KATG_RHOJR
ID KATG_RHOJR Reviewed; 742 AA.
AC Q0S5Y0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
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};
GN OrderedLocusNames=RHA1_ro05275;
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG97056.1; -; Genomic_DNA.
DR RefSeq; WP_011597474.1; NC_008268.1.
DR AlphaFoldDB; Q0S5Y0; -.
DR SMR; Q0S5Y0; -.
DR STRING; 101510.RHA1_ro05275; -.
DR PRIDE; Q0S5Y0; -.
DR EnsemblBacteria; ABG97056; ABG97056; RHA1_ro05275.
DR KEGG; rha:RHA1_ro05275; -.
DR PATRIC; fig|101510.16.peg.5329; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_11; -.
DR OMA; EEIFWGP; -.
DR Proteomes; UP000008710; 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;
KW Reference proteome.
FT CHAIN 1..742
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354890"
FT REGION 1..43
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 742 AA; 81161 MW; 5716C8F021346A71 CRC64;
MSDSCPVAHE GNTQSTSESE NPVIPSPTPA ANRPRNNRDW WPNQPELSVL HAHTSKSNPM
GEDFDYAEEF AKLDVEALKR DVIDLMTTSQ DWWPADYGHY GGLFIRMSWH AAGTYRIADG
RGGGGQGAQR FAPLNSWPDN ANLDKARRLL WPVKQKYGKQ ISWADLLVFA GNCALESMGF
KTFGFGFGRE DIWEPEEMYW GPEDTWLGDE RYSGDRELSG PLGAVQMGLI YVNPEGPNGQ
PDPLAAARDI RETFSRMAMN DVETAALIAG GHTFGKTHGA GDADLVGPEP EGAPIEQQGL
GWKSAYGTGV GKDAITSGLE VVWTPTPTKW DNSFLEVLYG YEWELTKSPA GAWQWTAKDG
AGAGTIPDPF DSSAGRAPTM LTTDLSLRID PAYEKITRRW LDHPEEFAEE FAKAWYKLLH
RDMGPVTRYL GPWVPEAQLW QDPVPAVDHQ LIGDSEIAAL KGKILDSGLS IPQLVSTAWA
SAATHRSTDM RGGANGARIR LAPQKDWEIN SPAELSTILQ TLEQIQQDFN SSQSGGVKVS
LADVIVLAGA AAVEKAAKNA GHDVTVPFTP GRTDATQEQT DVESFAVLEP KADGFRNYLR
AGEKLPAEAL LVDRAYMLNL TAPEMTVLVG GLRALNANFG QTKHGVFTDR PEALTNDFFV
NLLDMGTEWK GASSAENVYE GTDRVTGAAK WTATAVDLVF GSNSQLRALA EVYAADDAQQ
KFVQDFVSAW NKVMNLDRFD LD
