ID A0A2T5M1A0_9EURO Unreviewed; 721 AA.
AC A0A2T5M1A0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 03-MAY-2023, entry version 17.
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=P175DRAFT_0473087 {ECO:0000313|EMBL:PTU22311.1};
OS Aspergillus ochraceoroseus IBT 24754.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1392256 {ECO:0000313|EMBL:PTU22311.1, ECO:0000313|Proteomes:UP000244073};
RN [1] {ECO:0000313|EMBL:PTU22311.1, ECO:0000313|Proteomes:UP000244073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24754 {ECO:0000313|EMBL:PTU22311.1,
RC ECO:0000313|Proteomes:UP000244073};
RX PubMed=29317534; DOI=10.1073/pnas.1715954115;
RA Kaerboelling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S., Kuo A.,
RA Bowyer P., Matsuda Y., Mondo S., Lyhne E.K., Kogle M.E., Clum A.,
RA Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R.;
RT "Linking secondary metabolites to gene clusters through genome sequencing
RT of six diverse Aspergillus species.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E753-E761(2018).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|RuleBase:RU004142}.
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 ECO:0000256|RuleBase:RU000498};
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,
CC ECO:0000256|RuleBase:RU000498}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PTU22311.1}.
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DR EMBL; MSFN02000002; PTU22311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5M1A0; -.
DR VEuPathDB; FungiDB:P175DRAFT_0473087; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000244073; 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; 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; 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; PS00438; CATALASE_2; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..721
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015648300"
FT DOMAIN 53..440
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 99
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 172
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 386
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 721 AA; 79362 MW; 29863A6439D20F23 CRC64;
MAFQALSLVG LIGLANAVCP YMTGELSARD TNLDASEDFL SPYYLNDQDA FMTSDVGGPI
EDQFSLKAGE RGSTLLEDFI FRQKIQRFDH ERVPERAVHA RGAGAHGVFT SYGDFSNITA
ASFLGAKDKQ TPIFVRFSTV AGSRGSSDLA RDVHGFATRF YTDEGNFDIV GNNIPVFFIQ
DAIRFPDLIH AVKPRGDNEI PQAATAHDSA WDFFSQQPST MHTLFWAMAG HGIPRSFRHI
DGFGVHTFRF VTDAGASKLV KFHWKTLQGK ASLVWEEAQQ VSGKNADYQR QDLYEAIEAE
RYPEWELAVQ IMDEEDQLRF GFDLLDPTKI VPEEYVPLTK LGKMTLNRNP RNYFAETEQI
MFQPGHIIRG IDFTEDPLLQ GRLFSYLDTQ LNRNGGPNFE QLPINQPRVP VHNNNRDGAG
QMFIPLNPNA YTPNTLNQGA PKQANQTVGR GFFTAPDRAA SGHLVRALSS TFEDVWSQPR
LFFNSLVPAE QQFLINAIRF ETSNVASSIV RSNVVLQLNR ISNDLARRVA RVIGVEEPQP
DPTFYHHNVT TDVGAFGHKL QRLDGLKVGV LASVNVSASI ESASSLADQI SDDGVDVIVV
AERLVNGVDQ TYSATDAIQF DAIIVAPGTE SLFGPHSATA PPNVGSTLYP AGRPLQILID
GFRFGKPVGA LGSGSVALGN SGISESRDGV YVAQSVTDAF VGDIKDGLRT FKFLDRFPVD
Q
//
