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Catalase-peroxidase 2 (CP 2) (EC 1.11.1.21) (Peroxidase/catalase 2)

 KATG2_MAGO7             Reviewed;         786 AA.
A4QUT2; G4NII0;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
15-MAY-2007, sequence version 1.
20-DEC-2017, entry version 82.
RecName: Full=Catalase-peroxidase 2 {ECO:0000255|HAMAP-Rule:MF_03108};
Short=CP 2 {ECO:0000255|HAMAP-Rule:MF_03108};
EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_03108};
AltName: Full=Peroxidase/catalase 2 {ECO:0000255|HAMAP-Rule:MF_03108};
Flags: Precursor;
Name=KATG2; Synonyms=CPXB, MagKatG2; ORFNames=MGG_09834;
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice
blast fungus) (Pyricularia oryzae).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Magnaporthales; Magnaporthaceae;
Magnaporthe.
NCBI_TaxID=242507;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
PubMed=15846337; DOI=10.1038/nature03449;
Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W.,
Harding M., Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J.,
Calvo S.E., Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E.,
Birren B.W.;
"The genome sequence of the rice blast fungus Magnaporthe grisea.";
Nature 434:980-986(2005).
[2]
PROTEIN SEQUENCE OF 418-432, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21043575; DOI=10.1094/MPMI-07-10-0175;
Tanabe S., Ishii-Minami N., Saitoh K., Otake Y., Kaku H., Shibuya N.,
Nishizawa Y., Minami E.;
"The role of catalase-peroxidase secreted by Magnaporthe oryzae during
early infection of rice cells.";
Mol. Plant Microbe Interact. 24:163-171(2011).
[3]
GENE NAME.
PubMed=18498226; DOI=10.1089/ars.2008.2046;
Zamocky M., Furtmueller P.G., Obinger C.;
"Evolution of catalases from bacteria to humans.";
Antioxid. Redox Signal. 10:1527-1548(2008).
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBUNIT.
PubMed=21971530; DOI=10.1016/j.biochi.2011.09.020;
Zamocky M., Droghetti E., Bellei M., Gasselhuber B., Pabst M.,
Furtmuller P.G., Battistuzzi G., Smulevich G., Obinger C.;
"Eukaryotic extracellular catalase-peroxidase from Magnaporthe grisea
-- Biophysical/chemical characterization of the first representative
from a novel phytopathogenic KatG group.";
Biochimie 94:673-683(2012).
[5]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 24-786, CATALYTIC ACTIVITY,
COFACTOR, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=22822072; DOI=10.1074/jbc.M112.384271;
Zamocky M., Garcia-Fernandez Q., Gasselhuber B., Jakopitsch C.,
Furtmuller P.G., Loewen P.C., Fita I., Obinger C., Carpena X.;
"High conformational stability of secreted eukaryotic catalase-
peroxidases: Answers from first crystal structure and unfolding
studies.";
J. Biol. Chem. 287:32254-32262(2012).
-!- FUNCTION: Bifunctional enzyme with both catalase and broad-
spectrum peroxidase activity. Confers resistance to H(2)O(2) in
hyphae. May play an antioxidative role in fungal defense against
the host-produced H(2)O(2) (oxidative burst) at the early stage of
plant infection. {ECO:0000255|HAMAP-Rule:MF_03108,
ECO:0000269|PubMed:21043575, ECO:0000269|PubMed:21971530}.
-!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
{ECO:0000255|HAMAP-Rule:MF_03108}.
-!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
{ECO:0000255|HAMAP-Rule:MF_03108}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000255|HAMAP-Rule:MF_03108,
ECO:0000269|PubMed:22822072};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
monomer. {ECO:0000255|HAMAP-Rule:MF_03108,
ECO:0000269|PubMed:22822072};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.84 mM for H(2)O(2) for the catalase reaction (at pH 5.25)
{ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072};
KM=2.77 mM for H(2)O(2) for the catalase reaction (at pH 7.0)
{ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072};
Note=kcat is 6446 sec(-1) with H(2)O(2) as substrate at pH 5.25
and 3290 sec(-1) with H(2)O(2) as substrate at pH 7.0.;
pH dependence:
Optimum pH is 5.25 for the catalase reaction. Stable from pH 5.5
to pH 11. {ECO:0000269|PubMed:21971530,
ECO:0000269|PubMed:22822072};
-!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000255|HAMAP-
Rule:MF_03108, ECO:0000269|PubMed:21971530,
ECO:0000269|PubMed:22822072}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_03108,
ECO:0000269|PubMed:21043575}.
