ID Q0IHE6_XENLA Unreviewed; 503 AA.
AC Q0IHE6;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN Name=cat.3.L {ECO:0000313|RefSeq:NP_001098738.1,
GN ECO:0000313|Xenbase:XB-GENE-22041689};
GN Synonyms=cat {ECO:0000313|Xenbase:XB-GENE-22041689}, cat.3
GN {ECO:0000313|Xenbase:XB-GENE-22041689}, LOC100125664
GN {ECO:0000313|EMBL:AAI23187.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAI23187.1};
RN [1] {ECO:0000313|RefSeq:NP_001098738.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI23187.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fat bodies {ECO:0000313|EMBL:AAI23187.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001098738.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|RuleBase:RU004142}.
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:0000256|ARBA:ARBA00000720,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000256|ARBA:ARBA00001937};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR EMBL; BC123186; AAI23187.1; -; mRNA.
DR RefSeq; NP_001098738.1; NM_001105268.1.
DR STRING; 8355.Q0IHE6; -.
DR PaxDb; 8355-Q0IHE6; -.
DR DNASU; 100125664; -.
DR GeneID; 100125664; -.
DR KEGG; xla:100125664; -.
DR AGR; Xenbase:XB-GENE-22041689; -.
DR CTD; 100125664; -.
DR Xenbase; XB-GENE-22041689; cat.3.L.
DR OMA; PNSYGRW; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 100125664; Expressed in zone of skin and 14 other cell types or tissues.
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 {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|RuleBase:RU000498};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038928-2}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000498};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT DOMAIN 10..395
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 57
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 130
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 340
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:0000256|PIRSR:PIRSR038928-2"
SQ SEQUENCE 503 AA; 57410 MW; 3FCFBCC1D692F714 CRC64;
MAQQTHPILT TGAGIPTGDK LNVLTAGPRG PMLMQDVVFT DEMAHFDRER IPERVVHAKG
AGAFGYFEVT HDITKYCRAK VFEKVGKRTD VAVRFSTVAG EAGSADTVRD PRGFAVKFYT
EEGIWDLVGN NIPIFFLRDP MMFPSFIHSQ KRNPQTHLKD PDTVWDFWSL RPETLHQVTF
LFSDRGIPDG HRHMNGYGSH TFKLVNAEGN AVYCKFHYKT DQGIKNLSVE EADRLVVSDP
DYGIRDLFQA IAKKNFPSWT MYIQVMTFEE AEKCPFNPFD LTKVWPHKDY PLIPIGKLVL
NRNPENYFAE VEQIAFDPSH MPPGIEASPD KMLQGRLFSY PDTHRYRLGP NYLHLPVNCP
RGVKVAHYQR DGPMCMFNTP SHMPNYYPNS FSSPRDDPKC KDSTFVASGD VDRHDCSDED
NVSQVRAFYT QTLTEEERQR LCENLARNLS EAQIFIQERA VKNFSNIHPD YGADIKALLD
KFNAEGGKKE TLHNYICHKA ARV
//
