CATA_DANRE
ID CATA_DANRE Reviewed; 526 AA.
AC Q9PT92; Q9I8V5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=cat;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10888504; DOI=10.1021/jf990838+;
RA Ken C.F., Lin C.T., Wu J.L., Shaw J.F.;
RT "Cloning and expression of a cDNA coding for catalase from zebrafish (Danio
RT rerio).";
RL J. Agric. Food Chem. 48:2092-2096(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11281262; DOI=10.1016/s0305-0491(00)00285-6;
RA Gerhard G.S., Kauffman E.J., Grundy M.A.;
RT "Molecular cloning and sequence analysis of the Danio rerio catalase
RT gene.";
RL Comp. Biochem. Physiol. 127B:447-457(2000).
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; AJ007505; CAB64949.1; -; mRNA.
DR EMBL; AF170069; AAF89686.1; -; mRNA.
DR AlphaFoldDB; Q9PT92; -.
DR SMR; Q9PT92; -.
DR STRING; 7955.ENSDARP00000013402; -.
DR PaxDb; Q9PT92; -.
DR ZFIN; ZDB-GENE-000210-20; cat.
DR eggNOG; KOG0047; Eukaryota.
DR InParanoid; Q9PT92; -.
DR PhylomeDB; Q9PT92; -.
DR Reactome; R-DRE-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR Reactome; R-DRE-9033241; Peroxisomal protein import.
DR PRO; PR:Q9PT92; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0046688; P:response to copper ion; IDA:ZFIN.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..526
FT /note="Catalase"
FT /id="PRO_0000084906"
FT REGION 1..29
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"
FT CONFLICT 110
FT /note="V -> A (in Ref. 2; AAF89686)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="P -> S (in Ref. 2; AAF89686)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="T -> I (in Ref. 2; AAF89686)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="S -> F (in Ref. 2; AAF89686)"
FT /evidence="ECO:0000305"
FT CONFLICT 350..352
FT /note="MLQ -> NAA (in Ref. 2; AAF89686)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="M -> T (in Ref. 2; AAF89686)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 59654 MW; E1120D3796522785 CRC64;
MADDREKSTD QMKLWKEGRG SQRPDVLTTG AGVPIGDKLN AMTAGPRGPL LVQDVVFTDE
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EHVGKTTPIV VRFSTVAGEA
GSPDTVRDPR GFAVKFYTDE GNWDLTGNNT PTFFIRDTLL SPSFIHSQKR NPQTHLKDPD
MVWDFWSLRP ESLHQVSFLF SDRGIPDGYR HMNGYGSHTF KLVNAQGQPV YCKFHYKTNQ
GIKNIPVEEA DRLAATDPDY SIRDLYNAIA NGNFPSWTFY IQVMTFEQAE NWKWNPFDLT
KVWSHKEFPL IPVGRFVLNR NPVNYFAEVE QLAFDPSNMP PGIEPSPDKM LQGRLFSYPD
THRHRLGANY LQLPVNCPYR TRVANYQRDG PMCMHDNQGG APNYYPNSFS APDVQPRFLE
SKCKVSPDVA RYNSADDDNV TQVRTFFTQV LNEAERERLC QNMAGHLKGA QLFIQKRMVQ
NLMAVHSDYG NRVQALLDKH NAEGKKNTVH VYSRGGASAV AAASKM
