KATG_ASPFC
ID KATG_ASPFC Reviewed; 759 AA.
AC B0YAK0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_03108};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_03108};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_03108};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_03108};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_03108}; ORFNames=AFUB_084930;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_03108}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03108};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03108};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03108};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
CC {ECO:0000255|HAMAP-Rule:MF_03108};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_03108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03108}.
CC -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC for the catalase, but not the peroxidase activity of the enzyme.
CC {ECO:0000255|HAMAP-Rule:MF_03108}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03108}.
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DR EMBL; DS499600; EDP49043.1; -; Genomic_DNA.
DR AlphaFoldDB; B0YAK0; -.
DR SMR; B0YAK0; -.
DR Allergome; 8994; Asp f CP.
DR EnsemblFungi; EDP49043; EDP49043; AFUB_084930.
DR VEuPathDB; FungiDB:AFUB_084930; -.
DR HOGENOM; CLU_025424_2_0_1; -.
DR PhylomeDB; B0YAK0; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR HAMAP; MF_01961; Catal_peroxid; 1.
DR InterPro; IPR000763; Catalase_peroxidase.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR30555; PTHR30555; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 2.
DR TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 2.
PE 3: Inferred from homology;
KW Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase.
FT CHAIN 1..759
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354099"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT BINDING 283
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT SITE 93
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 96..242
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 268)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 242..268
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 96)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
SQ SEQUENCE 759 AA; 83762 MW; 4519FF268CE43B8F CRC64;
MTQDKCPFKE QSSQPNFAGG GTSNKDWWPD RLKLNILRQH TAVSNPLDAD FDYAAAFNSL
DYEGLKKDLR ALMTDSQDWW PADFGHYGGL FIRMAWHSAG TYRVFDGRGG AGQGQQRFAP
LNSWPDNVSL DKARRLLWPI KQKYGNKISW ADLLILTGNV ALESMGFKTF GFAGGRPDTW
EADEATYWGR ETTWLGNDAR YAKGFSGSDK RGSLIADEES HKTTHSRELE TPLAAAHMGL
IYVNPEGPDG NPDPVAAAHD IRDTFGRMAM NDEETVALIA GGHTFGKTHG AAPADNVGKE
PEAAGLEAQG LGWANKHGSG KGPHTITSGL EVTWTKTPTQ WNNNFLEYLF KFEWELTKSP
AGAHQWVAKN ADEIIPDAYD ASKKHKPTML TTDLSLRFDP AYEKIARRFL EHPDQFADAF
ARAWFKLTHR DMGPRARYLG PEVPSEVLIW QDPIPAVNHP LVDASDIAAL KDEILASGVP
PRSFISTAWA AASTFRGSDK RGGANGARIR LAPQRDWEVN NQPWLREALS ALEAVQSRFN
ARGDSKKVSL ADLIVLAGCA AVEKAAQDAG HPIKVPFVPG RMDASQEETD VQSFNHMEPF
ADGFRNFAKG PARPRAEHYL VDKAQLLNLS APEMTVLVGG LRVLNTNYDG STHGVFTSRP
GALTNDFFVH LLDMNTAWKD VGNGELFEGS DRKTGGKKWT ATRADLVFGS NAELRAIAEV
YASNDGDMKF VKDFVAAWNK VMNLDRFDLK GKQTIPARL