CATB_DICDI
ID CATB_DICDI Reviewed; 692 AA.
AC Q55DH8; Q6TWC1; Q9U6L8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Catalase-B;
DE EC=1.11.1.6;
GN Name=catB; ORFNames=DDB_G0269108;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY SRFA.
RC STRAIN=AX4;
RX PubMed=15075287; DOI=10.1128/ec.3.2.564-566.2004;
RA Escalante R., Iranfar N., Sastre L., Loomis W.F.;
RT "Identification of genes dependent on the MADS box transcription factor
RT SrfA in Dictyostelium discoideum development.";
RL Eukaryot. Cell 3:564-566(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 166-692, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX3-1;
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 [4]
RP DEVELOPMENTAL STAGE.
RC STRAIN=NC-4;
RX PubMed=11553701; DOI=10.1091/mbc.12.9.2590;
RA Iranfar N., Fuller D., Sasik R., Hwa T., Laub M., Loomis W.F.;
RT "Expression patterns of cell-type-specific genes in Dictyostelium.";
RL Mol. Biol. Cell 12:2590-2600(2001).
RN [5]
RP FUNCTION.
RC STRAIN=AX4;
RX PubMed=12788229; DOI=10.1016/s0167-4889(03)00064-8;
RA Garcia M.X.U., Alexander H., Mahadeo D., Cotter D.A., Alexander S.;
RT "The Dictyostelium discoideum prespore-specific catalase B functions to
RT control late development and to protect spore viability.";
RL Biochim. Biophys. Acta 1641:55-64(2003).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC Its accumulation in prespore cells affords the spores protection from
CC oxidation during prolonged dormancy. Required for normal developmental
CC timing, possibly through a regulatory role in differentiation and
CC morphogenesis. {ECO:0000269|PubMed:12788229}.
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 ECO:0000269|PubMed:11004503};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable. Still active after heating at 65 degrees Celsius for 15
CC minures.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11004503}.
CC -!- DEVELOPMENTAL STAGE: Expressed initially during formation of apical
CC tips in aggregates, accumulates rapidly during terminal cell
CC differentiation, and peaks at about 21 hours. Expressed only in
CC prespore cells. {ECO:0000269|PubMed:11004503,
CC ECO:0000269|PubMed:11553701}.
CC -!- INDUCTION: By srfA, in response to late development signals.
CC {ECO:0000269|PubMed:15075287}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ94087.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY386221; AAQ94087.1; ALT_INIT; Genomic_DNA.
DR EMBL; AAFI02000005; EAL71903.1; -; Genomic_DNA.
DR EMBL; AF183177; AAD55449.1; -; mRNA.
DR RefSeq; XP_646153.1; XM_641061.1.
DR AlphaFoldDB; Q55DH8; -.
DR SMR; Q55DH8; -.
DR STRING; 44689.DDB0191496; -.
DR PeroxiBase; 4098; DdKat02.
DR PaxDb; Q55DH8; -.
DR EnsemblProtists; EAL71903; EAL71903; DDB_G0269108.
DR GeneID; 8617104; -.
DR KEGG; ddi:DDB_G0269108; -.
DR dictyBase; DDB_G0269108; catB.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_3_0_1; -.
DR InParanoid; Q55DH8; -.
DR OMA; VMWQMSD; -.
DR PhylomeDB; Q55DH8; -.
DR PRO; PR:Q55DH8; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IDA: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:0006979; P:response to oxidative stress; IBA:GO_Central.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; PTHR42821; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; SSF52317; 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 1: Evidence at protein level;
KW Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Reference proteome.
FT CHAIN 1..692
FT /note="Catalase-B"
FT /id="PRO_0000328239"
FT ACT_SITE 69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 356
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"
SQ SEQUENCE 692 AA; 78033 MW; C3522F583364686A CRC64;
MNKKLEQLEK FKTNDKNPVY STTNTGVSLS DDANSLKAGP RGPTLLEDFV LREKITHFDH
ERIPERIVHA RGTGAHGYFL SYKDHSKLTK ADFLSKQDKK TPVFIRISTV QGPRGSADTV
RDVHGFAVKF YTDEGNYDLV GNNMPVFFIQ DASSFPDFVH AVKMEPQNEM PTGGSAHDTF
YDFCGLKPES AHSVLWVMSD RGIPISLRHQ QGFGVHSYRF INQEGKSTFV KLHWKPLSGT
CSLLWDEAQK IAGKDCDYHR RRFWEDIESG DFPQWELGAQ LLDEDLQKKF DFDILDPTKL
IPEELTPVIP LGRMVIDRNP DNFFAETEQV AFCVSHVVPG IDFSNDPLLQ GRIFSYLDTQ
LSRLGGPNFN EIPINRPVCP FANNQRDGIH RMTINKGGAS YFPNSIDKGY PLLKEPSANK
GGFRPYPENI SGTKSYDRSE TFEDHFSQAT MFWNSMSQHE KNHIIAAYTF EISKCSRPEV
RTRYVNNILV NIDSVLAEKV AKNLGVKIEP TSTKPIKKIM VKPSPALSQP NLLSGDIVSR
RISVIIEKGV DYDDVINFKD DMEKRGAMVM LVSSTLAQVE CSGGEMLSPK GTIIGNPSIF
FDAVYVPKST EEATKILSDD GNFLHYILEA FKHLKTIAFG GSVSVIKELL RLPQDHGLLL
GNGYKDITEQ FFYSLAHHRV WERESKVSKI PA
