(data stored in ACNUC7421 zone)

SWISSPROT: KATG_ASPNC

ID   KATG_ASPNC              Reviewed;         762 AA.
AC   A2Q7T1;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 79.
DE   RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_03108};
DE            Short=CP {ECO:0000255|HAMAP-Rule:MF_03108};
DE            EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_03108};
DE   AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_03108};
GN   Name=katG {ECO:0000255|HAMAP-Rule:MF_03108}; ORFNames=An01g01830;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513;
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.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.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: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_03108}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03108};
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=1.11.1.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03108};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03108};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
CC       {ECO:0000255|HAMAP-Rule:MF_03108};
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_03108}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03108}.
CC   -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC       for the catalase, but not the peroxidase activity of the enzyme.
CC       {ECO:0000255|HAMAP-Rule:MF_03108}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03108}.
DR   EMBL; AM269954; CAK43554.1; -; Genomic_DNA.
DR   RefSeq; XP_001388622.1; XM_001388585.2.
DR   SMR; A2Q7T1; -.
DR   PeroxiBase; 5224; AnCP01.
DR   PaxDb; A2Q7T1; -.
DR   PRIDE; A2Q7T1; -.
DR   EnsemblFungi; CAK43554; CAK43554; An01g01830.
DR   GeneID; 4977099; -.
DR   KEGG; ang:ANI_1_228014; -.
DR   HOGENOM; HOG000218110; -.
DR   KO; K03782; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01961; Catal_peroxid; 1.
DR   InterPro; IPR000763; Catalase_peroxidase.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   PANTHER; PTHR30555; PTHR30555; 1.
DR   Pfam; PF00141; peroxidase; 2.
DR   PRINTS; PR00460; BPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 2.
DR   TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q7T1.
DR   SWISS-2DPAGE; A2Q7T1.
KW   Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase.
FT   CHAIN           1..762
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354101"
FT   ACT_SITE        97
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT   METAL           283
FT                   /note="Iron (heme axial ligand)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT   SITE            93
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT   CROSSLNK        96..242
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   268)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT   CROSSLNK        242..268
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   96)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
SQ   SEQUENCE   762 AA;  84251 MW;  373EFFF72FC82CDC CRC64;
     MAEAKCPFSQ SRSNANVAGG GTRNTDWWPD QLNLGILRQH APASNPFERD FDYTAAFNSL
     DYYALKKDLH ALMTDSQDWW PADFGHYGGL FIRMAWHSAG TYRVFDGRGG GGQGQQRFAP
     LNSWPDNASL DKARRLLWPI KQKYGAKISW ADLMLLAGNV ALESMGFKTY GFSGGRADTW
     EADESVYWGG ESTWMGNDVR YSDGFPGVTK HGALSGDEPP HRNIHTRDLE KPLAASHMGL
     IYVNPEGPDG NPDPVAAARD IRTTFGRMGM NDEETVALIA GGHSFGKTHG AASSENVDVE
     PAAAGLENQG LGWSNRYQSG KGPHTITSGI EVTWTKTPTK WSHAFLEYLF RFDWELTKSP
     GGANQWQAKN TEAIIPDAYD PSKKHLPKML TTDLSLRYDP AYEKIARRFL DHPDEFADAF
     SRAWFKLLHR DMGPRTRYIG PEAPTEDLIW QDPIPAVNHT LVDANDIAAL KRTILDTGLN
     KSNFVSTAWA SASTFRGTDK RGGANGARIR LAPQRQWEVN NQPWLEETLS ALEKIQKDFN
     DRVSSTGKKI SLADLIVLAG CAAVEKAAQE AGQTITVPFT PGRMDASQEQ TEVESFSHLE
     PVADGFRNYG KSSSRVRAEH YLVDKAHLLT LTAPEMTVLV GGLRVLNTNY DGSKHGVLTS
     SPGRLTNDFF TNVLDMNTAW KAKDGGRDLY EGTDRKTGQP KWTATRADLV FGSHAELRAL
     AEVYGSSDGQ EKFVKDFVSA WDKVMNLDRF DLKGSGIARS KL
//

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