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Q96VB8 (CATA_CANBO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peroxisomal catalase
EC=1.11.1.6
Gene names
Name:CTA1
OrganismCandida boidinii (Yeast)
Taxonomic identifier5477 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Subcellular location

Peroxisome. Note: Bimodally distributed between the cytosol and peroxisomes in methanol-grown cells but is localized exclusively in peroxisomes in oleate- and D-alanine-grown cells. Ref.1

Sequence similarities

Belongs to the catalase family.

Ontologies

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

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

Chain1 – 504504Peroxisomal catalase
PRO_0000084919

Regions

Motif502 – 5043Microbody targeting signal

Sites

Active site631 By similarity
Active site1361 By similarity
Metal binding3451Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q96VB8 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: CCF63C4FA752DC3B

FASTA50457,095
        10         20         30         40         50         60 
MSNPPTYTTS QGCPVSDAFS TQRISGTKIS IKTPVGPLLL QDFKFLDSLA HFDRERIPER 

        70         80         90        100        110        120 
VVHAKGAGAY GVFEVTEDIS DICSAKFLDT VGKKTKIFTR FSTVGGEKGS SDSARDPRGF 

       130        140        150        160        170        180 
ATKFYTEEGN LDLVYNNTPI FFIRDPTKFP HFIHTQKRNP ATNCKDANMF WDYLTNNPES 

       190        200        210        220        230        240 
LHQIMYLFSN RGTPTSYRKM NGYSGHSYKW YNAKGEWVSS VHFISNQGVH NMTDEEAGDL 

       250        260        270        280        290        300 
SGKDPDFQTM DLYKAIEQGD YPSWECYVQT MTLEEAKKQP FSVYDLTKVW PHKDFPLRHF 

       310        320        330        340        350        360 
GKFTLNENAQ NYFAEVEQAA FSPSHTVPGM EPSNDPVLQS RLFSYPDTHR HRLGVNYSQI 

       370        380        390        400        410        420 
PVNCPMRAVF APQIRDGSMM VNGNLGGTPN YAGAYNCPVQ YQAPIKASSK TPEEQYEGET 

       430        440        450        460        470        480 
LSYDWTEVNE YDFYQPGRFW EVLGKTKGEQ EALVHNVANH VSGADEFIQD RVFAYFSKAN 

       490        500 
PVIGDLIRKE VLKKSPRGAS KNKF

« Hide

References

[1]"Peroxisomal catalase in the methylotrophic yeast Candida boidinii: transport efficiency and metabolic significance."
Horiguchi H., Yurimoto H., Goh T.K., Nakagawa T., Kato N., Sakai Y.
J. Bacteriol. 183:6372-6383(2001) [PubMed: 11591682] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
Strain: S2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB064338 Genomic DNA. Translation: BAB69893.1.

3D structure databases

ProteinModelPortalQ96VB8.
SMRQ96VB8. Positions 1-490.
ModBaseSearch...

Protein family/group databases

PeroxiBase5262. CboiKat01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13166.

Family and domain databases

InterProIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[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]
PIRSFPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSPR00067. CATALASE.
SMARTSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMSSF56634. Catalase_N. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATA_CANBO
AccessionPrimary (citable) accession number: Q96VB8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 50 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

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