KATG_METPP
ID KATG_METPP Reviewed; 715 AA.
AC A2SMA4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Mpe_A3740;
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX NCBI_TaxID=420662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX PubMed=17158667; DOI=10.1128/jb.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
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_01961};
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_01961};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01961}.
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_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR EMBL; CP000555; ABM96693.1; -; Genomic_DNA.
DR RefSeq; WP_011831313.1; NC_008825.1.
DR AlphaFoldDB; A2SMA4; -.
DR SMR; A2SMA4; -.
DR STRING; 420662.Mpe_A3740; -.
DR PeroxiBase; 2346; MpetCP01.
DR EnsemblBacteria; ABM96693; ABM96693; Mpe_A3740.
DR KEGG; mpt:Mpe_A3740; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_4; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000000366; Chromosome.
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 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; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..715
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354832"
FT REGION 260..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 256
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_01961"
FT SITE 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 91..215
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 241)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 215..241
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 91)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 715 AA; 77828 MW; FEF5A0F70B124663 CRC64;
MATESKCPFN HAAGGGTTNQ DWWPSQLRLE LLNQHSSKSD PLGAGFDYAE EFKKLDYFAL
KKDLLALMTD SQDWWPADFG HYGPQFVRMA WHAAGTYRTA DGRGGGGRGQ QRFAPLNSWP
DNVNIDKSRR LLWPIKQKYG QRISWADLLI LTGNVALESM GFRTFGFAGG REDVWEPDND
VNWGNETTWL ATDKRFTGDR DLDQPLAATH MGLIYVNPEG PNASGDPLAA AKDIRATFGR
MAMDDEEIVA LIAGGHTFGK AHGAAPESHK GPEPEGAPLE AQGLGWTSSF GSGHGKDTVS
SGLEVTWTTT PARWSNDFFE HLFKFEWELT QSPAGAKQWT AKDAPEIIPD AHVPGKKLKP
TMLTTDLTLR VDPEFEKISR RFLDNPQGFA DAFARAWFKL THRDMGPKVR YLGPEVPKEE
LLWQDPLPPA TLPAPNAADV AELKAKIAAS GLTVAQLVAT AWASASTFRG GDKRGGANGA
RLRLAPQKDW EANTPGELAK VLATLETLQK ASGKFSLADV IVLAGGVGVE QAAKAAGVGI
EVPFAPGRVD ATQEQTDVES FAFLEPVADG FRNYFKGPGS VPVEHLLVDK AQLLTLTAPE
MTVLVGGLRV LGANAGGSRH GVFTDRPGVL TPDFFVNLLD MRTTWQPANG VYEGKDRQTG
QQKWTATRVD LAFGSNAVLR ALAEVYASAD GQTKFVHDFV AAWTKVMNLD RYDLA
