ID A0A1L9SZR8_9EURO Unreviewed; 732 AA.
AC A0A1L9SZR8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=catalase {ECO:0000256|ARBA:ARBA00012314};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314};
GN ORFNames=ASPSYDRAFT_214330 {ECO:0000313|EMBL:OJJ52533.1};
OS Aspergillus sydowii CBS 593.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036612 {ECO:0000313|EMBL:OJJ52533.1, ECO:0000313|Proteomes:UP000184356};
RN [1] {ECO:0000313|Proteomes:UP000184356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 593.65 {ECO:0000313|Proteomes:UP000184356};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329}.
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DR EMBL; KV878601; OJJ52533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9SZR8; -.
DR STRING; 1036612.A0A1L9SZR8; -.
DR VEuPathDB; FungiDB:ASPSYDRAFT_214330; -.
DR OrthoDB; 5535879at2759; -.
DR Proteomes; UP000184356; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000184356}.
FT DOMAIN 39..424
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
SQ SEQUENCE 732 AA; 81797 MW; 3F5BDFFC33E9E555 CRC64;
MNHLAVARGP EDVADISDNQ KLLDLAEDTV DINAESNMTT DAGAPIPLKE QSIYDSSNQI
MVPLDAVEKI QHFNGERIPE RAVYARGTGA FGNFRLIQSA EDLTMAGILC DRSRTTPALA
RFSNLTGSAG SSDTSRDVRG FAVKMYTTEG NWDMLCQNIP VSAVRDGEAF SDFVHSIKPE
PHTGLSYGHL GHNNFWDFVT LHPESIHMAL WLMSDHGIPR SYRMMKAFGV NTFTMINKQG
KRHYVRFQWI PTLGTRFLHP EEAVRLAGHD PDYYRRDLRE SIASKCYPKW NLAIQAIPEV
ESGDMEFDIF DPTLLWPEGR VPLRIIGVLE LNHNVDEMFS QVEQAAFRPT NLVPGITISP
DPLLQYRALA YADAQARRVG SNVAELPVNR PCCPVLNHNR DGGMRLRITR GSVNYWPNRF
WACPPDSSCL QTSGESKGPK HKIHQTGASD DSVFNLDQVK TFITSLDDIE RRHITDNLAL
NLGYCDDPTV PEHFLDQHMV RIDQGIAQSI AEALGVELKG IHGAAEAKEH QRSHSNSLPA
VLNNHSRSLR IAIFVDNGYD KDDFEAGIST LQAAGCFTYI ISPTPAKVFH AGADPIHSTG
LRPDHSFLTR QSTEFDGLFV PGGVHIEELA RKHSVRSWIS ETFWHFKPIG VIGNAVEPVK
DALSTVSGIE LATDERKTVD WYGVVSTVEQ VRPYSVLDVA GSSTRSDFVG LFHARICERS
IREREREFRY LL
//
