ID K1X3B2_MARBU Unreviewed; 772 AA.
AC K1X3B2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Catalase-peroxidase {ECO:0000256|HAMAP-Rule:MF_03108, ECO:0000256|RuleBase:RU003451};
DE Short=CP {ECO:0000256|HAMAP-Rule:MF_03108};
DE EC=1.11.1.21 {ECO:0000256|HAMAP-Rule:MF_03108, ECO:0000256|RuleBase:RU003451};
DE AltName: Full=Peroxidase/catalase {ECO:0000256|HAMAP-Rule:MF_03108};
DE Flags: Precursor;
GN Name=katG {ECO:0000256|HAMAP-Rule:MF_03108};
GN ORFNames=MBM_01653 {ECO:0000313|EMBL:EKD19701.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD19701.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD19701.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD19701.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(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:0000256|HAMAP-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:0000256|ARBA:ARBA00001378, ECO:0000256|HAMAP-
CC Rule:MF_03108, ECO:0000256|RuleBase:RU003451};
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:0000256|HAMAP-
CC Rule:MF_03108, ECO:0000256|RuleBase:RU003451};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03108};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
CC {ECO:0000256|HAMAP-Rule:MF_03108};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|HAMAP-
CC Rule:MF_03108}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|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:0000256|HAMAP-Rule:MF_03108}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03108,
CC ECO:0000256|RuleBase:RU003451}.
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DR EMBL; JH921430; EKD19701.1; -; Genomic_DNA.
DR RefSeq; XP_007289542.1; XM_007289480.1.
DR AlphaFoldDB; K1X3B2; -.
DR STRING; 1072389.K1X3B2; -.
DR GeneID; 18757588; -.
DR KEGG; mbe:MBM_01653; -.
DR eggNOG; ENOG502QTDY; Eukaryota.
DR HOGENOM; CLU_025424_2_0_1; -.
DR InParanoid; K1X3B2; -.
DR OMA; WPCELNL; -.
DR OrthoDB; 317402at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
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 Gene3D; 1.10.520.10; -; 2.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
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 NCBIfam; TIGR00198; cat_per_HPI; 1.
DR PANTHER; PTHR30555:SF0; CATALASE-PEROXIDASE; 1.
DR PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_03108};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_03108};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324, ECO:0000256|HAMAP-
KW Rule:MF_03108};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03108};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03108};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03108};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW Rule:MF_03108}; Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Secreted {ECO:0000256|HAMAP-Rule:MF_03108};
KW Signal {ECO:0000256|HAMAP-Rule:MF_03108, ECO:0000256|RuleBase:RU003451}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108,
FT ECO:0000256|RuleBase:RU003451"
FT CHAIN 17..772
FT /note="Catalase-peroxidase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108,
FT ECO:0000256|RuleBase:RU003451"
FT /id="PRO_5006992512"
FT DOMAIN 122..433
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|Pfam:PF00141"
FT DOMAIN 505..743
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|Pfam:PF00141"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
FT BINDING 308
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
FT SITE 131
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
FT CROSSLNK 134..267
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with Met-
FT 293)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
FT CROSSLNK 267..293
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 134)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
SQ SEQUENCE 772 AA; 83306 MW; 331AE5230940E7CF CRC64;
MKSALLLLLP LVSAEGCPYA AANKRDLFGR QAESSESSLQ TLSSSFGKCS ALSDAAGGGT
RSADLWPCAL KLNVLRQFSA EQNPLGGDFD YAAAFATLDY DALKADLKAL MTDSQPWWPA
DFGHYGGFFI RMAWHSAGTY RSIDGRGGGG MGQQRFAPLN SWPDNSNLDK ARRLLLPIKQ
KYGRKISWAD LILLTGNVAL EDMGFPTIGF GAGRPDVWQS DESVYWGSET TLMPQGNDIR
YNGSTDYEAR ASQLQKPLAA THQGLIYVNP QGPDGNGDTM QSALDIRTTF ERMGMNDSET
VALIAGGHAF GKCHGAGEGN SGPPPAGAPM EQQDFGWTSS FGSGVGEDAV TSGLEVIWSE
TPTNWSNNYL ISLYKNNWTA TTSPTGAKQF EAVNGPLTYP EPFGTGKRRP SMLVSDLAIK
DDPIYGEITK AWSEDLPALT HAFAHAWFKL THRDMGPRVR YLGPEVPAES FLWQDPLPST
GAFQLSAAQQ TQLKNRILTT PGLSISSLVS VAWASASTYR DGDKRGGANG ARIALEPQVS
WPVNNPKQLK TVLDALKAIK ASFKSVSLAD LIVLGGNAAV EHAAALAGQT ISVPFTPGRV
DATQENTDLH SFEFLRPQAD GFRNFRNTTG WAISRTEELL VDKAQQLKLT APELTVLVGG
MRALNANFDG SSVGILTTTP GKLNANFFKN LLDMNTAWSA DASGELFTGS DRASGQEKWT
ASRADLIFGS HAELRAIAEV YTEAGSEAQF VSDFARTWAK VMDLDRFDVK KA
//
