(data stored in SCRATCH zone)

SWISSPROT: A2Q7T0_ASPNC

ID   A2Q7T0_ASPNC            Unreviewed;       730 AA.
AC   A2Q7T0;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 92.
DE   RecName: Full=Catalase {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
GN   Name=catR {ECO:0000313|EMBL:CAK43553.1};
GN   ORFNames=An01g01820 {ECO:0000313|EMBL:CAK43553.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK43553.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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|PIRNR:PIRNR038927,
CC         ECO:0000256|PIRSR:PIRSR038927-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; AM269954; CAK43553.1; -; Genomic_DNA.
DR   RefSeq; XP_001388621.1; XM_001388584.2.
DR   SMR; A2Q7T0; -.
DR   PeroxiBase; 5302; AnKat04.
DR   PaxDb; A2Q7T0; -.
DR   EnsemblFungi; CAK43553; CAK43553; An01g01820.
DR   GeneID; 4978057; -.
DR   KEGG; ang:ANI_1_2296014; -.
DR   HOGENOM; HOG000087851; -.
DR   KO; K03781; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0005777; C:peroxisome; IDA:AspGD.
DR   GO; GO:0004096; F:catalase activity; IMP:AspGD.
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   Gene3D; 2.40.180.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR037060; Catalase_core_sf.
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   Pfam; PF18011; Catalase_C; 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;
DR   PRODOM; A2Q7T0.
DR   SWISS-2DPAGE; A2Q7T0.
KW   Heme {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
KW   Hydrogen peroxide {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2,
KW   ECO:0000256|RuleBase:RU000498};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|PIRSR:PIRSR038927-2, ECO:0000256|RuleBase:RU000498};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498, ECO:0000313|EMBL:CAK43553.1};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498,
KW   ECO:0000313|EMBL:CAK43553.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..730
FT                   /note="Catalase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002644029"
FT   DOMAIN          59..446
FT                   /note="Catalase"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          403..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           392
FT                   /note="Iron (heme axial ligand)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-2"
SQ   SEQUENCE   730 AA;  80496 MW;  6905E59B7A6CED89 CRC64;
     MRHFWLLPAV AGIAGAQCPY LSGEMSFTQE QDNAGDTIEV TEQPIDNTLY VNDTGSYMTT
     DFGTPISDQT SLKAGPRGPT LLEDFIFRQK LQRFDHERVP ERVVHARGAG AYGTFKSYAD
     WSNVTAADFL SANDKETPMF CRFSTVVGFR GSVDTARDVH GHACQFYTDE GNYDIVGINF
     APFFIQDAIQ FPDLVHAIKP MPNNEIPQAA TAHTSAWDFF SQQSTALHSA LWLMSGNGIP
     RSFRHMNGYG VHSFRFVAAN GTSKVVRYRW KSQQGVASLV WDEAQAAAGK NSDYHRQDLY
     NAIANGHYPK YELQAQIMDE ADMLRFGFDL LDPTKLVPEE VVPYTPLGMM ELNANPTNYF
     AEVEQAGFQP GHVVPGIDFT DDPLLQGRLF SYLDTQLTRH GGPNFEQIPV NRPRKPVHNN
     NRDGFGQQQI PTNNWAYTPN SMSNGYPMQA NQTQGHGFFT APYRYASGHL VRQTSPTFND
     HWSQPAMFWN SLIPAEQQMV VNAIVFQNSK VNSPHVRKNV VNQLNMVNNN LAVRVARGLG
     LDEPSPNPTY YTSNKTSNVG TFGKPLLSIE GLQVGFLASN SHPESIKQGQ AMAAQFSAAG
     VDLNIVSEAY ADGVNTTYAL SDAIDFDALI IADGVQSLFA SPALANQMNS TATSTLYPPA
     RPFQILVDSF RYGKPVAAVG SGSVALKNAG IDSSRSGVYT GSSETTEKIA KEVLEGLYTF
     RFVDRFALDE
//

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