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Reviewed, UniProtKB/Swiss-Prot P00432 (CATA_BOVIN)

Last modified January 19, 2010. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Catalase
    EC=1.11.1.6
Gene names
Name: CAT
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

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Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentPeroxisome
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMitogen
Oxidoreductase
Peroxidase
   PTMPhosphoprotein
   Technical term3D-structure
Direct 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

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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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 residue2311Phosphotyrosine By similarity
Modified residue3081Phosphotyrosine By similarity
Modified residue5171Phosphoserine By similarity

Experimental info

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

Secondary structure

1 ................................................................................ 527
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00432-1 [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

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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: 7082009] [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: 7328661] [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: 10417406] [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: 3712444] [Abstract]
Cited for: SIMILARITY TO P.VITALE CATALASE.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC103066 mRNA. Translation: AAI03067.1.
IPIIPI00705932.
PIRCSBO. A00500.
RefSeqNP_001030463.1.
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[»]
4BLCX-ray2.30A/B/C/D2-507[»]
7CATX-ray2.50A/B2-506[»]
8CATX-ray2.50A/B2-506[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP00432.

Protein family/group databases

PeroxiBase5281. BtKat01.

Genome annotation databases

EnsemblENSBTAT00000027941; ENSBTAP00000027941; ENSBTAG00000020980; Bos taurus. [Genome view]
GeneID531682.
KEGGbta:531682.

Organism-specific databases

CTD531682.

Phylogenomic databases

eggNOGmaNOG07901.
HOVERGENP00432.
InParanoidP00432.
PhylomeDBP00432.

Enzyme and pathway databases

BRENDA1.11.1.6. 251.

Family and domain databases

InterProIPR002226. Catalase.
IPR020835. Catalase-like_haem-dep.
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.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: January 19, 2010
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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