CATA_GLARU
ID CATA_GLARU Reviewed; 528 AA.
AC Q9PWF7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=cat;
OS Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Glandirana.
OX NCBI_TaxID=8410;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Kubo H., Kashiwagi A.;
RT "cDNA sequence of Rana rugosa liver catalase.";
RL Submitted (AUG-1999) 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 -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; AB031872; BAA83685.1; -; mRNA.
DR AlphaFoldDB; Q9PWF7; -.
DR SMR; Q9PWF7; -.
DR PeroxiBase; 5274; RrugKat01.
DR PRIDE; Q9PWF7; -.
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; NADP; Oxidoreductase;
KW Peroxidase; Peroxisome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..528
FT /note="Catalase"
FT /id="PRO_0000084907"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 358
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 528 AA; 60251 MW; B02C073C5B13BB06 CRC64;
MADRREKSAD QMKLWKESRA NQKPDVLTTG GGNPVSDKLN LLTVGPRGPL LVQDVVFTDE
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EFIGKRTPIA VRFSTVAGEA
GSADTVRDPR GFAVKFYTED GNWDLTGNNT PIFFVRDAML FPSFIHSQKR NPQTHMKDPD
MVWDFWALRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNAKDEPI YCKFHFKTDQ
GIRNLTVEEA NRLSAEDPDY GIHDLYEAIA NGNYPSWTFY IQVMTFEQAE RYPFNPFDLT
KIWPHKDYPL IPVGKLVLNR NPANYFAEVE QIAFDPSNMP PGIEPSPDKM LQGRLFSYPD
THRHRLGANY LQLPVNCPYK ARVANYQRDG PMCFSDNQGG APNYFPNSFS APENQPAARE
SKFRVSADVA RYNSSDDDNV SQVRDFYTKV LSEEERKRLC ENIAGHLKGA QIFIQKRAVK
NFTDVHPDYG NRVQALLDKY NAEGHHKKVI KTYTQHSAHV TANDKANL