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KATG_ASPCL
ID   KATG_ASPCL              Reviewed;         760 AA.
AC   A1C8R3;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=ACLA_044200;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR   EMBL; DS027046; EAW13700.1; -; Genomic_DNA.
DR   RefSeq; XP_001275126.1; XM_001275125.1.
DR   AlphaFoldDB; A1C8R3; -.
DR   SMR; A1C8R3; -.
DR   STRING; 5057.CADACLAP00004027; -.
DR   PRIDE; A1C8R3; -.
DR   EnsemblFungi; EAW13700; EAW13700; ACLA_044200.
DR   GeneID; 4707337; -.
DR   KEGG; act:ACLA_044200; -.
DR   VEuPathDB; FungiDB:ACLA_044200; -.
DR   eggNOG; ENOG502QTDY; Eukaryota.
DR   HOGENOM; CLU_025424_2_0_1; -.
DR   OMA; MILAGNC; -.
DR   OrthoDB; 352289at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
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;
KW   Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase; Reference proteome.
FT   CHAIN           1..760
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354098"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        97
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT   BINDING         283
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
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   760 AA;  83843 MW;  F4ED7671BC8562C4 CRC64;
     MAESKCPFKS QGSRSNVAGG GTRNTDWWPE QLKLNILRQH TTVTNPLGAD FDYAAAFNTL
     DYDALKKDLT ALMTDSQEWW PADFGHYGGL FIRMAWHSAG TYRVFDGRGG AGQGQQRFAP
     LNSWPDNVSL DKARRLLWPI KQKYGDKISW ADLMILTGNV ALESMGFKTF GFAGGRADTW
     EADESAYWGR ETTWLGNDAR YEKGFSGSDK QGTVIADEAS HKTTHSRELE NPLAAAHMGL
     IYVNPEGPDG NPDPVAAAHD IRVTFGRMAM NDEETVALIA GGHTFGKTHG AAPADNVGKE
     PEAAGLEAQG LGWQNSHGSG KGPDTITSGL EVTWTKTPTK WSNQFLEYLF KFDWELTKSP
     AGAHQWVAKN ADDIIPDAYD AFKKHKPTML TTDLSLRFDP AYEKISRRFL ENPDQFADAF
     ARAWFKLTHR DMGPRARYLG PEVPGEVLLW QDPIPAVNHA LIDTVDTAAL KRDVLATGVN
     PSKFISTAWA AASTFRGSDK RGGANGARIR FAPQRSWEVN NQPWLQESLS ALEGVQSRFN
     ASRPDRKQVS LADLIVLAGC AAVEQAAHDA GFPVRVPFTP GRMDASQDET DVESFSHMEP
     IADGFRNYAK PYVHGRAEHY LVDKAQLLNL SAPEMTVLVG GLRVLNTNYD GSAHGVFTSR
     PGVLSNDFFV NLLDMNTAWQ AGHNGEIFEG ADRKSGAKKW TATRADLVFG SHAELRAVAE
     VYASADGQRK FVNDFVAAWN KVMNLDRFDL QGKQFIYPRL
 
 
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