(data stored in ACNUC7421 zone)

SWISSPROT: A2Q7Q4_ASPNC

ID   A2Q7Q4_ASPNC            Unreviewed;       727 AA.
AC   A2Q7Q4;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 81.
DE   RecName: Full=Catalase {ECO:0000256|PIRNR:PIRNR038927};
DE            EC=1.11.1.6 {ECO:0000256|PIRNR:PIRNR038927};
GN   ORFNames=An01g01550 {ECO:0000313|EMBL:CAK43527.1};
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:CAK43527.1, 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: 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   -!- 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}.
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DR   EMBL; AM269954; CAK43527.1; -; Genomic_DNA.
DR   RefSeq; XP_001388595.1; XM_001388558.2.
DR   PeroxiBase; 5301; AnKat02.
DR   PaxDb; A2Q7Q4; -.
DR   EnsemblFungi; CAK43527; CAK43527; An01g01550.
DR   GeneID; 4978376; -.
DR   KEGG; ang:ANI_1_2270014; -.
DR   HOGENOM; HOG000087851; -.
DR   KO; K03781; -.
DR   Proteomes; UP000006706; Chromosome 2R.
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   Gene3D; 2.40.180.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR018028; Catalase.
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; SSF56634; SSF56634; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q7Q4.
DR   SWISS-2DPAGE; A2Q7Q4.
KW   Heme {ECO:0000256|PIRNR:PIRNR038927};
KW   Hydrogen peroxide {ECO:0000256|PIRNR:PIRNR038927};
KW   Iron {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|PIRSR:PIRSR038927-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000313|EMBL:CAK43527.1};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927, ECO:0000313|EMBL:CAK43527.1}.
FT   DOMAIN          53..440
FT                   /note="Catalase"
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   METAL           386
FT                   /note="Iron (heme axial ligand)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-2"
SQ   SEQUENCE   727 AA;  80216 MW;  E75B128E315FD002 CRC64;
     MRPIGLVGLI GLANAACPYM SRDLSARDSS DASESTEEFL SQYYLNDNNT YLTSDVGGPI
     EDQNSLSAGE RGPTLLEDFI FRQKIQRFDH ERVPERAVHA RGVGAHGVFV SYGDFSNLTA
     ASFLSEQGKE TPMFVRFSTV AGSRGSTDLA RDVHGFATRF YTDEGNFDLV GNNIPVFFIQ
     DAIQFPDLIH AVKPRGDSEI PQAATAHDSA WDFFSQQPSA LHTLFWAMAG HGIPRSFRHV
     DGFGVHTYRL VTDSGASKLV KFHWKSLQGK ASMVWEEAQQ VSGKNSDFMR QDLWTSIEYG
     RYPEWELGVQ IMDEEDQLRF GFDLFDPTKI VPEEYVPITK LGKMTLNRNP LNYFAETEQV
     MFQPGHIVRG VDFTEDPLLQ GRLFSYLDTQ LNRHGGPNFE QLPINQPRVP IHNNNRDGAG
     QMYIPLNPNA YSPNTLNSAS PKQANQTTGN GFFTSPGRTT SGHLLRSTSP TFQDVWSQPR
     LFYNSLVPTE QQFLIDAIRF ETSNVKSTTV RQNVIIQLNR ISNDLARRVA RAIDVPAPDP
     DPTYYHDNKT ADVGTFGTKL KKLSNLRVGF LASVQTPSSI TAAQDLATEL KDDEVDVVVV
     AERLTDGVDQ TYSASDAIQF DAVVVAPGAE GLFASGSVTA PQLNSTASAV STLYPAGRPL
     QVLVDAFRFG KTVGAVGSGK GALQNAGIDD EREGVVVGQT IGADFVDSVR EGLRTFRFLD
     RFALDEE
//

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