-!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is
important for the catalase, but not the peroxidase activity of the
enzyme. {ECO:0000255|HAMAP-Rule:MF_03108}.
-!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
subfamily. {ECO:0000255|HAMAP-Rule:MF_03108}.
-----------------------------------------------------------------------
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EMBL; CM001236; EHA48040.1; -; Genomic_DNA.
RefSeq; XP_003720407.1; XM_003720359.1.
PDB; 3UT2; X-ray; 1.55 A; A/B=24-786.
PDB; 5CJH; X-ray; 1.60 A; A/B=24-786.
PDB; 5JHX; X-ray; 1.40 A; A/B=24-786.
PDB; 5JHY; X-ray; 1.40 A; A/B=24-786.
PDB; 5JHZ; X-ray; 1.70 A; A/B=24-786.
PDBsum; 3UT2; -.
PDBsum; 5CJH; -.
PDBsum; 5JHX; -.
PDBsum; 5JHY; -.
PDBsum; 5JHZ; -.
ProteinModelPortal; A4QUT2; -.
SMR; A4QUT2; -.
STRING; 318829.MGG_09834T0; -.
PeroxiBase; 2337; MgrCP02.
PRIDE; A4QUT2; -.
EnsemblFungi; MGG_09834T0; MGG_09834T0; MGG_09834.
GeneID; 2680833; -.
KEGG; mgr:MGG_09834; -.
EuPathDB; FungiDB:MGG_09834; -.
InParanoid; A4QUT2; -.
KO; K03782; -.
OrthoDB; EOG092C0YTX; -.
BRENDA; 1.11.1.21; 3152.
Proteomes; UP000009058; Chromosome 6.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004096; F:catalase activity; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
HAMAP; MF_01961; Catal_peroxid; 1.
InterPro; IPR000763; Catalase_peroxidase.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
InterPro; IPR019794; Peroxidases_AS.
InterPro; IPR019793; Peroxidases_heam-ligand_BS.
PANTHER; PTHR30555; PTHR30555; 1.
Pfam; PF00141; peroxidase; 2.
PRINTS; PR00460; BPEROXIDASE.
PRINTS; PR00458; PEROXIDASE.
SUPFAM; SSF48113; SSF48113; 2.
TIGRFAMs; TIGR00198; cat_per_HPI; 1.
PROSITE; PS00435; PEROXIDASE_1; 1.
PROSITE; PS00436; PEROXIDASE_2; 1.
PROSITE; PS50873; PEROXIDASE_4; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
Metal-binding; Oxidoreductase; Peroxidase; Reference proteome;
Secreted; Signal.
SIGNAL 1 23 {ECO:0000255|HAMAP-Rule:MF_03108}.
CHAIN 24 786 Catalase-peroxidase 2.
/FTId=PRO_0000345091.
ACT_SITE 141 141 Proton acceptor.
METAL 314 314 Iron (heme axial ligand).
SITE 137 137 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_03108}.
CARBOHYD 248 248 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 384 384 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 572 572 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 55 55 Interchain (with C-74).
DISULFID 74 74 Interchain (with C-55).
CROSSLNK 140 273 Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
(with M-299).
CROSSLNK 273 299 Tryptophyl-tyrosyl-methioninium (Tyr-Met)
(with W-140).
HELIX 68 71 {ECO:0000244|PDB:5JHX}.
HELIX 79 81 {ECO:0000244|PDB:5JHX}.
STRAND 82 84 {ECO:0000244|PDB:5JHX}.
HELIX 86 88 {ECO:0000244|PDB:5JHX}.
HELIX 97 102 {ECO:0000244|PDB:5JHX}.
HELIX 106 117 {ECO:0000244|PDB:5JHX}.
HELIX 127 129 {ECO:0000244|PDB:5JHX}.
HELIX 132 143 {ECO:0000244|PDB:5JHX}.
TURN 148 150 {ECO:0000244|PDB:5JHX}.
