KATG_HERSE
ID KATG_HERSE Reviewed; 748 AA.
AC A2RPW9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
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};
OS Herbaspirillum seropedicae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA de Oliveira Pedrosa F.;
RT "Genome sequence of the nitrogen fixing bacterium Herbaspirillum
RT seropedicae.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; AM490531; CAM32626.1; -; Genomic_DNA.
DR RefSeq; WP_013233264.1; NZ_JWZZ01000023.1.
DR AlphaFoldDB; A2RPW9; -.
DR SMR; A2RPW9; -.
DR KEGG; hsz:ACP92_06240; -.
DR PATRIC; fig|964.11.peg.1307; -.
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; 2.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..748
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354808"
FT REGION 194..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 283
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 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 91..242
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 268)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 242..268
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 91)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 748 AA; 81181 MW; 72B8D9B4CA803A63 CRC64;
MSNEAKCPFN HTAGSGTSNR DWWPKQLRVD LLAQHSSKSN PMGEDFDYAE AFKSLDLAAV
KADLAKVMTD SQDWWPADFG HYGPLFVRMA WHSAGTYRIG DGRGGAGRGQ QRFAPLNSWP
DNVNLDKARR LLWPVKQKYG NKISWADLLI LTGNVALETM GFKTFGFAGG RADVWEPDLD
VYWGTESTWL GGDDRYGKGK GSSSQGEIPA DAHRHGQEQA RTAPAGRNLE NPLAAVQMGL
IYVNPEGPEG NPDPLAAAHD IRETFARMAM DDEETVALIA GGHTFGKTHG AGDAKHVGRE
PEGEDMDSQG LGWKSSFGSG VGGDTISSGL EVTWTQTPAQ WSNYFFENLF KYEWELTKSP
AGAHQWVAKG ADAVIPHAHG GAPLLPTMLT TDLSLRFDPA YEKISRRFLE HPEQFADAFA
RAWFKLTHRD LGPRSRYLGP EVPAEELIWQ DPLPQAEGAQ IDAADVAALK AKVLGSGLSV
PELVATAWAS ASTFRGGDMR GGANGARIRL APQKDWAANQ PAQLAKVLKT LEGIQSAFNQ
GGKKVSLADL IVLAGSAAVE KAAQDAGVAV AVPFRAGRVD ASQEQTDAAS FAPLEPIVDG
FRNFQKQRYA VRGEDMLIDK AQQLTLSAPE MTVLVGGLRV LGNNVGGSTK GMFTDRVGVL
SNDFFVNLLD MATEWKSTSP AQEEFEGRDR KTGAVKWAGT RVDLVFGSNA VLRALAEVYA
SADAKEKFVK DFVAAWVKVM ELDRFDLK
