KATG_SYMTH
ID KATG_SYMTH Reviewed; 725 AA.
AC Q67LP5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=STH2416;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD41401.1; -; Genomic_DNA.
DR RefSeq; WP_011196539.1; NC_006177.1.
DR AlphaFoldDB; Q67LP5; -.
DR SMR; Q67LP5; -.
DR STRING; 292459.STH2416; -.
DR PeroxiBase; 2350; SthCP01_IAM14863.
DR EnsemblBacteria; BAD41401; BAD41401; STH2416.
DR KEGG; sth:STH2416; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_9; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000000417; 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..725
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354940"
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 252
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 85
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 88..211
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 237)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 211..237
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 88)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 725 AA; 81957 MW; 951B04CA6355A898 CRC64;
MREEDIRSTA GHGTSNKDWW PNQLNLRILH QHSEKANPMG PDFNYREEFK KLDYWALKED
LRKLMTESQD WWPADFGHYG PLIIRMAWHS AGTYRIQDGR GGAESGAQRF APLNSWPDNI
NLDKARRLLW PIKQKYGRRI SWADLMILAG NVALESMGLK TIGFAGGRAD VWEPEEDIYW
GSEQQWLGRD RFGEEGKLED PLAASEMGLI YVNPEGPGRE PDPLKAAQQI RETFKRMGMN
DEETVALIAG GHTFGKTHGA ASPSHLGPEP EAAPIEEMGL GWKNSYGTGK GGDTITSGLE
VTWTSSPTKW TSNFLWNLFG YEWELTKSPA GAWQWRPKNG AGEGTVPDAH DPNKRHAPGM
LTTDIALRVD PVYEKIARRF LENPDEFAKA FARAWFKLTH RDLGPRSRYL GPEVPEEEFI
WQDPLPKRDY DLIDEGDIAE LKKRIQASGM SIREMVMTAW ASASTFRGSD KRGGANGARI
RLAPQIGWEV NEPEQLRPVL ETLEGIQQEF NRSQTGRKRV SLADLIVLAG CVGIEQAARN
AGFEITVPFT PGRVDATQEQ TDVESFSYLE PVHDGFRNYL KRKFSVPAEH LLIDRANLLT
LTAPEMTVLI GGLRVLDCNW GRTKHGVLTD RPGALTNDFF VNLLDMRWKW NATDDENVFE
GRDRATGELK WTATRVDLIF GSNAQLRAIA EVYASNDGQE KFVQDFVKAW TKVMNLDRFD
LLVKK
