ID   CATA_BACFR              Reviewed;         486 AA.
AC   P45737;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 131.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; Synonyms=katB; OrderedLocusNames=BF1245;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
OC   Bacteroidaceae; Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20.
RC   STRAIN=638;
RX   PubMed=7768808; DOI=10.1128/jb.177.11.3111-3119.1995;
RA   Rocha E.R., Smith C.J.;
RT   "Biochemical and genetic analyses of a catalase from the anaerobic
RT   bacterium Bacteroides fragilis.";
RL   J. Bacteriol. 177:3111-3119(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide. May be
CC       involved in aerotolerance of B.fragilis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = O2 + 2 H2O; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- SUBUNIT: Homodimer.
CC   -!- INDUCTION: Up-regulated by oxygenation and stationary phase.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U18676; AAC43384.1; -; Genomic_DNA.
DR   EMBL; AP006841; BAD47995.1; -; Genomic_DNA.
DR   PIR; A57262; A57262.
DR   RefSeq; WP_005785885.1; NC_006347.1.
DR   AlphaFoldDB; P45737; -.
DR   SMR; P45737; -.
DR   STRING; 295405.BF1245; -.
DR   GeneID; 60369098; -.
DR   KEGG; bfr:BF1245; -.
DR   PATRIC; fig|295405.11.peg.1232; -.
DR   HOGENOM; CLU_010645_2_0_10; -.
DR   OrthoDB; 9760293at2; -.
DR   SABIO-RK; P45737; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:InterPro.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:TreeGrafter.
DR   CDD; cd08156; catalase_clade_3; 1.
DR   FunFam; 2.40.180.10:FF:000001; Catalase; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF61; CATALASE; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase.
FT   CHAIN           1..486
FT                   /note="Catalase"
FT                   /id="PRO_0000084976"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         337
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   486 AA;  55906 MW;  4F28A24ED9B9A966 CRC64;
     MENKKLTAAN GRPIADNQNS QTAGPRGPIM LQDPWLIEKL AHFDREVIPE RRMHAKGSGA
     YGTFTVTHDI TKYTRAAIFS QVGKQTECFV RFSTVAGERG AADAERDIRG FAMKFYTEEG
     NWDLVGNNTP VFFLRDPLKF PDLNHAVKRD PRNNMRSANN NWDFWTLLPE ALHQVTITMS
     PRGIPASYRH MHGFGSHTYS FLNAENKRIW VKFHLKTMQG IKNLTDQEAE AIIAKDRESH
     QRDLYESIER GDFPKWKFQI QLMTEEEADN YRINPFDLTK VWPHKDFPLQ DVGILELNRN
     PENYFAEVEQ SAFNPMNIVE GIGFSPDKML QGRLFSYGDA QRYRLGVNSE QIPVNKPRCP
     FHAFHRDGAM RVDGNYGSAK GYEPNSYGEW QDSPEKKEPP LKVHGDVFNY NEREYDDDYY
     SQPGDLFRLM PADEQQLLFE NTARAMGDAE LFIKQRHVRN CYKADPAYGT GVAQALGIDL
     EEALKE
//