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   25-NOV-2008, entry version 52.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricognathi; Caviidae; 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   MEDLINE=96180320; 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
RT   pig 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
CC       peroxide. Promotes growth of cells.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- COFACTOR: NADP (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome (By similarity).
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; AJ005111; CAB57222.1; -; mRNA.
DR   EMBL; U39841; AAC52717.1; -; mRNA.
DR   HSSP; P00432; 4BLC.
DR   SMR; Q64405; 5-501.
DR   HOVERGEN; Q64405; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR011614; Catalase_N.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PRINTS; PR00067; CATALASE.
DR   ProDom; PD000510; Catalase; 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; Mitogen; NADP;
KW   Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    527       Catalase.
FT                                /FTId=PRO_0000084900.
FT   ACT_SITE     75     75       By similarity.
FT   ACT_SITE    148    148       By similarity.
FT   METAL       358    358       Iron (heme axial ligand) (By similarity).
FT   MOD_RES     231    231       Phosphotyrosine (By similarity).
FT   MOD_RES     308    308       Phosphotyrosine (By similarity).
FT   MOD_RES     517    517       Phosphoserine (By similarity).
FT   CONFLICT      9      9       Missing (in Ref. 2; AAC52717).
FT   CONFLICT     83     83       A -> G (in Ref. 2; AAC52717).
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
//