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Reviewed, UniProtKB/Swiss-Prot P07820 (CATA_CANTR)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxisomal catalase
    EC=1.11.1.6
Alternative name(s):
    PXP-9
Gene names
Name: POX9
OrganismCandida tropicalis (Yeast)
Taxonomic identifier5482 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.

Catalytic activity

2 H2O2 = O2 + 2 H2O.

Cofactor

Heme group.

Subunit structure

Homotetramer.

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the catalase family.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentPeroxisome
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: EC

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 485484Peroxisomal catalase
PRO_0000084920

Sites

Active site531 By similarity
Active site1261 By similarity
Metal binding3361Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict1661T → S in AAA34327. Ref.2
Sequence conflict3771L → V in CAA29093. Ref.4
Sequence conflict3901I → V in AAA34327. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P07820-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 612629F910FF4E8D

FASTA48554,938
        10         20         30         40         50         60 
MAPTFTNSNG QPIPEPFATQ RVGQHGPLLL QDFNLIDSLA HFDRERIPER VVHAKGSGAY 

        70         80         90        100        110        120 
GVFEVTDDIT DVCAAKFLDT VGKKTRIFTR FSTVGGELGS ADTARDPRGF ATKFYTEEGN 

       130        140        150        160        170        180 
LDLVYNNTPV FFIRDPSKFP HFIHTQKRNP ETHLKDANMF WDYLTTNEES VHQVMVLFSD 

       190        200        210        220        230        240 
RGTPASYREM NGYSGHTYKW SNNKGEWFYV QVHFISDQGI KTLTNEEAGS LAGSNPDYAQ 

       250        260        270        280        290        300 
EDLFKNIAAG NYPSWTCYIQ TMTEAQAKEA EFSVFDLTKV WPHGKYPMRR FGKFTLNENP 

       310        320        330        340        350        360 
KNYFAEVEQA AFSPAHTVPH MEPSADPVLQ SRLFSYADTH RHRLGTNYTQ IPVNCPVTGA 

       370        380        390        400        410        420 
VFNPHMRDGA MNVNGNLGNH PNYLASDKPI EFKQFSLQED QEVWHGAATP FHWKATPADF 

       430        440        450        460        470        480 
KQATELWKVL KKYPNQQEHL AHNVAVHASA ADAPIQDRVI AYFTKVHPDL GDLIKKEILE 


LSPRK 

« Hide

References

[1]"Catalase gene of the yeast Candida tropicalis. Sequence analysis and comparison with peroxisomal and cytosolic catalases from other sources."
Okada H., Ueda M., Sugaya T., Atomi H., Mozaffar S., Hishida T., Teranishi Y., Okazaki K., Takechi T., Kamiryo T., Tanaka A.
Eur. J. Biochem. 170:105-110(1987) [PubMed: 3691514] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of complementary DNA and the deduced amino acid sequence of peroxisomal catalase of the yeast Candida tropicalis pK233."
Murray W.W., Rachubinski R.A.
Gene 61:401-413(1987) [PubMed: 3446581] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 20336 / pK233 / NCYC 997.
[3]"Nucleotide sequence of peroxisomal catalase from the yeast Candida tropicalis pK233: identification of an upstream BamHI site polymorphism."
Murray W.W., Rachubinski R.A.
Nucleic Acids Res. 17:3600-3600(1989) [PubMed: 2726500] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 20336 / pK233 / NCYC 997.
[4]"Isolation of cDNA clones coding for peroxisomal proteins of Candida tropicalis: identification and sequence of a clone for catalase."
Rachubinski R.A., Fujiki Y., Lazarow P.B.
Biochim. Biophys. Acta 909:35-43(1987) [PubMed: 3580373] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 377-385.
Strain: ATCC 20336 / pK233 / NCYC 997.
[5]"Isolation of several cDNAs encoding yeast peroxisomal enzymes."
Ueda M., Okada H., Hishida T., Teranishi Y., Tanaka A.
FEBS Lett. 220:31-35(1987) [PubMed: 2440725] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 394-451, PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases

M18832 mRNA. Translation: AAA34327.1.
X05886 mRNA. Translation: CAA29310.1.
X05604 mRNA. Translation: CAA29093.1.
X06660 Genomic DNA. Translation: CAA29859.1.
X13978 Genomic DNA. Translation: CAA32159.1.
PIRCSCKPT. A29629.

3D structure databases

HSSPHSSP built from PDB template 1A4E based on UniProtKB P15202.
ModBaseSearch...

Protein family/group databases

PeroxiBase5256. CtKat01.

Enzyme and pathway databases

BRENDA1.11.1.6. 1242.

Family and domain databases

InterProIPR002226. Catalase.
IPR010582. Catalase-rel_immune_responsive.
IPR011614. Catalase_N.
IPR018028. Catalase_rel_subgroup.
[Graphical view]
Gene3DG3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHERPTHR11465. Catalase. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PRINTSPR00067. CATALASE.
ProDomPD000510. Catalase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATA_CANTR
AccessionPrimary (citable) accession number: P07820
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 69 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents