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P00432 (CATA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catalase

EC=1.11.1.6
Gene names
Name:CAT
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length527 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. Promotes growth of cells.

Catalytic activity

2 H2O2 = O2 + 2 H2O.

Cofactor

Heme group.

NADP.

Subunit structure

Homotetramer.

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the catalase family.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentPeroxisome
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMitogen
Oxidoreductase
Peroxidase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processUV protection

Inferred from electronic annotation. Source: Ensembl

aerobic respiration

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Inferred from electronic annotation. Source: Ensembl

hemoglobin metabolic process

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

oxidation-reduction process

Inferred from direct assay PubMed 6946424. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

triglyceride metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: Ensembl

peroxisomal membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: Ensembl

aminoacylase activity

Inferred from electronic annotation. Source: Ensembl

catalase activity

Inferred from direct assay PubMed 6946424. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 16781659. Source: UniProtKB

heme binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 527526Catalase
PRO_0000084898

Sites

Active site751 Ref.3
Active site1481
Metal binding3581Iron (heme axial ligand) Ref.3

Amino acid modifications

Modified residue21Blocked amino end (Ala) Ref.2
Modified residue131N6-succinyllysine By similarity
Modified residue2211N6-succinyllysine By similarity
Modified residue2331N6-acetyllysine By similarity
Modified residue4171Phosphoserine By similarity
Modified residue4341Phosphoserine By similarity
Modified residue4491N6-acetyllysine; alternate By similarity
Modified residue4491N6-succinyllysine; alternate By similarity
Modified residue4801N6-acetyllysine; alternate By similarity
Modified residue4801N6-succinyllysine; alternate By similarity
Modified residue4991N6-acetyllysine By similarity

Experimental info

Sequence conflict2131N → D AA sequence Ref.2
Sequence conflict2261N → D AA sequence Ref.2

Secondary structure

....................................................................................... 527
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00432 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2F97E793153D7AF9

FASTA52759,915
        10         20         30         40         50         60 
MADNRDPASD QMKHWKEQRA AQKPDVLTTG GGNPVGDKLN SLTVGPRGPL LVQDVVFTDE 

        70         80         90        100        110        120 
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EHIGKRTPIA VRFSTVAGES 

       130        140        150        160        170        180 
GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDALL FPSFIHSQKR NPQTHLKDPD 

       190        200        210        220        230        240 
MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ 

       250        260        270        280        290        300 
GIKNLSVEDA ARLAHEDPDY GLRDLFNAIA TGNYPSWTLY IQVMTFSEAE IFPFNPFDLT 

       310        320        330        340        350        360 
KVWPHGDYPL IPVGKLVLNR NPVNYFAEVE QLAFDPSNMP PGIEPSPDKM LQGRLFAYPD 

       370        380        390        400        410        420 
THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMMDNQGG APNYYPNSFS APEHQPSALE 

       430        440        450        460        470        480 
HRTHFSGDVQ RFNSANDDNV TQVRTFYLKV LNEEQRKRLC ENIAGHLKDA QLFIQKKAVK 

       490        500        510        520 
NFSDVHPEYG SRIQALLDKY NEEKPKNAVH TYVQHGSHLS AREKANL 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Rumen reticulum.
[2]"The complete amino acid sequence of bovine liver catalase and the partial sequence of bovine erythrocyte catalase."
Schroeder W.A., Shelton J.R., Shelton J.B., Robberson B., Apell G., Fang R.S., Bonaventura J.
Arch. Biochem. Biophys. 214:397-421(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-507.
Tissue: Liver.
[3]"Structure of beef liver catalase."
Murthy M.R.N., Reid T.J. III, Sicignano A., Tanaka N., Rossmann M.G.
J. Mol. Biol. 152:465-499(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Tissue: Liver.
[4]"The refined structure of beef liver catalase at 2.5-A resolution."
Fita I., Silva A.M., Murthy M.R.N., Rossmann M.G.
Acta Crystallogr. B 42:497-515(1986)
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Tissue: Liver.
[5]"Structure of orthorhombic crystals of beef liver catalase."
Ko T.P., Day J., Malkin A.J., McPherson A.
Acta Crystallogr. D 55:1383-1394(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Tissue: Liver.
[6]"Comparison of beef liver and Penicillium vitale catalases."
Melik-Adamyan W.R., Barynin V.V., Vagin A.A., Borisov V.V., Vainshtein B.K., Fita I., Murthy M.R.N., Rossmann M.G.
J. Mol. Biol. 188:63-72(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: SIMILARITY TO P.VITALE CATALASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC103066 mRNA. Translation: AAI03067.1.
PIRCSBO. A00500.
RefSeqNP_001030463.1. NM_001035386.2.
UniGeneBt.48925.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TGUX-ray2.80A/B/C/D2-507[»]
1TH2X-ray2.80A/B/C/D2-507[»]
1TH3X-ray2.80A/B/C/D2-507[»]
1TH4X-ray2.98A/B/C/D2-507[»]
3NWLX-ray2.69A/B/C/D1-527[»]
3RE8X-ray1.90A/B/C/D4-502[»]
3RGPX-ray1.88A/B/C/D4-502[»]
3RGSX-ray1.99A/B/C/D4-502[»]
4BLCX-ray2.30A/B/C/D2-507[»]
7CATX-ray2.50A/B2-506[»]
8CATX-ray2.50A/B2-506[»]
ProteinModelPortalP00432.
SMRP00432. Positions 4-502.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000027941.

Protein family/group databases

PeroxiBase5281. BtKat01.

Proteomic databases

PaxDbP00432.
PRIDEP00432.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000027941; ENSBTAP00000027941; ENSBTAG00000020980.
GeneID531682.
KEGGbta:531682.

Organism-specific databases

CTD847.

Phylogenomic databases

eggNOGCOG0753.
GeneTreeENSGT00390000018100.
HOGENOMHOG000087852.
HOVERGENHBG003986.
InParanoidP00432.
KOK03781.
OMALYTQINA.
OrthoDBEOG7V7660.
TreeFamTF300540.

Enzyme and pathway databases

SABIO-RKP00432.

Family and domain databases

Gene3D2.40.180.10. 1 hit.
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]
PANTHERPTHR11465. PTHR11465. 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. SSF56634. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00432.
NextBio20875507.

Entry information

Entry nameCATA_BOVIN
AccessionPrimary (citable) accession number: P00432
Secondary accession number(s): Q3SZ80
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references