KATG1_MAGO7
ID KATG1_MAGO7 Reviewed; 750 AA.
AC A4R5S9; G4NGE6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Catalase-peroxidase 1 {ECO:0000255|HAMAP-Rule:MF_03108};
DE Short=CP 1 {ECO:0000255|HAMAP-Rule:MF_03108};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_03108};
DE AltName: Full=Peroxidase/catalase 1 {ECO:0000255|HAMAP-Rule:MF_03108};
GN Name=katG1 {ECO:0000255|HAMAP-Rule:MF_03108}; Synonyms=MagKatG1;
GN ORFNames=MGG_04337;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP GENE NAME.
RX PubMed=18498226; DOI=10.1089/ars.2008.2046;
RA Zamocky M., Furtmueller P.G., Obinger C.;
RT "Evolution of catalases from bacteria to humans.";
RL Antioxid. Redox Signal. 10:1527-1548(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=19000033; DOI=10.1042/bj20081478;
RA Zamocky M., Furtmuller P.G., Bellei M., Battistuzzi G., Stadlmann J.,
RA Vlasits J., Obinger C.;
RT "Intracellular catalase/peroxidase from the phytopathogenic rice blast
RT fungus Magnaporthe grisea: expression analysis and biochemical
RT characterization of the recombinant protein.";
RL Biochem. J. 418:443-451(2009).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_03108,
CC ECO:0000269|PubMed:19000033}.
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, ECO:0000269|PubMed:19000033};
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 ECO:0000269|PubMed:19000033};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03108,
CC ECO:0000269|PubMed:19000033};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
CC {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:19000033};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.8 mM for H(2)O(2) for the catalase reaction
CC {ECO:0000269|PubMed:19000033};
CC Note=kcat is 7010 sec(-1) with H(2)O(2) as substrate.;
CC pH dependence:
CC Optimum pH is 6.0 for the catalase reaction.
CC {ECO:0000269|PubMed:19000033};
CC -!- SUBUNIT: Homodimer or homotetramer. Predominantly homodimeric.
CC {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:19000033}.
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; CM001236; EHA47103.1; -; Genomic_DNA.
DR RefSeq; XP_003719470.1; XM_003719422.1.
DR AlphaFoldDB; A4R5S9; -.
DR SMR; A4R5S9; -.
DR STRING; 318829.MGG_04337T0; -.
DR PeroxiBase; 2288; MgrCP01.
DR PRIDE; A4R5S9; -.
DR EnsemblFungi; MGG_04337T0; MGG_04337T0; MGG_04337.
DR GeneID; 2677580; -.
DR KEGG; mgr:MGG_04337; -.
DR VEuPathDB; FungiDB:MGG_04337; -.
DR eggNOG; ENOG502QTDY; Eukaryota.
DR HOGENOM; CLU_025424_2_0_1; -.
DR InParanoid; A4R5S9; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 352289at2759; -.
DR BRENDA; 1.11.1.21; 3152.
DR Proteomes; UP000009058; Chromosome 6.
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; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Reference proteome.
FT CHAIN 1..750
FT /note="Catalase-peroxidase 1"
FT /id="PRO_0000345090"
FT REGION 199..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT BINDING 279
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 87
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 90..238
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 264)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 238..264
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 90)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
SQ SEQUENCE 750 AA; 82859 MW; E327E7C3950B46DE CRC64;
MGECPLRTAN VAGGGTRNRD WWPNTLKLNI LRQHTEATNP YDPNFDYAEA FKSLDYEGLK
KDLRALMTDS QEYWPADFGH YGGLFVRMAW HSAGTYRVMD GRGGGGQGQQ RFAPLNSWPD
NVSLDKARRL LWPIKQKYGN KISWADLMLL TGNVALEDMG FKTFGFAGGR PDTWEADEST
YWGGETTWLG NEVRYSSGNE GHKESGVIDG SESKKGHKDI HTRDLEKPVS AAHMGLIYVN
PEGPDGIPDP VAAARDIRTT FSRMAMNDEE TVALIAGGHT VGKTHGAAPS DNVGPEPEAA
PIENQGLGWS NKHGSGKGPD TITSGLEVIW TKEPAKFTMN YLEYLFKYEW ELTKSPAGAN
QWVAKNAEEF IPDAFDPSKK HKPRMLTTDL SLRFDPEYEK ISRRFLENPE QFKDAFARAW
FKLLHRDMGP RSRWLGPEVP KETLLWEDPI PTPDHPIIDG SDVDSLKKAI LATGVAPSKL
IQTAWASAST FRGGDKRGGA NGARIRLEPQ NKWEVNNPQQ LAEVLKALEG VKADFEKSGK
KVSIADLIVL AGVAAVEQAA GVPVPFTPGR GDATQEQTDV ESFTHLEPAA DAFRNYGKGT
SRVTTEQIMV DRAQQLTLTA PELTVLVGGL RVLGANYDGS SHGVWTDKPG KLTNDFFVTL
LDPYTSWKSV DGEVFEGTNS KSGKKLTGTR ADLVFGSHSE LRALAEVYGS ADGQQKFTKD
FVAAWDKVMN LDRFDVRRGI YDETRLKSKL
