CATA_DICDI
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 03-AUG-2022, entry version 124.
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; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=AX3;
RX 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 PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA 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., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., 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., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., 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; DOI=10.1099/00221287-148-1-333;
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 loss of
RT 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 peroxide.
CC {ECO:0000269|PubMed:11782526}.
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 -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout growth and development.
CC Exclusively localized in the prestalk cells.
CC {ECO:0000269|PubMed:11004503}.
CC -!- DISRUPTION PHENOTYPE: Cells are resistant to methanol, acriflavine and
CC thiabendazole. {ECO:0000269|PubMed:11782526}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; AF090443; AAC36743.1; -; mRNA.
DR EMBL; AAFI02000012; EAL70190.1; -; Genomic_DNA.
DR RefSeq; XP_643894.1; XM_638802.1.
DR AlphaFoldDB; O77229; -.
DR SMR; O77229; -.
DR STRING; 44689.DDB0185123; -.
DR PeroxiBase; 4096; DdKat01.
DR PaxDb; O77229; -.
DR EnsemblProtists; EAL70190; EAL70190; DDB_G0274595.
DR GeneID; 8619320; -.
DR KEGG; ddi:DDB_G0274595; -.
DR dictyBase; DDB_G0274595; catA.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_2_0_1; -.
DR InParanoid; O77229; -.
DR OMA; WTCYVQV; -.
DR PhylomeDB; O77229; -.
DR Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-9033241; Peroxisomal protein import.
DR PRO; PR:O77229; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0004096; F:catalase activity; IDA:dictyBase.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:dictyBase.
DR GO; GO:1904643; P:response to curcumin; IDA:dictyBase.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0033986; P:response to methanol; IMP:dictyBase.
DR GO; GO:0006979; P:response to oxidative stress; IDA:dictyBase.
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 Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Peroxisome; Reference proteome.
FT CHAIN 1..496
FT /note="Catalase-A"
FT /id="PRO_0000084911"
FT MOTIF 494..496
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 338
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 CONFLICT 67
FT /note="P -> T (in Ref. 1; AAC36743)"
FT /evidence="ECO:0000305"
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
