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KATG_ASPFU
ID   KATG_ASPFU              Reviewed;         759 AA.
AC   Q7Z7W6; Q4WBB1;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=Catalase-2;
DE   AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_03108};
GN   Name=katG {ECO:0000255|HAMAP-Rule:MF_03108}; Synonyms=CAT2;
GN   ORFNames=AFUA_8G01670;
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], PROTEIN SEQUENCE OF 385-397, SUBUNIT,
RP   ACTIVITY REGULATION, AND FUNCTION.
RX   PubMed=12761140; DOI=10.1128/iai.71.6.3551-3562.2003;
RA   Paris S., Wysong D., Debeaupuis J.-P., Shibuya K., Philippe B.,
RA   Diamond R.D., Latge J.-P.;
RT   "Catalases of Aspergillus fumigatus.";
RL   Infect. Immun. 71:3551-3562(2003).
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: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. May be involved in protection from the host during
CC       host infection. {ECO:0000255|HAMAP-Rule:MF_03108,
CC       ECO:0000269|PubMed:12761140}.
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   -!- ACTIVITY REGULATION: Sensitive to heat and heavy metals.
CC       {ECO:0000269|PubMed:12761140}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12761140}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03108}.
CC   -!- PTM: Not glycosylated.
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; AY125354; AAM95780.1; -; Genomic_DNA.
DR   EMBL; AAHF01000014; EAL85001.1; -; Genomic_DNA.
DR   RefSeq; XP_747039.1; XM_741946.1.
DR   AlphaFoldDB; Q7Z7W6; -.
DR   SMR; Q7Z7W6; -.
DR   STRING; 746128.CADAFUBP00008269; -.
DR   Allergome; 8994; Asp f CP.
DR   PeroxiBase; 1881; AfumCP01.
DR   SwissPalm; Q7Z7W6; -.
DR   EnsemblFungi; EAL85001; EAL85001; AFUA_8G01670.
DR   GeneID; 3504583; -.
DR   KEGG; afm:AFUA_8G01670; -.
DR   VEuPathDB; FungiDB:Afu8g01670; -.
DR   eggNOG; ENOG502QTDY; Eukaryota.
DR   HOGENOM; CLU_025424_2_0_1; -.
DR   InParanoid; Q7Z7W6; -.
DR   OMA; MILAGNC; -.
DR   OrthoDB; 352289at2759; -.
DR   Proteomes; UP000002530; Chromosome 8.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004096; F:catalase activity; IDA:AspGD.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IDA:AspGD.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IBA:GO_Central.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Reference proteome.
FT   CHAIN           1..759
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354100"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
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   759 AA;  83762 MW;  4519FF268CE43B8F CRC64;
     MTQDKCPFKE QSSQPNFAGG GTSNKDWWPD RLKLNILRQH TAVSNPLDAD FDYAAAFNSL
     DYEGLKKDLR ALMTDSQDWW PADFGHYGGL FIRMAWHSAG TYRVFDGRGG AGQGQQRFAP
     LNSWPDNVSL DKARRLLWPI KQKYGNKISW ADLLILTGNV ALESMGFKTF GFAGGRPDTW
     EADEATYWGR ETTWLGNDAR YAKGFSGSDK RGSLIADEES HKTTHSRELE TPLAAAHMGL
     IYVNPEGPDG NPDPVAAAHD IRDTFGRMAM NDEETVALIA GGHTFGKTHG AAPADNVGKE
     PEAAGLEAQG LGWANKHGSG KGPHTITSGL EVTWTKTPTQ WNNNFLEYLF KFEWELTKSP
     AGAHQWVAKN ADEIIPDAYD ASKKHKPTML TTDLSLRFDP AYEKIARRFL EHPDQFADAF
     ARAWFKLTHR DMGPRARYLG PEVPSEVLIW QDPIPAVNHP LVDASDIAAL KDEILASGVP
     PRSFISTAWA AASTFRGSDK RGGANGARIR LAPQRDWEVN NQPWLREALS ALEAVQSRFN
     ARGDSKKVSL ADLIVLAGCA AVEKAAQDAG HPIKVPFVPG RMDASQEETD VQSFNHMEPF
     ADGFRNFAKG PARPRAEHYL VDKAQLLNLS APEMTVLVGG LRVLNTNYDG STHGVFTSRP
     GALTNDFFVH LLDMNTAWKD VGNGELFEGS DRKTGGKKWT ATRADLVFGS NAELRAIAEV
     YASNDGDMKF VKDFVAAWNK VMNLDRFDLK GKQTIPARL
 
 
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