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 22-FEB-2023, entry version 84.
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 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 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:SF9; 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 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
//
