ID   KATG_VIBC1              Reviewed;         726 AA.
AC   A7MZ01;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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};
GN   OrderedLocusNames=VIBHAR_01773;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-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; CP000789; ABU70742.1; -; Genomic_DNA.
DR   RefSeq; WP_012127584.1; NC_022269.1.
DR   AlphaFoldDB; A7MZ01; -.
DR   SMR; A7MZ01; -.
DR   EnsemblBacteria; ABU70742; ABU70742; VIBHAR_01773.
DR   KEGG; vha:VIBHAR_01773; -.
DR   PATRIC; fig|338187.25.peg.904; -.
DR   OMA; MILAGNC; -.
DR   OrthoDB; 49441at2; -.
DR   Proteomes; UP000008152; Chromosome I.
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   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; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN           1..726
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354949"
FT   ACT_SITE        97
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         265
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            93
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        96..224
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   250)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        224..250
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   96)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   726 AA;  81628 MW;  B9329E51C0E17E3B CRC64;
     MSDKNHHSKC PVIHGANTNQ QASEFNWWPK SLNLEILHQH DHKTDPMGAD FNYADAFNSL
     DFEEVKKDLK DLMTDSQDWW PADWGHYGGL MIRMAWHSAG TYRIADGRGG ASRGNQRFAP
     LNSWPDNGNL DKARRLLWPI KRKYGNKLSW ADLMILAGNM AYESMGFKTF GFAGGREDIW
     HPEKDIYWGA EKEWLQPSGG ENNRYSGERD LENPLAAVMM GLIYVNPEGV DGKPDPLKTA
     HDMRVTFARM AMNDEETVAL TAGGHTVGKA HGNGDASVLE PEPEGAEIED QGFGWLNKTS
     RGIGRDTVTS GVEGAWTTHP TKWDNGYFHL LFTYDWEITK SPAGAAQWEP IDIKEEDMPV
     DVEDSSIRHN PMMTDADMAL KYDPEYRKIA ERFRDNPKEF EDCFARAWFK LTHRDLGPKS
     RYLGPDVPAE DLIWQDPVPP VSYYLSEDNI DALKMAILNS ELSIAELVST AWDSARTYRG
     SDRRGGANGA RIRLAPQKDW VGNEPERLQK VLNVLDEIRT MHHSPISMAD LIVLAGGVGI
     EKAASNAGMN ISVPFSQGRG DATDVMTDAE SFDVLEPIHD GFRNWLKSDY VVTAEELLLE
     RSQLMQLTAV EMTVLIGGMR VLGTNYGGTS QGVFTDNVGA LTNDFFVHLT DMSYTWHPAG
     DNQYEIRERA SGQTKWTASR VDLVFGSNSV LRSYAEVYAQ DDNKEKFVQD FVAAWVKVMN
     NDRFDL