ID   CATA_ASPFU              Reviewed;         750 AA.
AC   P78574; Q4WD88;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   04-NOV-2026, entry version 151.
DE   RecName: Full=Catalase A;
DE            EC=1.11.1.6 {ECO:0000255|PROSITE-ProRule:PRU10013};
DE   AltName: Full=Fast catalase;
GN   Name=catA; ORFNames=AFUA_6G03890;
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Wysong D.R., Diamond R.D., Robbins P.W.;
RT   "Cloning, sequencing and characterization of Aspergillus fumigatus catalase
RT   genes.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2))
CC       generated by peroxisomal oxidases to water and oxygen, thereby
CC       protecting cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000250|UniProtKB:P04040}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = O2 + 2 H2O; 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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P15202};
CC   -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P15202}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; U87630; AAB47761.1; -; Genomic_DNA.
DR   EMBL; AAHF01000012; EAL85650.1; -; Genomic_DNA.
DR   RefSeq; XP_747688.1; XM_742595.2.
DR   AlphaFoldDB; P78574; -.
DR   SMR; P78574; -.
DR   STRING; 330879.P78574; -.
DR   PeroxiBase; 5205; AfumKat01.
DR   SwissPalm; P78574; -.
DR   EnsemblFungi; Afu6g03890-T; Afu6g03890-T-p1; Afu6g03890.
DR   GeneID; 3505035; -.
DR   KEGG; afm:AFUA_6G03890; -.
DR   VEuPathDB; FungiDB:Afu6g03890; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   HOGENOM; CLU_010645_3_0_1; -.
DR   InParanoid; P78574; -.
DR   OMA; AADHHYE; -.
DR   OrthoDB; 6880011at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
DR   GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:UniProtKB-ARBA.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR   CDD; cd03132; GATase1_catalase; 1.
DR   FunFam; 2.40.180.10:FF:000003; Catalase; 1.
DR   FunFam; 3.40.50.880:FF:000050; Catalase; 1.
DR   FunFam; 1.20.1370.20:FF:000001; Catalase HPII; 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:SF1; CATALASE-B; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 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; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Peroxisome; Reference proteome.
FT   CHAIN           1..750
FT                   /note="Catalase A"
FT                   /id="PRO_0000084915"
FT   REGION          30..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         380
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|UniProtKB:P04040"
FT   CONFLICT        328
FT                   /note="D -> N (in Ref. 1; AAB47761)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462
FT                   /note="S -> N (in Ref. 1; AAB47761)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        577
FT                   /note="F -> S (in Ref. 1; AAB47761)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        604..605
FT                   /note="DG -> T (in Ref. 1; AAB47761)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        681
FT                   /note="D -> H (in Ref. 1; AAB47761)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   750 AA;  84633 MW;  95AA8090D28BA007 CRC64;
     MATKIAGGLH RAQEVLQNTS SKSKKLVDLE RDTADAHTQQ PLTTDHGVRV SNTDQWLRVT
     NDRRTGPSLL EDQIAREKIH RFDHERIPER VVHARGTGAF GNFKLKESIE DLTYAGVLTD
     TSRNTPVFVR FSTVQGSRGS ADTVRDVRGF AVKFYTDEGN WDIVGNNIPV FFIQDAVKFP
     DFVHAVKPEP HNEVPQAQTA HNNFWDFVYL HPEATHMFMW AMSDRAIPRS YRMMQGFGVN
     TFALVNKEGK RHFVKFHWIP HLGVHSLVWD EALKLGGQDP DFHRKDLMEA IDNKAYPKWD
     FAIQVIPEEK QDDFEFDILD ATKIWPEDLV PLRVIGELEL NRNVDEFFPQ TEQVAFCTSH
     IVPGIDFTDD PLLQGRNFSY FDTQISRLGI NWEELPINRP VCPVLNHNRD GQMRHRITQG
     TVNYWPNRFE AVPPTGTKGS GVGGGFTTYP QRVEGIKNRA LSDKFREHHN QAQLFYNSMS
     EHEKLHMKKA FSFELDHCDD PTVYERLAGH RLAEIDLELA QKVAEMVGAP IPAKALKQNH
     GRRAPHLSQT EFIPKNPTIA SRRIAIIIGD GYDPVAFTGL KTAIKAASAL PFIIGTKRSA
     IYADGEDKTS SKGIIPDHHY DGQRSTMFDA TFIPGGPHVA TLRQNGQIKY WISETFGHLK
     ALGATGEAVD LVKETLSGTL DVQVASSQSP EPVEWYGVVT AGGKQKPESF KESVQILKGA
     TDFVGKFFYQ ISQHRNYQRE LDGLASTIAF
//