KATG_PHANO
ID KATG_PHANO Reviewed; 751 AA.
AC Q0U324;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=SNOG_13840;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445352; EAT78864.1; -; Genomic_DNA.
DR RefSeq; XP_001804042.1; XM_001803990.1.
DR AlphaFoldDB; Q0U324; -.
DR SMR; Q0U324; -.
DR STRING; 13684.SNOT_13840; -.
DR PeroxiBase; 3449; PnoCP01.
DR PRIDE; Q0U324; -.
DR EnsemblFungi; SNOT_13840; SNOT_13840; SNOG_13840.
DR GeneID; 5980964; -.
DR KEGG; pno:SNOG_13840; -.
DR eggNOG; ENOG502QTDY; Eukaryota.
DR HOGENOM; CLU_025424_2_0_1; -.
DR InParanoid; Q0U324; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 352289at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Reference proteome.
FT CHAIN 1..751
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354109"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT BINDING 281
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 89
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 92..240
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 266)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 240..266
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 92)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
SQ SEQUENCE 751 AA; 83498 MW; FC5E1BFA5C89B85B CRC64;
MSKGECPMRT ANVAGGGTKI KDWWPNELPV SVLRQHDPRQ NPLTSDFNYA EEFKKLDYNA
LKKDLTALMT DSQDWWPADF GHYGGLFVRM AWHSAGTYRV TDGRGGGGDG QQRFAPLNAW
PDNVSLDKAR RLLWPIKQKY GNKISWADLM LLTGNVALES MGCETFGFAG GRPDTFQSDE
SIYWGGEDTW LGNDVRYSNG NKGVSGEGVV DGDQHKMDHK DIHSRDLEQP VAAAHMGLIY
VNPEGPDGVP DPIAAARDIR TTFHRMAMND EETAALIIGG HSFGKTHGAA PSENTGPDPN
SEDLSTQGFG WINKHGSGKG PDTITSGLEV TWTGTPTKWS NKYLEYLYKY EWELEKSPAG
ANQWVAKTED HIIPDAYDAN KKHKPRMLTT DMSMRMDPGF EKITRRWLDH PQELHDAFIR
AWFKLLHRDM GPRSRWVGPE IPKEVLLWED PVPEVDHALV EESDISALKK QILEAGIEPS
KLIRTAWASA ASYRGSDKRG GANGARIRLA PQKDWEVNNP KELAEVLKAL EGVQSKFNGS
ASGGKKISLA DLIVLAGTAA VEKAAGVSVP FTPGRTDATE EQTDAKSFEH LEPATDPFRN
YGKSSDRART EQLDLDKASL LRLTAPELTV LVGGMRALNA NWDSSSHGIF TKRPGQLTND
FFVNLLDINT EWKAADSSKL PELYEGFDRK SGQKKWTGTR HDLVYGSHPE LRAIAEVYAQ
PDNSDKFVKD FVKAWDKVMS NDRFDLKAKS S
