ID   CATA_DICDI              Reviewed;         496 AA.
AC   O77229; Q556B6; Q86A71;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   16-JUN-2009, entry version 52.
DE   RecName: Full=Catalase-A;
DE            EC=1.11.1.6;
GN   Name=catA; Synonyms=cat; ORFNames=DDB_G0274595;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=AX3;
RX   MEDLINE=20461835; PubMed=11004503; DOI=10.1016/S0167-4781(00)00063-4;
RA   Garcia M.X.U., Foote C., van Es S., Devreotes P.N., Alexander S.,
RA   Alexander H.;
RT   "Differential developmental expression and cell type specificity of
RT   Dictyostelium catalases and their response to oxidative stress and UV-
RT   light.";
RL   Biochim. Biophys. Acta 1492:295-310(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   MEDLINE=22092622; PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
RA   Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
RA   Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
RA   Platzer M., Rosenthal A., Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11782526;
RA   Garcia M.X.U., Roberts C., Alexander H., Stewart A.M., Harwood A.,
RA   Alexander S., Insall R.H.;
RT   "Methanol and acriflavine resistance in Dictyostelium are caused by
RT   loss of catalase.";
RL   Microbiology 148:333-340(2002).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen
CC       peroxide.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout growth and development.
CC       Exclusively localized in the prestalk cells.
CC   -!- DISRUPTION PHENOTYPE: Cells are resistant to methanol, acriflavine
CC       and thiabendazole.
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; AF090443; AAC36743.1; -; mRNA.
DR   EMBL; AC116986; AAO51894.1; -; Genomic_DNA.
DR   EMBL; AAFI02000012; EAL70190.1; -; Genomic_DNA.
DR   RefSeq; XP_643894.1; -.
DR   HSSP; P04040; 1DGF.
DR   PeroxiBase; 4096; DdKat01.
DR   GeneID; 3395200; -.
DR   KEGG; ddi:DDB_0185123; -.
DR   dictyBase; DDB_G0274595; catA.
DR   OMA; O77229; VEPANFA.
DR   BRENDA; 1.11.1.6; 424.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
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   Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase; Peroxisome.
FT   CHAIN         1    496       Catalase-A.
FT                                /FTId=PRO_0000084911.
FT   MOTIF       494    496       Microbody targeting signal (Potential).
FT   ACT_SITE     54     54       By similarity.
FT   ACT_SITE    128    128       By similarity.
FT   METAL       338    338       Iron (heme axial ligand) (By similarity).
FT   CONFLICT     67     67       P -> T (in Ref. 1; AAC36743).
SQ   SEQUENCE   496 AA;  55680 MW;  254CA4D38E698C9F CRC64;
     MSAPVLTTSS GSPIDNNLNS MTAGVNGPIL IQDFTLIDKL AHFDRERIPE RVVHAKGAGA
     HGYFEVPSSD VPKWCKAKFL NKVGKRTPIF TRFSTVGGEK GSSDSERDPR GFAVKFYTEE
     GNFDMVGNNT PVFFIRDPSK FPDFIHTQKR NPQTNCKDPN MFWDFLGQTP ESTHQVSILF
     SDRGTPKSYR HMHGFSSHTL KFVNAQGKPY WVKLHFTSET GIQNYTAEEA AKMSMNDPDS
     ATRDLFETIA KGGEPAWKVS IQLMEFEDAL KYRFNPFDVT KIWSHKDYPL IQIGRMVLNR
     NPENYFAEVE QAAFSPSHMV PGIEPSPDKM LQGRLFSYPD THRHRLGVNY QQIPVNCPFA
     VKGGVKNYQR DGFMAVNGNG GKGPNYQPNS FGGPEPHPEF AQHKFDVSGF AARQPYNHPN
     DDFVQPGDLY RLMSEDAKSR FVSNLVGHMS GVTIKEIQVR AVSNFYKADK DLGARLCKGL
     GIDVNDVIKF AARSNL
//