KATG2_MAGO7
ID KATG2_MAGO7 Reviewed; 786 AA.
AC A4QUT2; G4NII0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Catalase-peroxidase 2 {ECO:0000255|HAMAP-Rule:MF_03108};
DE Short=CP 2 {ECO:0000255|HAMAP-Rule:MF_03108};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_03108};
DE AltName: Full=Peroxidase/catalase 2 {ECO:0000255|HAMAP-Rule:MF_03108};
DE Flags: Precursor;
GN Name=KATG2; Synonyms=CPXB, MagKatG2; ORFNames=MGG_09834;
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 PROTEIN SEQUENCE OF 418-432, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21043575; DOI=10.1094/mpmi-07-10-0175;
RA Tanabe S., Ishii-Minami N., Saitoh K., Otake Y., Kaku H., Shibuya N.,
RA Nishizawa Y., Minami E.;
RT "The role of catalase-peroxidase secreted by Magnaporthe oryzae during
RT early infection of rice cells.";
RL Mol. Plant Microbe Interact. 24:163-171(2011).
RN [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=21971530; DOI=10.1016/j.biochi.2011.09.020;
RA Zamocky M., Droghetti E., Bellei M., Gasselhuber B., Pabst M.,
RA Furtmuller P.G., Battistuzzi G., Smulevich G., Obinger C.;
RT "Eukaryotic extracellular catalase-peroxidase from Magnaporthe grisea
RT -- Biophysical/chemical characterization of the first representative from a
RT novel phytopathogenic KatG group.";
RL Biochimie 94:673-683(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 24-786, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22822072; DOI=10.1074/jbc.m112.384271;
RA Zamocky M., Garcia-Fernandez Q., Gasselhuber B., Jakopitsch C.,
RA Furtmuller P.G., Loewen P.C., Fita I., Obinger C., Carpena X.;
RT "High conformational stability of secreted eukaryotic catalase-peroxidases:
RT Answers from first crystal structure and unfolding studies.";
RL J. Biol. Chem. 287:32254-32262(2012).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. Confers resistance to H(2)O(2) in hyphae. May play
CC an antioxidative role in fungal defense against the host-produced
CC H(2)O(2) (oxidative burst) at the early stage of plant infection.
CC {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:21043575,
CC ECO:0000269|PubMed:21971530}.
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 ECO:0000269|PubMed:22822072};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
CC {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:22822072};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.84 mM for H(2)O(2) for the catalase reaction (at pH 5.25)
CC {ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072};
CC KM=2.77 mM for H(2)O(2) for the catalase reaction (at pH 7.0)
CC {ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072};
CC Note=kcat is 6446 sec(-1) with H(2)O(2) as substrate at pH 5.25 and
CC 3290 sec(-1) with H(2)O(2) as substrate at pH 7.0.;
CC pH dependence:
CC Optimum pH is 5.25 for the catalase reaction. Stable from pH 5.5 to
CC pH 11. {ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000255|HAMAP-Rule:MF_03108,
CC ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_03108,
CC ECO:0000269|PubMed:21043575}.
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; EHA48040.1; -; Genomic_DNA.
DR RefSeq; XP_003720407.1; XM_003720359.1.
DR PDB; 3UT2; X-ray; 1.55 A; A/B=24-786.
DR PDB; 5CJH; X-ray; 1.60 A; A/B=24-786.
DR PDB; 5JHX; X-ray; 1.40 A; A/B=24-786.
DR PDB; 5JHY; X-ray; 1.40 A; A/B=24-786.
DR PDB; 5JHZ; X-ray; 1.70 A; A/B=24-786.
DR PDBsum; 3UT2; -.
DR PDBsum; 5CJH; -.
DR PDBsum; 5JHX; -.
DR PDBsum; 5JHY; -.
DR PDBsum; 5JHZ; -.
DR AlphaFoldDB; A4QUT2; -.
DR SMR; A4QUT2; -.
DR STRING; 318829.MGG_09834T0; -.
DR PeroxiBase; 2337; MgrCP02.
DR PRIDE; A4QUT2; -.
DR EnsemblFungi; MGG_09834T0; MGG_09834T0; MGG_09834.
DR GeneID; 2680833; -.
DR KEGG; mgr:MGG_09834; -.