HELIX 159 161 {ECO:0000244|PDB:5JHX}.
HELIX 165 167 {ECO:0000244|PDB:5JHX}.
HELIX 169 171 {ECO:0000244|PDB:5JHX}.
HELIX 174 188 {ECO:0000244|PDB:5JHX}.
HELIX 189 191 {ECO:0000244|PDB:5JHX}.
HELIX 194 208 {ECO:0000244|PDB:5JHX}.
TURN 244 249 {ECO:0000244|PDB:5JHX}.
TURN 253 258 {ECO:0000244|PDB:5JHX}.
STRAND 266 268 {ECO:0000244|PDB:5JHX}.
STRAND 272 274 {ECO:0000244|PDB:5JHX}.
HELIX 279 281 {ECO:0000244|PDB:5JHX}.
HELIX 285 298 {ECO:0000244|PDB:5JHX}.
HELIX 303 313 {ECO:0000244|PDB:5JHX}.
HELIX 325 327 {ECO:0000244|PDB:5JHX}.
HELIX 332 334 {ECO:0000244|PDB:5JHX}.
HELIX 337 339 {ECO:0000244|PDB:5JHX}.
HELIX 353 355 {ECO:0000244|PDB:5JHX}.
STRAND 357 360 {ECO:0000244|PDB:5JHX}.
HELIX 375 382 {ECO:0000244|PDB:5JHX}.
STRAND 386 389 {ECO:0000244|PDB:5JHX}.
STRAND 395 398 {ECO:0000244|PDB:5JHX}.
STRAND 406 408 {ECO:0000244|PDB:5JHX}.
STRAND 411 416 {ECO:0000244|PDB:5JHX}.
HELIX 422 425 {ECO:0000244|PDB:5JHX}.
HELIX 426 428 {ECO:0000244|PDB:5JHX}.
HELIX 431 442 {ECO:0000244|PDB:5JHX}.
HELIX 444 460 {ECO:0000244|PDB:5JHX}.
HELIX 466 468 {ECO:0000244|PDB:5JHX}.
HELIX 480 482 {ECO:0000244|PDB:5JHX}.
STRAND 489 491 {ECO:0000244|PDB:5JHX}.
HELIX 495 506 {ECO:0000244|PDB:5JHX}.
HELIX 513 524 {ECO:0000244|PDB:5JHX}.
TURN 529 532 {ECO:0000244|PDB:5JHX}.
HELIX 540 542 {ECO:0000244|PDB:5JHX}.
HELIX 546 548 {ECO:0000244|PDB:5JHX}.
HELIX 550 552 {ECO:0000244|PDB:5JHX}.
HELIX 554 571 {ECO:0000244|PDB:5JHX}.
TURN 572 574 {ECO:0000244|PDB:5JHX}.
STRAND 575 577 {ECO:0000244|PDB:5JHY}.
HELIX 582 600 {ECO:0000244|PDB:5JHX}.
HELIX 618 620 {ECO:0000244|PDB:5JHX}.
HELIX 623 627 {ECO:0000244|PDB:5JHX}.
STRAND 632 634 {ECO:0000244|PDB:5JHX}.
TURN 635 638 {ECO:0000244|PDB:5JHX}.
HELIX 648 658 {ECO:0000244|PDB:5JHX}.
HELIX 663 675 {ECO:0000244|PDB:5JHX}.
HELIX 698 703 {ECO:0000244|PDB:5JHX}.
STRAND 708 712 {ECO:0000244|PDB:5JHX}.
STRAND 714 717 {ECO:0000244|PDB:5JHY}.
STRAND 719 724 {ECO:0000244|PDB:5JHX}.
TURN 725 727 {ECO:0000244|PDB:5JHX}.
STRAND 730 735 {ECO:0000244|PDB:5JHX}.
HELIX 736 739 {ECO:0000244|PDB:5JHX}.
HELIX 740 742 {ECO:0000244|PDB:5JHX}.
HELIX 745 755 {ECO:0000244|PDB:5JHX}.
HELIX 760 775 {ECO:0000244|PDB:5JHX}.
TURN 776 778 {ECO:0000244|PDB:5JHX}.
TURN 780 782 {ECO:0000244|PDB:5JHY}.
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


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