KATG_RHOE4
ID KATG_RHOE4 Reviewed; 740 AA.
AC C0ZSW0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=RER_12250;
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=234621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AP008957; BAH31933.1; -; Genomic_DNA.
DR RefSeq; WP_020906506.1; NC_012490.1.
DR AlphaFoldDB; C0ZSW0; -.
DR SMR; C0ZSW0; -.
DR STRING; 234621.RER_12250; -.
DR EnsemblBacteria; BAH31933; BAH31933; RER_12250.
DR KEGG; rer:RER_12250; -.
DR PATRIC; fig|234621.6.peg.1689; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_11; -.
DR OMA; EEIFWGP; -.
DR Proteomes; UP000002204; 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 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 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..740
FT /note="Catalase-peroxidase"
FT /id="PRO_1000216226"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 110
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 272
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 106
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 109..231
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 257)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 231..257
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 109)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 740 AA; 80838 MW; 89718B33D8DBE547 CRC64;
MSDSCPVAHD GNTASTSESE NPAIPSPTPT GNRPRTNRDW WPNQPDLSVL HAHSSKSNPM
GADFDYAQEF AKLDVEALKR DVIALMTASQ DWWPADYGHY GGLFVRMSWH AAGTYRIADG
RGGGGQGAQR FAPLNSWPDN ASLDKARRLL WPVKQKYGKQ VSWADLLVFA GNCALESMGF
TTFGFGFGRE DIWEPEEIYW GPEDTWLGDE RYSGDRELSG PLGAVQMGLI YVNPEGPNGQ
PDPVAAARDI RETFARMAMN DVETAALIAG GHTFGKTHGA GPADLVGPEP EGAPVEQQGL
GWKSAFGTGV GKDAITSGLE VVWTPTPTKW DNTFLEILYG YDWELTKSPA GAWQWIPKDG
AGAGTIPDPF DSSAGRTPTM LTTDLSLRLD PTYEKITRRW LDHPEEFAEE FAKAWYKLLH
RDMGPVTRYL GPWVPEPQLW QDPVPSADDQ LIGDADIAIL KSRLLDSGLS VSQLVSTAWA
SAASFRSTDM RGGANGARIR LEPQKNWEVN EPATLSAVLQ TLERVQQEFN QAGGAKVSLA
DLIVLGGTAA VEQAAKNAGQ DITVSFTPGR TDATQEQTDV DSFEVLEPRA DGFRNYLKGG
EKIPAEILLV DRAYMLSLTP PEVTVLVGGL RALNANFGKT GHGVFTDRPE TLTNDFFVNL
LDMGTEWKPS KTEENVYDGV DRATGDPKYT ATAVDLVFGS NSQLRALSEV YASEDAKQKF
AEDFAAAWTK VMDLDRFDVN
