KATG_ALKHC
ID KATG_ALKHC Reviewed; 735 AA.
AC Q9KEE6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=BH0906;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB04625.1; -; Genomic_DNA.
DR PIR; B83763; B83763.
DR RefSeq; WP_010897079.1; NC_002570.2.
DR AlphaFoldDB; Q9KEE6; -.
DR SMR; Q9KEE6; -.
DR STRING; 272558.10173521; -.
DR PeroxiBase; 2372; BhaCP01_C-125.
DR EnsemblBacteria; BAB04625; BAB04625; BAB04625.
DR KEGG; bha:BH0906; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_9; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001258; 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..735
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354724"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 99
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 263
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 95
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 98..222
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 248)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 222..248
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 98)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 735 AA; 81531 MW; E93B4B5EBFA3A593 CRC64;
MDTNNTGKCP FHHGATTSPK SSGTTNNDWW PNALNLNILR QHDKKSNPMG EEFDYAEEFS
KLDYDALKQD VRDLMRDSQD WWPADFGHYG PFFIRMSWHA AGTYRIGDGR GGGGTGNQRF
APLNSWPDNG NLDKARRLLW PIKQKYGNKI SWADLLVLAG NVAIEDMGGP VIGFGAGRED
IWHPEEDIYW GSEKEWLTGD KRYSGDRELE NPLAAVEMGL IYVNPEGPDG KPDPIKAAHD
IRETFGRMGM NDEETVALIA GGHTFGKAHG AGNPDHVGPE PEAAPIEAQG LGWQNTYGSG
KGRDTITSGL EGAWTANPTQ WDNGFFDLLF GYEWWLTKSP AGAYQWQAVD PDEKDLAPDA
EDPSVKVPTV MLTTDLALRH DPEYEKISRR FHKNPDEFAD AFARAWFKLL HRDMGPKARY
LGPEVPAEDF IWQDPVPTVD YELTDAEVEE LKAKILDSGL TVSELVTTAW ASASTFRNSD
KRGGANGARI RLAPQKDWEV NQPEQLEKVL SVLENIQSQL DKKVSIADLI VLGGSAAVEK
AAKEAGFDVT VPFAPGRGDA TQEQTDVEGF AVLEPVSDGF RNYQKKEYSV SPEELLIDKA
QLLDLTAPEM TALIGGMRAL GANYGGTQHG VFTDCVGTLT NDFFVNLLDM GIEWKPVDYN
LYEGRDRKTG EVVRTATRVD LVFGSNSILR AIAEVYAQDD NKGKFVEDFI AAWVKVMNAD
RFDLKLNKKA QLTSK
