ID J4ULC5_BEAB2 Unreviewed; 734 AA.
AC J4ULC5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN ORFNames=BBA_05603 {ECO:0000313|EMBL:EJP65272.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP65272.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP65272.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP65272.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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:0000256|PIRNR:PIRNR038927};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|PIRNR:PIRNR038927}.
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DR EMBL; JH725164; EJP65272.1; -; Genomic_DNA.
DR RefSeq; XP_008598922.1; XM_008600700.1.
DR AlphaFoldDB; J4ULC5; -.
DR STRING; 655819.J4ULC5; -.
DR GeneID; 19888615; -.
DR HOGENOM; CLU_010645_3_0_1; -.
DR InParanoid; J4ULC5; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
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; CATALASE; 1.
DR PANTHER; PTHR42821:SF3; CATALASE B; 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; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..734
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003780885"
FT DOMAIN 62..452
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 32..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 111
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 184
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 398
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:0000256|PIRSR:PIRSR038927-2"
SQ SEQUENCE 734 AA; 79972 MW; 7D99170DE393E0FC CRC64;
MVQLTTIAGA LCAIGLVSAQ CPYANPAYLS KREESVDATS NRDGSRGHMQ GYEVDDSSGF
LTSDVGGPFS DQESLKAGDR GPTLLEDFIF RQKITHFDHE RASSSPGDPV HARGAGAYGT
FTSYDDFGNI TAASFLGAKG KKTPMFVRFS TVLGSRGSTD TARDIRGFAT RFYTDEGNFD
IVGNNAPVFF IQDAIQFPDL VHALKPESKN EIPQASTAHD TAWDFFSQQT TALHAVFWAL
SGHGVPRSFR HMDGFGVHTY RLVTEKGDSK LVKWHWRSKQ GLASLYQEES QHITGKGADF
HRQDLYDAIE AGYYPEWELN VQIVDEDKAL AFGFDLLDPT KILPEELAPL HPLGVMRLDA
NPANYFAETE QVMFQPGHIV RGVDFSDDPL LQGRIFSYLD TQINRHGGPN FEQLPINRPI
ARVRNNNRDG AGQVFIHKNA APYSPNTLNN GSPLQADQST GRGFFTAPGR QAPGHLGRRR
SATFADHWSQ PRLFYNSLSK AEQQMLIDVL RLELSVLVQP GIRKNVLKQL NRISHDIARR
VGRALGTEDP PLPPDDHYYH DNTTAHMSAY GAAPLPTIAG LRVGVLVDSE SGASVAQGRA
VRDGLRAAKV FASTVGERTV EGVDRTLAAT DATVFDAVVV ADGTAALFEA GAGAAAARST
YYPPGRPGQI VTDSFHWGKP VGFLGTGKEA INRTGIKAGP GVYVGSDVES MVKNVKEGLA
TFKFLDRIAL DESE
//
