ID   CATA_ASCSU              Reviewed;         541 AA.
AC   P90682;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=CAT;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Eckelt V.H.O.;
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to 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; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; Y10611; CAA71618.1; -; mRNA.
DR   AlphaFoldDB; P90682; -.
DR   SMR; P90682; -.
DR   PRIDE; P90682; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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;
KW   Peroxisome.
FT   CHAIN           1..541
FT                   /note="Catalase"
FT                   /id="PRO_0000084908"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         357
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   541 AA;  61962 MW;  70890E1AECA170B0 CRC64;
     MPQTKGKPHE EQLEQYKNSQ TKPFVLTTSN GAPIFNKKAS LTVGPRGPLL LQDVVFLDEM
     AHFDRERIPE RVVHAKGGGA HGFFEVTDDI TKYCKADVFS TIGKRTPIFI RFSTVGGELG
     SADTQRDPRG FAIKFYTEEG NWDLVGNNTP IFFIRDPIFF PNFIHTQKRN PVTHLKDPNM
     MWDFFSLRPE TTHQVMILFG DRGIPDGFRH MDGFGSHTFK LVNKDGNAVY CKFHIKTAQG
     IRNLPPDVAI KLAGEDPDYS IRDLYDSIEN GNYPVWRLMI QVMTFEEAAN YRFNPFDITK
     VWSHKEFPLI LVGKIVLNKN PTNYFAEVEQ IAFAPSHVVP GIEFSPDKML QGRLFAYPDT
     QFHRLGPNYV QLPINCPYRS RAHNTQRDGC FALDYNQGGM PTYHPNSFNG AIERTDVKES
     AWSVSGDVDR FNGDDEDNFS QPRDLWLKVM DETERARLVD NIADSLKYCK AFIQERAINN
     FTQVHQDFGN ALRNALQKAN EAMQKKREEE AEFNAKESVM MPCAIDDRMK NISNLAKYCK
     Y