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
