KATG_FRAP2
ID KATG_FRAP2 Reviewed; 739 AA.
AC B0TYQ6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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};
DE Flags: Precursor;
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Fphi_0203;
OS Francisella philomiragia subsp. philomiragia (strain ATCC 25017 / FSC 153 /
OS O#319-036).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=484022;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25017 / FSC 153 / O#319-036;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Richardson P.;
RT "Complete sequence of chromosome of Francisella philomiragia subsp.
RT philomiragia ATCC 25017.";
RL Submitted (DEC-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; CP000937; ABZ86421.1; -; Genomic_DNA.
DR RefSeq; WP_012279727.1; NC_010336.1.
DR AlphaFoldDB; B0TYQ6; -.
DR SMR; B0TYQ6; -.
DR STRING; 484022.Fphi_0203; -.
DR EnsemblBacteria; ABZ86421; ABZ86421; Fphi_0203.
DR KEGG; fph:Fphi_0203; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; EEIFWGP; -.
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 Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 24..739
FT /note="Catalase-peroxidase"
FT /id="PRO_5000309079"
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 262
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..221
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 247)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 221..247
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 100)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 739 AA; 82097 MW; CAC0FDA50FCB170B CRC64;
MLKKIVTALG MSGMLLAANS AIADDKNTEM ATPQSVDLSP LRNLNKLDSP MGKNYDYHQS
FKKLNTEELK KDMQDLLTQS QDWWPADFGN YGPFFIRLSW HDAGTYRLAD GRGGANRGQQ
RFSPLNSWPD NVNLDKARQL LWPIKQKYGD AVSWSDLIVL AGTVSLESMG MKPIGFAFGR
EDDWQGDDTN WGISPEQLMS SNVKDGKLAP AYAATQMGLI YVNPEGPDGK PDIKGAASEI
RQAFRAMGMT DKETVALIAG GHTFGKTHGA VPEKDIKKDI GPAPDKAPIE QQGLGWHNSY
GTGMGDDTMG SGLEGSWTST PTFWNHDFLH NLYNLNWEKT LSPSGAHQWT PTNAKPENMV
PDAHKPGVKH KPIMFTTDLA LKEDDGFNKY TQEFYNNPQE FKEEFAKAWF KLTHRDMGPK
SRYIGPWIPE QNFIWQDPVP VADYKQVSAQ DIAQLKQDII NSGLTNQQLI RTAWDSASTY
RKTDYRGGSN GARIALAPEK DWQMNEPAKL EVVLAKLKEI QTNFNNNKTD GTKVSLADLI
VLGGNVGVEQ AAKEAGYTIE IPFVPGRTDA TQAQTDIESF NYLKTKADGF VNYSDGSLAS
NKLPQALVEK ASMLNLNIPE MTVLVGGMRA LNVNYDDSQE GVFTKTPGQL NNNFFVNLLD
MSTKWEKSDT NSGEYIGIDR KTGAQKWTAT SVDLIFGSNS ELKAVAQVYA ENGNEQKFVN
DFAKAWHKVM MLGRFDVQE
