CATA_CAVPO
ID CATA_CAVPO Reviewed; 527 AA.
AC Q64405; Q9QZ51;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=CAT;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Pinteric M., Baumgart E., Bulitta C., Fahimi D., Voelkl A.;
RT "Molecular characterization of guinea pig catalase.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-138.
RC STRAIN=Hartley; TISSUE=Lung;
RX PubMed=8597602; DOI=10.1016/0167-4781(95)00214-6;
RA Yuan H.T., Bingle C.D., Kelly F.J.;
RT "Differential patterns of antioxidant enzyme mRNA expression in guinea pig
RT lung and liver during development.";
RL Biochim. Biophys. Acta 1305:163-171(1996).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC Promotes growth of cells.
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; AJ005111; CAB57222.1; -; mRNA.
DR EMBL; U39841; AAC52717.1; -; mRNA.
DR RefSeq; NP_001166396.1; NM_001172925.1.
DR AlphaFoldDB; Q64405; -.
DR SMR; Q64405; -.
DR STRING; 10141.ENSCPOP00000011320; -.
DR GeneID; 100135492; -.
DR KEGG; cpoc:100135492; -.
DR CTD; 847; -.
DR eggNOG; KOG0047; Eukaryota.
DR InParanoid; Q64405; -.
DR OrthoDB; 507937at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
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:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051781; P:positive regulation of cell division; 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 Acetylation; Heme; Hydrogen peroxide; Iron; Metal-binding; Mitogen; NADP;
KW Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P04040"
FT CHAIN 2..527
FT /note="Catalase"
FT /id="PRO_0000084900"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P04040"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04040"
FT MOD_RES 13
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 221
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 306
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 306
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 480
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 480
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 499
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 511
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04040"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04040"
FT MOD_RES 522
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT CONFLICT 9
FT /note="Missing (in Ref. 2; AAC52717)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="A -> G (in Ref. 2; AAC52717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 59934 MW; 7C53CDD76255F9A8 CRC64;
MADSRDPASD QMKHWKEERA AQKPDVLTTA GGNPVGDKLN IMTVGPRGPL LVQDVVFTDE
MAHFDRERIP ERVVHAKGAG AFAYFEVTHD ITKYCKAKVF EHIGKKTPIA VRFSTVAGES
GSADTVRDPR GFAVKFYTEE GIWDLVGNNT PIFFIRDALL FPSFIHSQKR NPQTHLKDPD
MMWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNGSGEAV YCKFHYKTDQ
GIKNLSVEDA ARLSQEDPDY GLRDLFNAIA TGNYPSWTLY IQVMTFQQAQ SFPFNPFDLT
KIWPHKDYPL IPVGKLVLNR NPVNYFAEVE QIAFDPSNMP PGIEPSPDKM LQGRLFAYPD
THRHRLGPNY LQIPVNCPYR TRVANYQRDG PMCVTDNQGG APNYYPNSFS APVEQRQALE
HTSRCSGDVG RYNSTDDDNV TQVRAFYTQV LNEEQRRRLC ENIAGHLKDA QLFIQKKAVK
NFMDVHPDYG NRIQTLLDKY NVEKPKNAIH TFVQDGSHLS AKEKANL