DR VEuPathDB; FungiDB:MGG_09834; -.
DR eggNOG; ENOG502QTDY; Eukaryota.
DR HOGENOM; CLU_025424_2_0_1; -.
DR InParanoid; A4QUT2; -.
DR OMA; DTWQADE; -.
DR OrthoDB; 352289at2759; -.
DR BRENDA; 1.11.1.21; 3152.
DR PHI-base; PHI:2183; -.
DR Proteomes; UP000009058; Chromosome 6.
DR GO; GO:0005576; C:extracellular region; 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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CHAIN 24..786
FT /note="Catalase-peroxidase 2"
FT /id="PRO_0000345091"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT BINDING 314
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 SITE 137
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55
FT /note="Interchain (with C-74)"
FT DISULFID 74
FT /note="Interchain (with C-55)"
FT CROSSLNK 140..273
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 299)"
FT CROSSLNK 273..299
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 140)"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:5JHX"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 174..188
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:5JHX"
FT TURN 244..249
FT /evidence="ECO:0007829|PDB:5JHX"
FT TURN 253..258
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 285..298
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 303..313
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 375..382
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 431..442
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 444..460
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 495..506
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 513..524
FT /evidence="ECO:0007829|PDB:5JHX"
FT TURN 529..532
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 540..542
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 546..548
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 554..571
FT /evidence="ECO:0007829|PDB:5JHX"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:5JHY"
FT HELIX 582..600
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 623..627
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:5JHX"
FT TURN 635..638
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 648..658
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 663..675
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 698..703
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 708..712
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 714..717
FT /evidence="ECO:0007829|PDB:5JHY"
FT STRAND 719..724
FT /evidence="ECO:0007829|PDB:5JHX"
FT TURN 725..727
FT /evidence="ECO:0007829|PDB:5JHX"
FT STRAND 730..735
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 736..739
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 740..742
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 745..755
FT /evidence="ECO:0007829|PDB:5JHX"
FT HELIX 760..775
FT /evidence="ECO:0007829|PDB:5JHX"
FT TURN 776..778
FT /evidence="ECO:0007829|PDB:5JHX"
FT TURN 780..782
FT /evidence="ECO:0007829|PDB:5JHY"
SQ SEQUENCE 786 AA; 85587 MW; 2A6C8B2B043C3879 CRC64;
MHASLSSWLL AASLLTQPIS VSGQGCPFAK RDGTVDSSLP QKRADAPETT TFGRCAVKSN
QAGGGTRSHD WWPCQLRLDV LRQFQPSQNP LGGDFDYAEA FQSLDYEAVK KDIAALMTES
QDWWPADFGN YGGLFVRMAW HSAGTYRAMD GRGGGGMGQQ RFAPLNSWPD NQNLDKARRL
IWPIKQKYGN KISWADLMLL TGNVALENMG FKTLGFGGGR ADTWQSDEAV YWGAETTFVP
QGNDVRYNNS VDINARADKL EKPLAATHMG LIYVNPEGPN GTPDPAASAK DIREAFGRMG
MNDTETVALI AGGHAFGKTH GAVKGSNIGP APEAADLGMQ GLGWHNSVGD GNGPNQMTSG
LEVIWTKTPT KWSNGYLESL INNNWTLVES PAGAHQWEAV NGTVDYPDPF DKTKFRKATM
LTSDLALIND PEYLKISQRW LEHPEELADA FAKAWFKLLH RDLGPTTRYL GPEVPKESFI
WQDPLPAREG DLIDDADVDK LKAAILSTDG LDVSKLASTA MACATTYRNS DKRGGCNGAR
IALEPQRNWV SNNPTQLSAV LDALKKVQSD FNGSNGNKKV SLADLIVLGG TAAVEKAAKD
AGVDIKVPFS AGRVDATQEQ TDVTQFSYLE PQADGFRNYG RGTARARTEE IMVDKASQLT
LTPPELTVLV GGMRALGANY DGSDVGVFTA NKGKLTPDFF VNLVDMNIAW TASGADGESW
VGTDRKSRSE KYKGSRADLV FGSHAELRAI AEVYAENGNQ EKFVKDFVAA WTKVMNLDRF
DLKVKK
