CATA_ONCVE
ID CATA_ONCVE Reviewed; 482 AA.
AC Q27710; O85499;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=cat;
OS Onchocerca volvulus endobacterium.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=77551;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Henkle-Duehrsen K.J.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Henkle-Duehrsen K.J., Eckelt V.H.O., Wildenburg G., Blaxter M.L.,
RA Walter R.D.;
RT "Gene structure, activity and localization of a catalase from intracellular
RT bacteria in Onchocerca volvulus.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
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 -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; X82176; CAA57666.1; -; mRNA.
DR EMBL; AF069070; AAC79431.1; -; Genomic_DNA.
DR PIR; S49465; S49465.
DR AlphaFoldDB; Q27710; -.
DR SMR; Q27710; -.
DR PRIDE; Q27710; -.
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 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; PTHR11465; 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; SSF56634; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 2: Evidence at transcript level;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..482
FT /note="Catalase"
FT /id="PRO_0000084993"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 338
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 482 AA; 53700 MW; B1DA5F49BA39F776 CRC64;
MSQNKTLTTA SGPPVADNQN SRSAGPRGPL LLDDFHLIEK LAHFNRENIP ERRVHAKGSG
AYGTFTVTQD ITQYTSAKLF DSVGKQTPTF LRFSTVGGER GSADTERDPR GFALKFYTEE
GNWDIVGNNT PVFFIRDPLK FPDFIHTQKR LPQSNLKSAQ MMWDFWSHSP EALHQVTILF
SDRGIPDGYR HMHGFGSHTY SLINAKGERH WVKWHYKTKQ GIKNLAPADA ARLAGTDPDY
AQRDLFGAIE RGDFPKWRVC IQIMTEAQAN AHYENPFDVT KTWSQKEFPL IEVGELELNR
NPLNYFAEVE QAAFGPSNMV PGVGLSPDRM LQGRVFAYAD AHRYRVGTNH QQLPVNAPRS
PVNSYQRDGS MAFGSNGGAA PNYEPNSYAD APKQAPQYAE PALALSGAAD RYDHREDTDY
YSHAGALFRL MNDEQKALLI NNIAGAMAGV SSDVVQRQLQ YFFKADPAYG EGIASALGVS
LN