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 27-MAR-2024, entry version 123.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=katA; Synonyms=katB; OrderedLocusNames=BF1245;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC 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 = 2 H2O + O2; 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}.
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DR EMBL; U18676; AAC43384.1; -; Genomic_DNA.
DR EMBL; AP006841; BAD47995.1; -; Genomic_DNA.
DR PIR; A57262; A57262.
DR RefSeq; WP_005785885.1; NZ_UYXF01000002.1.
DR RefSeq; YP_098529.1; NC_006347.1.
DR AlphaFoldDB; P45737; -.
DR SMR; P45737; -.
DR STRING; 295405.BF1245; -.
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 Proteomes; UP000002197; Chromosome.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
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 CDD; cd08156; catalase_clade_3; 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 COMPBIAS 12..26
FT /note="Polar residues"
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
//
