ID   KATG_VIBVU              Reviewed;         723 AA.
AC   Q8D951;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=VV1_2755;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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; AE016795; AAO11099.1; -; Genomic_DNA.
DR   RefSeq; WP_011080593.1; NC_004459.3.
DR   AlphaFoldDB; Q8D951; -.
DR   SMR; Q8D951; -.
DR   PeroxiBase; 2651; VvuCP_CMPCP6.
DR   EnsemblBacteria; AAO11099; AAO11099; VV1_2755.
DR   KEGG; vvu:VV1_2755; -.
DR   HOGENOM; CLU_025424_2_0_6; -.
DR   OMA; MILAGNC; -.
DR   Proteomes; UP000002275; Chromosome 1.
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..723
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354952"
FT   ACT_SITE        99
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         267
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..226
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   252)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        226..252
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   98)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   723 AA;  80425 MW;  D714DD48FD7073FD CRC64;
     MEHKPTHTSG QCPVMHGGAT SSNSSNVAWW PKALNLDILH QHDRKSNPMG ADFSYREELK
     KLDVEALKRD LKTLMTDSQD WWPADWGHYG GLMIRMAWHS AGSYRVGDGR GGADTGNQRF
     APLNSWPDNA NLDKARRLLW PIKQKYGNKI SWADLMILAG NMAYESMGLK TFGFAFGRED
     IWHPEKDIYW GAEQEWLAPS GAENSRYSGE RDLENPLAAV MMGLIYVNPE GVDGNPDPLK
     TAKDMRVTFA RMGMNDEETV ALTAGGHTVG KAHGNGNAAN LGADPESADL EEQGLGWNNH
     KSRGIGRDTV TSGIEGAWTT NPTQWDNGFF HLLFSYDWWL QKSPAGAWQW EPVNIKEEDK
     PVDVEDPTIR HNPIMTDADM ALKLDPEYRK ISERFHKDPA YFSETFARAW FKLTHRDMGP
     KARYFGPDVP AETLIWQDPV PTGRKDYDVD AVKAKIIASG LSIGEMVSTA WDSARTFRNS
     DKRGGANGAR IRLAPQKDWL GNEPEKLAKV LNVLEAIASE FNISVADTIV LAGNVGVEQA
     AKAAGIAITV PFAAGRGDAT IEQTDVESFD VLEPIADGFR NWQKQHYAVN PEELLLDRAQ
     LLGLSAPEMT VLIGGLRVLG TNHGGTKHGV FTDNVGALSN DFFVNLTDMR YTWKPTGRNS
     YDIVERNSGN VKWTATRVDL VFGSNSILRA YAEVYAQDDN KEKFVKDFVA AWTKVMNADR
     FDI