Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q7Z7W6 (KATG_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catalase-peroxidase

Short name=CP
EC=1.11.1.21
Alternative name(s):
Catalase-2
Peroxidase/catalase
Gene names
Name:katG
Synonyms:CAT2
ORF Names:AFUA_8G01670
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length759 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May be involved in protection from the host during host infection. Ref.1

Catalytic activity

Donor + H2O2 = oxidized donor + 2 H2O.

2 H2O2 = O2 + 2 H2O.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group.

Enzyme regulation

Sensitive to heat and heavy metals. Ref.1

Subunit structure

Monomer. Ref.1

Post-translational modification

Not glycosylated.

The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity.

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 759759Catalase-peroxidase
PRO_0000354100

Sites

Active site971Proton acceptor By similarity
Metal binding2831Iron (heme axial ligand) By similarity
Site931Transition state stabilizer By similarity

Amino acid modifications

Cross-link96 ↔ 242Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-268) By similarity
Cross-link242 ↔ 268Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-96) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7Z7W6 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 4519FF268CE43B8F

FASTA75983,762
        10         20         30         40         50         60 
MTQDKCPFKE QSSQPNFAGG GTSNKDWWPD RLKLNILRQH TAVSNPLDAD FDYAAAFNSL 

        70         80         90        100        110        120 
DYEGLKKDLR ALMTDSQDWW PADFGHYGGL FIRMAWHSAG TYRVFDGRGG AGQGQQRFAP 

       130        140        150        160        170        180 
LNSWPDNVSL DKARRLLWPI KQKYGNKISW ADLLILTGNV ALESMGFKTF GFAGGRPDTW 

       190        200        210        220        230        240 
EADEATYWGR ETTWLGNDAR YAKGFSGSDK RGSLIADEES HKTTHSRELE TPLAAAHMGL 

       250        260        270        280        290        300 
IYVNPEGPDG NPDPVAAAHD IRDTFGRMAM NDEETVALIA GGHTFGKTHG AAPADNVGKE 

       310        320        330        340        350        360 
PEAAGLEAQG LGWANKHGSG KGPHTITSGL EVTWTKTPTQ WNNNFLEYLF KFEWELTKSP 

       370        380        390        400        410        420 
AGAHQWVAKN ADEIIPDAYD ASKKHKPTML TTDLSLRFDP AYEKIARRFL EHPDQFADAF 

       430        440        450        460        470        480 
ARAWFKLTHR DMGPRARYLG PEVPSEVLIW QDPIPAVNHP LVDASDIAAL KDEILASGVP 

       490        500        510        520        530        540 
PRSFISTAWA AASTFRGSDK RGGANGARIR LAPQRDWEVN NQPWLREALS ALEAVQSRFN 

       550        560        570        580        590        600 
ARGDSKKVSL ADLIVLAGCA AVEKAAQDAG HPIKVPFVPG RMDASQEETD VQSFNHMEPF 

       610        620        630        640        650        660 
ADGFRNFAKG PARPRAEHYL VDKAQLLNLS APEMTVLVGG LRVLNTNYDG STHGVFTSRP 

       670        680        690        700        710        720 
GALTNDFFVH LLDMNTAWKD VGNGELFEGS DRKTGGKKWT ATRADLVFGS NAELRAIAEV 

       730        740        750 
YASNDGDMKF VKDFVAAWNK VMNLDRFDLK GKQTIPARL 

« Hide

References

« Hide 'large scale' references
[1]"Catalases of Aspergillus fumigatus."
Paris S., Wysong D., Debeaupuis J.-P., Shibuya K., Philippe B., Diamond R.D., Latge J.-P.
Infect. Immun. 71:3551-3562(2003) [PubMed: 12761140] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 385-397, SUBUNIT, ENZYME REGULATION, FUNCTION.
[2]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
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. expand/collapse author list , 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.
Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY125354 Genomic DNA. Translation: AAM95780.1.
AAHF01000014 Genomic DNA. Translation: EAL85001.1.
RefSeqXP_747039.1. XM_741946.1.

3D structure databases

HSSPHSSP built from PDB template 1ITK based on UniProtKB O59651.
ProteinModelPortalQ7Z7W6.
SMRQ7Z7W6. Positions 21-749.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7Z7W6.

Protein family/group databases

Allergome8994. Asp f CP.
PeroxiBase1881. AfumCP01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00000896; CADAFUAP00000896; CADAFUAG00000896.
GeneID3504583.
GenomeReviewsGene locus katG in contig CM000176_GR.
KEGGafm:AFUA_8G01670.

Phylogenomic databases

eggNOGfuNOG06405.
GeneTreeEFGT00050000003307.
HOGENOMHBG285610.
OMAKRHAPSM.
OrthoDBEOG41CB4B.

Family and domain databases

InterProIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
KOK03782.
PfamPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 2 hits.
TIGRFAMsTIGR00198. Cat_per_HPI. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG_ASPFU
AccessionPrimary (citable) accession number: Q7Z7W6
Secondary accession number(s): Q4WBB1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 1, 2003
Last modified: December 14, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families