CATA_ASPFU
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 03-AUG-2022, entry version 138.
DE RecName: Full=Catalase A;
DE EC=1.11.1.6;
DE AltName: Full=Fast catalase;
GN Name=catA; ORFNames=AFUA_6G03890;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
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 / Af293 / CBS 101355 / FGSC A1100;
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: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
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_742595.1.
DR AlphaFoldDB; P78574; -.
DR SMR; P78574; -.
DR STRING; 746128.CADAFUBP00009176; -.
DR PeroxiBase; 5205; AfumKat01.
DR SwissPalm; P78574; -.
DR EnsemblFungi; EAL85650; EAL85650; AFUA_6G03890.
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; VMWQMSD; -.
DR OrthoDB; 507937at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
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 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 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW 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"
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
