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Catalase-A (EC 1.11.1.6)

 CATA_DICDI              Reviewed;         496 AA.
O77229; Q556B6; Q86A71;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 2.
07-NOV-2018, entry version 109.
RecName: Full=Catalase-A;
EC=1.11.1.6;
Name=catA; Synonyms=cat; ORFNames=DDB_G0274595;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
STRAIN=AX3;
PubMed=11004503; DOI=10.1016/S0167-4781(00)00063-4;
Garcia M.X.U., Foote C., van Es S., Devreotes P.N., Alexander S.,
Alexander H.;
"Differential developmental expression and cell type specificity of
Dictyostelium catalases and their response to oxidative stress and UV-
light.";
Biochim. Biophys. Acta 1492:295-310(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=12097910; DOI=10.1038/nature00847;
Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
Platzer M., Rosenthal A., Noegel A.A.;
"Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
Nature 418:79-85(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11782526;
Garcia M.X.U., Roberts C., Alexander H., Stewart A.M., Harwood A.,
Alexander S., Insall R.H.;
"Methanol and acriflavine resistance in Dictyostelium are caused by
loss of catalase.";
Microbiology 148:333-340(2002).
-!- FUNCTION: Occurs in almost all aerobically respiring organisms and
serves to protect cells from the toxic effects of hydrogen
peroxide. {ECO:0000269|PubMed:11782526}.
-!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
{ECO:0000255|PROSITE-ProRule:PRU10013}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
-!- DEVELOPMENTAL STAGE: Expressed throughout growth and development.
Exclusively localized in the prestalk cells.
{ECO:0000269|PubMed:11004503}.
-!- DISRUPTION PHENOTYPE: Cells are resistant to methanol, acriflavine
and thiabendazole. {ECO:0000269|PubMed:11782526}.
-!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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EMBL; AF090443; AAC36743.1; -; mRNA.
EMBL; AAFI02000012; EAL70190.1; -; Genomic_DNA.
RefSeq; XP_643894.1; XM_638802.1.
ProteinModelPortal; O77229; -.
SMR; O77229; -.
STRING; 44689.DDB0185123; -.
PeroxiBase; 4096; DdKat01.
PaxDb; O77229; -.
PRIDE; O77229; -.
EnsemblProtists; EAL70190; EAL70190; DDB_G0274595.
GeneID; 8619320; -.
KEGG; ddi:DDB_G0274595; -.
dictyBase; DDB_G0274595; catA.
eggNOG; KOG0047; Eukaryota.
eggNOG; COG0753; LUCA.
InParanoid; O77229; -.
KO; K03781; -.
OMA; HADFGRM; -.
PhylomeDB; O77229; -.
Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-DDI-6798695; Neutrophil degranulation.
PRO; PR:O77229; -.
Proteomes; UP000002195; Chromosome 2.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005777; C:peroxisome; IDA:dictyBase.
GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
GO; GO:0004096; F:catalase activity; IDA:dictyBase.
GO; GO:0020037; F:heme binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:dictyBase.
GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
GO; GO:0033986; P:response to methanol; IMP:dictyBase.
GO; GO:0006979; P:response to oxidative stress; IMP:dictyBase.
Gene3D; 2.40.180.10; -; 1.
InterPro; IPR018028; Catalase.
InterPro; IPR024708; Catalase_AS.
InterPro; IPR024711; Catalase_clade1/3.
InterPro; IPR011614; Catalase_core.
InterPro; IPR037060; Catalase_core_sf.
InterPro; IPR002226; Catalase_haem_BS.
InterPro; IPR010582; Catalase_immune_responsive.
InterPro; IPR020835; Catalase_sf.
PANTHER; PTHR11465; PTHR11465; 1.
Pfam; PF00199; Catalase; 1.
Pfam; PF06628; Catalase-rel; 1.
PIRSF; PIRSF038928; Catalase_clade1-3; 1.
PRINTS; PR00067; CATALASE.
SMART; SM01060; Catalase; 1.
SUPFAM; SSF56634; SSF56634; 1.
PROSITE; PS00437; CATALASE_1; 1.
PROSITE; PS00438; CATALASE_2; 1.
PROSITE; PS51402; CATALASE_3; 1.
2: Evidence at transcript level;
Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding;
Oxidoreductase; Peroxidase; Peroxisome; Reference proteome.
CHAIN 1 496 Catalase-A.
/FTId=PRO_0000084911.
MOTIF 494 496 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 54 54 {ECO:0000255|PROSITE-ProRule:PRU10013}.
ACT_SITE 128 128 {ECO:0000255|PROSITE-ProRule:PRU10013}.
METAL 338 338 Iron (heme axial ligand). {ECO:0000250}.
CONFLICT 67 67 P -> T (in Ref. 1; AAC36743).
{ECO:0000305}.
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


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