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P00432

- CATA_BOVIN

UniProt

P00432 - CATA_BOVIN

Protein

Catalase

Gene

CAT

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

    Cofactori

    Heme group.
    NADP.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei75 – 7511 PublicationPROSITE-ProRule annotation
    Active sitei148 – 1481
    Metal bindingi358 – 3581Iron (heme axial ligand)1 Publication

    GO - Molecular functioni

    1. aminoacylase activity Source: Ensembl
    2. catalase activity Source: UniProtKB
    3. enzyme binding Source: UniProtKB
    4. heme binding Source: Ensembl
    5. metal ion binding Source: UniProtKB-KW
    6. NADP binding Source: Ensembl

    GO - Biological processi

    1. aerobic respiration Source: Ensembl
    2. cholesterol metabolic process Source: Ensembl
    3. hemoglobin metabolic process Source: Ensembl
    4. hydrogen peroxide catabolic process Source: UniProtKB-KW
    5. negative regulation of apoptotic process Source: Ensembl
    6. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
    7. oxidation-reduction process Source: UniProtKB
    8. positive regulation of cell division Source: UniProtKB-KW
    9. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
    10. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
    11. protein homotetramerization Source: Ensembl
    12. triglyceride metabolic process Source: Ensembl
    13. UV protection Source: Ensembl

    Keywords - Molecular functioni

    Mitogen, Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    ReactomeiREACT_204534. Detoxification of Reactive Oxygen Species.
    REACT_214112. Purine catabolism.
    SABIO-RKP00432.

    Protein family/group databases

    PeroxiBasei5281. BtKat01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catalase (EC:1.11.1.6)
    Gene namesi
    Name:CAT
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 15

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: Ensembl
    2. peroxisomal membrane Source: Ensembl

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 527526CatalasePRO_0000084898Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21Blocked amino end (Ala)1 Publication
    Modified residuei13 – 131N6-succinyllysineBy similarity
    Modified residuei221 – 2211N6-succinyllysineBy similarity
    Modified residuei233 – 2331N6-acetyllysineBy similarity
    Modified residuei417 – 4171PhosphoserineBy similarity
    Modified residuei434 – 4341PhosphoserineBy similarity
    Modified residuei449 – 4491N6-acetyllysine; alternateBy similarity
    Modified residuei449 – 4491N6-succinyllysine; alternateBy similarity
    Modified residuei480 – 4801N6-acetyllysine; alternateBy similarity
    Modified residuei480 – 4801N6-succinyllysine; alternateBy similarity
    Modified residuei499 – 4991N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP00432.
    PRIDEiP00432.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000027941.

    Structurei

    Secondary structure

    1
    527
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni7 – 104
    Helixi11 – 188
    Turni19 – 213
    Beta strandi38 – 403
    Beta strandi42 – 454
    Helixi55 – 6410
    Beta strandi73 – 753
    Beta strandi77 – 8711
    Turni92 – 943
    Helixi98 – 1003
    Beta strandi106 – 1149
    Beta strandi116 – 1183
    Beta strandi124 – 1285
    Beta strandi131 – 1388
    Beta strandi141 – 15111
    Helixi158 – 1603
    Helixi161 – 1688
    Turni172 – 1743
    Helixi179 – 18810
    Helixi190 – 1923
    Helixi193 – 1997
    Helixi202 – 2043
    Beta strandi205 – 2095
    Beta strandi220 – 2234
    Beta strandi229 – 23810
    Helixi247 – 25610
    Helixi260 – 27011
    Beta strandi276 – 2849
    Helixi286 – 2916
    Turni305 – 3073
    Beta strandi311 – 32010
    Helixi325 – 3284
    Turni329 – 3313
    Beta strandi343 – 3453
    Helixi349 – 36517
    Helixi370 – 3723
    Helixi374 – 3763
    Turni395 – 4006
    Beta strandi404 – 4063
    Helixi416 – 4183
    Beta strandi424 – 4307
    Beta strandi435 – 4373
    Helixi441 – 4488
    Helixi453 – 46715
    Helixi472 – 48514
    Helixi487 – 50014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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/B2-507[»]
    8CATX-ray2.50A/B2-507[»]
    ProteinModelPortaliP00432.
    SMRiP00432. Positions 4-502.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00432.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the catalase family.Curated

