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Catalase-peroxidase (CP) (EC 1.11.1.21) (Catalase-2) (Peroxidase/catalase)

 KATG_ASPFU              Reviewed;         759 AA.
Q7Z7W6; Q4WBB1;
25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
12-SEP-2018, entry version 101.
RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_03108};
Short=CP {ECO:0000255|HAMAP-Rule:MF_03108};
EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_03108};
AltName: Full=Catalase-2;
AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_03108};
Name=katG {ECO:0000255|HAMAP-Rule:MF_03108}; Synonyms=CAT2;
ORFNames=AFUA_8G01670;
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
A1100) (Aspergillus fumigatus).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=330879;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 385-397,
SUBUNIT, ACTIVITY REGULATION, AND FUNCTION.
PubMed=12761140; DOI=10.1128/IAI.71.6.3551-3562.2003;
Paris S., Wysong D., Debeaupuis J.-P., Shibuya K., Philippe B.,
Diamond R.D., Latge J.-P.;
"Catalases of Aspergillus fumigatus.";
Infect. Immun. 71:3551-3562(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
PubMed=16372009; DOI=10.1038/nature04332;
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
Machida M., Hall N., Barrell B.G., Denning D.W.;
"Genomic sequence of the pathogenic and allergenic filamentous fungus
Aspergillus fumigatus.";
Nature 438:1151-1156(2005).
-!- FUNCTION: Bifunctional enzyme with both catalase and broad-
spectrum peroxidase activity. May be involved in protection from
the host during host infection. {ECO:0000255|HAMAP-Rule:MF_03108,
ECO:0000269|PubMed:12761140}.
-!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
{ECO:0000255|HAMAP-Rule:MF_03108}.
-!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
{ECO:0000255|HAMAP-Rule:MF_03108}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000255|HAMAP-Rule:MF_03108};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
monomer. {ECO:0000255|HAMAP-Rule:MF_03108};
-!- ACTIVITY REGULATION: Sensitive to heat and heavy metals.
{ECO:0000269|PubMed:12761140}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12761140}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03108}.
-!- PTM: Not glycosylated.
-!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is
important for the catalase, but not the peroxidase activity of the
enzyme. {ECO:0000255|HAMAP-Rule:MF_03108}.
-!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
subfamily. {ECO:0000255|HAMAP-Rule:MF_03108}.
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EMBL; AY125354; AAM95780.1; -; Genomic_DNA.
EMBL; AAHF01000014; EAL85001.1; -; Genomic_DNA.
RefSeq; XP_747039.1; XM_741946.1.
ProteinModelPortal; Q7Z7W6; -.
SMR; Q7Z7W6; -.
STRING; 5085.CADAFUBP00008269; -.
Allergome; 8994; Asp f CP.
PeroxiBase; 1881; AfumCP01.
SwissPalm; Q7Z7W6; -.
PRIDE; Q7Z7W6; -.
EnsemblFungi; EAL85001; EAL85001; AFUA_8G01670.
GeneID; 3504583; -.
KEGG; afm:AFUA_8G01670; -.
EuPathDB; FungiDB:Afu8g01670; -.
HOGENOM; HOG000218110; -.
InParanoid; Q7Z7W6; -.
KO; K03782; -.
OMA; PEEDIYW; -.
OrthoDB; EOG092C0YTX; -.
Proteomes; UP000002530; Chromosome 8.
Proteomes; UP000002530; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; IDA:AspGD.
GO; GO:0004096; F:catalase activity; IDA:AspGD.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004601; F:peroxidase activity; IDA:AspGD.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
HAMAP; MF_01961; Catal_peroxid; 1.
InterPro; IPR000763; Catalase_peroxidase.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
InterPro; IPR019794; Peroxidases_AS.
InterPro; IPR019793; Peroxidases_heam-ligand_BS.
PANTHER; PTHR30555; PTHR30555; 1.
Pfam; PF00141; peroxidase; 2.
PRINTS; PR00460; BPEROXIDASE.
PRINTS; PR00458; PEROXIDASE.
SUPFAM; SSF48113; SSF48113; 2.
TIGRFAMs; TIGR00198; cat_per_HPI; 1.
PROSITE; PS00435; PEROXIDASE_1; 1.
PROSITE; PS00436; PEROXIDASE_2; 1.
PROSITE; PS50873; PEROXIDASE_4; 2.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing; Heme;
Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
Reference proteome.
CHAIN 1 759 Catalase-peroxidase.
/FTId=PRO_0000354100.
ACT_SITE 97 97 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03108}.
METAL 283 283 Iron (heme axial ligand).
{ECO:0000255|HAMAP-Rule:MF_03108}.
SITE 93 93 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_03108}.
CROSSLNK 96 242 Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
(with M-268). {ECO:0000255|HAMAP-
Rule:MF_03108}.
CROSSLNK 242 268 Tryptophyl-tyrosyl-methioninium (Tyr-Met)
(with W-96). {ECO:0000255|HAMAP-
Rule:MF_03108}.
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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