KATG_STRGG
ID KATG_STRGG Reviewed; 751 AA.
AC B1W5Q9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=SGR_6387;
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=455632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350;
RX PubMed=18375553; DOI=10.1128/jb.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG23216.1; -; Genomic_DNA.
DR RefSeq; WP_012381903.1; NC_010572.1.
DR AlphaFoldDB; B1W5Q9; -.
DR SMR; B1W5Q9; -.
DR STRING; 455632.SGR_6387; -.
DR EnsemblBacteria; BAG23216; BAG23216; SGR_6387.
DR GeneID; 6209390; -.
DR KEGG; sgr:SGR_6387; -.
DR PATRIC; fig|455632.4.peg.6547; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_11; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001685; 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..751
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354939"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 285
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 118
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 121..244
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 270)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 244..270
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 121)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 751 AA; 81589 MW; 3B7A2ED2878BC8F4 CRC64;
MTENHESHVF DPVTPDSPET AVPEVPGAQA AGCPVAHGRA PHPTQGGGNR QWWPDRLNLK
ILAKNPAVAN PLGGDFDYAA AFRGLDLPAV KRDIAEVLTT SQDWWPADFG NYGPLMIRMA
WHSAGTYRIS DGRGGAGAGQ QRFAPLNSWP DNGNLDKARR LLWPVKKKYG QALSWADLLI
LTGNVALETM GFKTFGFAGG REDVWESEED VYWGPETTWL DDERYTGDRE LENPLGAVQM
GLIYVNPEGP NGNPDPVAAA RDIRETFRRM AMNDEETVAL IAGGHTFGKT HGAGPAESVG
ADPEGAPLEE QGLGWRSSYR SGKGGDAITS GLEVTWTSTP TRWGNEFFHN LFAYEYELTK
SPAGAHQWIA KDAEATIPDA HDASKKQKPQ MLTTDLSLRF DPAYEQISRR FHENPEEFAD
AFARAWYKLT HRDMGPVQRY LGPEVPSEVL LWQDPLPART GEPLDAAEIA ALKEQVLATD
LTVAQLVSAA WASAASFRGS DKRGGANGAR VRLEPQRGWE ANDPDELAQV LRALEGVKES
FDAKGGKQVS LADLIVLAGG AAVEQAAKDA GVEVEVPFTP GRVDAAQDQT DVESFAALEP
AYDGFRNYVG KAARLPAEYL LLDRANLLTL SAPETTVLVG GLRVLGANTG GSKHGVLTDR
PGTLTNDFFV NLLDLGITWK STSSAQDEFE ARDASGKVKW TGTRADLVFG SNSELRALAE
VYAGDDARQK FVTDFVAAWS KVMDLDRFDL V
