ID   CATA_CALJA              Reviewed;         527 AA.
AC   Q2I6W4;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=CAT;
OS   Callithrix jacchus (Common marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Cebidae; Callitrichinae; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Atanasova S., von Ahsen N., Schlumbohm C., Wieland E., Oellerich M.,
RA   Armstrong V.;
RT   "Free radical scavenging enzymes in Callithrix jacchus.";
RL   Submitted (OCT-2005) 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
CC       peroxide. Promotes growth of cells (By similarity).
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; DQ241811; ABB71446.1; -; mRNA.
DR   SMR; Q2I6W4; 5-501.
DR   HOVERGEN; Q2I6W4; -.
DR   BRENDA; 1.11.1.6; 265156.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:EC.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0008283; P:cell proliferation; 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; IPR010582; Catalase-rel_immune_responsive.
DR   InterPro; IPR011614; Catalase_N.
DR   InterPro; IPR018028; Catalase_rel_subgroup.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 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_0000266027.
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     422    422       Phosphoserine (By similarity).
FT   MOD_RES     517    517       Phosphoserine (By similarity).
SQ   SEQUENCE   527 AA;  59800 MW;  437902E9E785C1EA CRC64;
     MADSRDPASD QMKHWKEQRA AQKADVLTTG AGNPVGDKLN VITAGPRGPL LVQDVVFTDE
     MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF EHIGKRTPIA VRFSTVAGES
     GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDPLL FPSFIHSQKR NPQTHLKHPD
     MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ
     GIKNLSVEDA ARLSQEDPDY GLRDLFNAIA TGNYPSWTFY IQVMTFSQAE TFPFNPFDVT
     KIWPHKDYPL IPVGKLVLNR NPVNYFAEVE QIAFDPSNMP PGIEASPDKM LQGRLFSYPD
     THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMQDNQGG APNYYPNSFG APEHQPSALE
     HSTRCSAEVQ RFNTANDDNV TQVRAFYVNV LNEEQRKRLC ENIAGHLKDA QLFIQKKAVK
     NFREVHNDYG TRIQALLDKY NAEKPKNAIH TFVQSGSHLA AREKANL
//