KATG_GEOKA
ID KATG_GEOKA Reviewed; 736 AA.
AC Q5KZ91;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=GK1710;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(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; BA000043; BAD75995.1; -; Genomic_DNA.
DR RefSeq; WP_011231203.1; NC_006510.1.
DR AlphaFoldDB; Q5KZ91; -.
DR SMR; Q5KZ91; -.
DR STRING; 235909.GK1710; -.
DR PeroxiBase; 2370; GkaCP01_HTA426.
DR EnsemblBacteria; BAD75995; BAD75995; GK1710.
DR KEGG; gka:GK1710; -.
DR PATRIC; fig|235909.7.peg.1835; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_9; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000001172; 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..736
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354799"
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 264
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 97
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 100..223
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 249)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 223..249
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 100)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 736 AA; 83226 MW; 1ED9B5D025BFAE8C CRC64;
MKNQNQHNTS KCPYHGSVTS YNSNRTTNKD WWPNQLNLSI LHQHDRKTNP HDEEFNYAEE
FQKLDYWALK EDLRKLMTES QDWWPADYGH YGPLFIRMAW HSAGTYRIGD GRGGGSTGTQ
RFAPLNSWPD NANLDKARRL LWPIKKKYGN KISWADLMIL AGNVAIESMG GKTIGFGGGR
EDVWHPEEDI YWGAEKEWLA SERYSGDREL ENPLAAVQMG LIYVNPEGPD GKPDPVAAAR
DIRETFRRMG MNDEETVALI AGGHTFGKAH GAGPASHVGP EPEAAPIEAQ GLGWISSYGK
GKGRDTITSG IEGAWTPTPT QWDNSYFRLL FEYEWKLTKS PAGAYQWEAV NLREEDLAPD
AEDPNVKVPP MMMTTDLALR FDPEYEKIAR RFYENPEEFA DAFARAWFKL THRDMGPKTR
YLGPEVPKED FIWQDPIPTV DYELSDAEIE EIKAKILNSG LTVSELVKTA WASASTFRNS
DKRGGANGAR IRLAPQKDWE VNEPERLAKV LSVYEDIQRE LPKKVSIADL IVLGGSAAVE
KAARDAGFDV KVPFIPGRGD ATQEQTDVES FSVLEPFADG FRNYQKKEYS VGPEELLIDK
AQLLGLTAPE MTVLVGGLRV LGANYRDLPH GVFTDRIGVL TNDFFVNLVD MNYEWVPTEG
GIYEIRDRQT GEVRWTATRV DLIFGANSIL RSYAEFYAQD DNREKFVRDF INAWVKVMNA
DRFDIHLKQA KESVTV
