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Q8X182 (KATG_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 80. 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:cat-2
ORF Names:NCU05770
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.

Catalytic activity

Donor + H2O2 = oxidized donor + 2 H2O.

2 H2O2 = O2 + 2 H2O.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per dimer By similarity. Ref.1

Enzyme regulation

Inhibited by KCN. Ref.1

Subunit structure

Homodimer or homotetramer By similarity.

Induction

Induced in late stationary growth phase. Ref.1

Post-translational modification

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.

Biophysicochemical properties

Kinetic parameters:

KM=13.2 mM for H2O2 for the catalase reaction Ref.1

pH dependence:

Optimum pH is 4.75 for the peroxidase reaction and 6.25 for the catalase reaction.

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 – 753753Catalase-peroxidase
PRO_0000055582

Sites

Active site911Proton acceptor By similarity
Metal binding2791Iron (heme axial ligand) By similarity
Site871Transition state stabilizer By similarity

Amino acid modifications

Cross-link90 ↔ 238Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-264) By similarity
Cross-link238 ↔ 264Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-90) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8X182 [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: DED01DC6D10BA582

FASTA75383,380
        10         20         30         40         50         60 
MSECPVRKSN VGGGGTRNHD WWPAQLRLNI LRQHTPVSNP LDKDFDYAAA FKSLDYEGLK 

        70         80         90        100        110        120 
KDLTKLMTDS QDWWPADFGH YGGLFIRMAW HSAGTYRVTD GRGGGGEGQQ RFAPLNSWPD 

       130        140        150        160        170        180 
NVSLDKARRL LWPIKQKYGN KISWSDLLLL TGNVALESMG FKTFGFAGGR PDTWEADESV 

       190        200        210        220        230        240 
YWGAETTWLG NEDRYSEGQE GHEGHGVVQG DESKKQHTDI HNRDLQSPLA SSHMGLIYVN 

       250        260        270        280        290        300 
PEGPDGIPDP VASAKDIRVT FGRMAMNDEE TVALIAGGHS FGKTHGAGPT HHVGKEPEAA 

       310        320        330        340        350        360 
PIEHQGLGWA NSFGQGKGPD TITSGLEVTW TPTPTKWGMG YLEYLYKFDW EPTKSPAGAN 

       370        380        390        400        410        420 
QWVAKNAEPT IPDAYDPNKK KLPTMLTTDI ALRMDPAYDK ICRDYLANPD KFADAFARAW 

       430        440        450        460        470        480 
FKLLHRDMGP RTRWIGPEVP SEILPWEDYI PPVDYQIIDD NDIAALKKEI LATGVAPKKL 

       490        500        510        520        530        540 
IFVAWSSASS FRGSDKRGGA NGARIRLAPQ NEWKVNDPST LREVLAALES VQQKFNDSSS 

       550        560        570        580        590        600 
GKKVSLADLI VLGGVAALEQ ASGLVVPFTP GRNDATQEHT DVHSFTHLEP HADGFRSYGK 

       610        620        630        640        650        660 
GTKRVRTEQF LIDRASLLTL SAPELTALIG GLRVLEANYD GSSYGVLTKT PGKLTNDYFV 

       670        680        690        700        710        720 
NLLDTNTAWK AADNEGEVFI GYDRKTHDKK WTATRADLIF GAHAELRALA EVYAAVDGEE 

       730        740        750 
KFKRDFVAAW HKVMNLDRFD LKQEGRGQNA PKL 

« Hide

References

« Hide 'large scale' references
[1]"Neurospora crassa catalases, singlet oxygen and cell differentiation."
Peraza L., Hansberg W.
Biol. Chem. 383:569-575(2002) [PubMed: 12033445] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 654-670, HEME-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, INDUCTION.
[2]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed: 12712197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF459787 mRNA. Translation: AAL66352.2.
AABX02000023 Genomic DNA. Translation: EAA30509.1.
RefSeqXP_959745.1. XM_954652.2.

3D structure databases

ProteinModelPortalQ8X182.
SMRQ8X182. Positions 15-741.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8X182.

Protein family/group databases

PeroxiBase2181. NcCP01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000005784; EFNCRP00000005777; EFNCRG00000005774.
GeneID3875883.
KEGGncr:NCU05770.
NMPDRfig|5141.1.peg.3558.

Phylogenomic databases

eggNOGfuNOG06405.
GeneTreeEFGT00050000003307.
OMAKRHAPSM.
OrthoDBEOG41CB4B.

Enzyme and pathway databases

BioCycNCRA-XX3-01:NCRA-XX3-01-009518-MONOMER.
BRENDA1.11.1.6. 3627.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG_NEUCR
AccessionPrimary (citable) accession number: Q8X182
Secondary accession number(s): Q7S4Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: October 1, 2002
Last modified: December 14, 2011
This is version 80 of the entry and version 2 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