPortaliQ8X182
    SMRiQ8X182
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000218110
    InParanoidiQ8X182
    KOiK03782
    OMAiPEEDIYW
    OrthoDBiEOG092C0YTX

    Family and domain databases

    HAMAPiMF_01961 Catal_peroxid, 1 hit
    InterProiView protein in InterPro
    IPR000763 Catalase_peroxidase
    IPR010255 Haem_peroxidase
    IPR002016 Haem_peroxidase_pln/fun/bac
    IPR019794 Peroxidases_AS
    IPR019793 Peroxidases_heam-ligand_BS
    PANTHERiPTHR30555 PTHR30555, 1 hit
    PfamiView protein in Pfam
    PF00141 peroxidase, 2 hits
    PRINTSiPR00460 BPEROXIDASE
    PR00458 PEROXIDASE
    SUPFAMiSSF48113 SSF48113, 2 hits
    TIGRFAMsiTIGR00198 cat_per_HPI, 1 hit
    PROSITEiView protein in PROSITE
    PS00435 PEROXIDASE_1, 1 hit
    PS00436 PEROXIDASE_2, 1 hit
    PS50873 PEROXIDASE_4, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q8X182-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSECPVRKSN VGGGGTRNHD WWPAQLRLNI LRQHTPVSNP LDKDFDYAAA
    60 70 80 90 100
    FKSLDYEGLK KDLTKLMTDS QDWWPADFGH YGGLFIRMAW HSAGTYRVTD
    110 120 130 140 150
    GRGGGGEGQQ RFAPLNSWPD NVSLDKARRL LWPIKQKYGN KISWSDLLLL
    160 170 180 190 200
    TGNVALESMG FKTFGFAGGR PDTWEADESV YWGAETTWLG NEDRYSEGQE
    210 220 230 240 250
    GHEGHGVVQG DESKKQHTDI HNRDLQSPLA SSHMGLIYVN PEGPDGIPDP
    260 270 280 290 300
    VASAKDIRVT FGRMAMNDEE TVALIAGGHS FGKTHGAGPT HHVGKEPEAA
    310 320 330 340 350
    PIEHQGLGWA NSFGQGKGPD TITSGLEVTW TPTPTKWGMG YLEYLYKFDW
    360 370 380 390 400
    EPTKSPAGAN QWVAKNAEPT IPDAYDPNKK KLPTMLTTDI ALRMDPAYDK
    410 420 430 440 450
    ICRDYLANPD KFADAFARAW FKLLHRDMGP RTRWIGPEVP SEILPWEDYI
    460 470 480 490 500
    PPVDYQIIDD NDIAALKKEI LATGVAPKKL IFVAWSSASS FRGSDKRGGA
    510 520 530 540 550
    NGARIRLAPQ NEWKVNDPST LREVLAALES VQQKFNDSSS GKKVSLADLI
    560 570 580 590 600
    VLGGVAALEQ ASGLVVPFTP GRNDATQEHT DVHSFTHLEP HADGFRSYGK
    610 620 630 640 650
    GTKRVRTEQF LIDRASLLTL SAPELTALIG GLRVLEANYD GSSYGVLTKT
    660 670 680 690 700
    PGKLTNDYFV NLLDTNTAWK AADNEGEVFI GYDRKTHDKK WTATRADLIF
    710 720 730 740 750
    GAHAELRALA EVYAAVDGEE KFKRDFVAAW HKVMNLDRFD LKQEGRGQNA

    PKL
    Length:753
    Mass (Da):83,380
    Last modified:October 1, 2002 - v2
    Checksum:iDED01DC6D10BA582
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF459787 mRNA Translation: AAL66352.2
    CM002242 Genomic DNA Translation: EAA30509.1
    RefSeqiXP_959745.1, XM_954652.3

    Genome annotation databases

    EnsemblFungiiEAA30509; EAA30509; NCU05770
    GeneIDi3875883
    KEGGincr:NCU05770

    Similar proteinsi

    Entry informationi

    Entry nameiKATG_NEUCR
    AccessioniPrimary (citable) accession number: Q8X182
    Secondary accession number(s): Q7S4Q3
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: October 1, 2002
    Last modified: March 28, 2018
    This is version 115 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health