    Phylogenomic databases

    eggNOGiCOG0753.
    GeneTreeiENSGT00390000018100.
    HOGENOMiHOG000087852.
    HOVERGENiHBG003986.
    InParanoidiP00432.
    KOiK03781.
    OMAiEVEQMAY.
    OrthoDBiEOG7V7660.
    TreeFamiTF300540.

    Family and domain databases

    Gene3Di2.40.180.10. 1 hit.
    InterProiIPR018028. 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]
    PANTHERiPTHR11465. PTHR11465. 1 hit.
    PfamiPF00199. Catalase. 1 hit.
    PF06628. Catalase-rel. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
    PRINTSiPR00067. CATALASE.
    SMARTiSM01060. Catalase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56634. SSF56634. 1 hit.
    PROSITEiPS00437. CATALASE_1. 1 hit.
    PS00438. CATALASE_2. 1 hit.
    PS51402. CATALASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00432-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADNRDPASD QMKHWKEQRA AQKPDVLTTG GGNPVGDKLN SLTVGPRGPL    50
    LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF 100
    EHIGKRTPIA VRFSTVAGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT 150
    PIFFIRDALL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF 200
    SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ GIKNLSVEDA 250
    ARLAHEDPDY GLRDLFNAIA TGNYPSWTLY IQVMTFSEAE IFPFNPFDLT 300
    KVWPHGDYPL IPVGKLVLNR NPVNYFAEVE QLAFDPSNMP PGIEPSPDKM 350
    LQGRLFAYPD THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMMDNQGG 400
    APNYYPNSFS APEHQPSALE HRTHFSGDVQ RFNSANDDNV TQVRTFYLKV 450
    LNEEQRKRLC ENIAGHLKDA QLFIQKKAVK NFSDVHPEYG SRIQALLDKY 500
    NEEKPKNAVH TYVQHGSHLS AREKANL 527
    Length:527
    Mass (Da):59,915
    Last modified:January 23, 2007 - v3
    Checksum:i2F97E793153D7AF9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti213 – 2131N → D AA sequence (PubMed:7082009)Curated
    Sequence conflicti226 – 2261N → D AA sequence (PubMed:7082009)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC103066 mRNA. Translation: AAI03067.1.
    PIRiA00500. CSBO.
    RefSeqiNP_001030463.1. NM_001035386.2.
    UniGeneiBt.48925.

    Genome annotation databases

    EnsembliENSBTAT00000027941; ENSBTAP00000027941; ENSBTAG00000020980.
    GeneIDi531682.
    KEGGibta:531682.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC103066 mRNA. Translation: AAI03067.1 .
    PIRi A00500. CSBO.
    RefSeqi NP_001030463.1. NM_001035386.2.
    UniGenei Bt.48925.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TGU X-ray 2.80 A/B/C/D 2-507 [» ]
    1TH2 X-ray 2.80 A/B/C/D 2-507 [» ]
    1TH3 X-ray 2.80 A/B/C/D 2-507 [» ]
    1TH4 X-ray 2.98 A/B/C/D 2-507 [» ]
    3NWL X-ray 2.69 A/B/C/D 1-527 [» ]
    3RE8 X-ray 1.90 A/B/C/D 4-502 [» ]
    3RGP X-ray 1.88 A/B/C/D 4-502 [» ]
    3RGS X-ray 1.99 A/B/C/D 4-502 [» ]
    4BLC X-ray 2.30 A/B/C/D 2-507 [» ]
    7CAT X-ray 2.50 A/B 2-507 [» ]
    8CAT X-ray 2.50 A/B 2-507 [» ]
    ProteinModelPortali P00432.
    SMRi P00432. Positions 4-502.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000027941.

    Protein family/group databases

    PeroxiBasei 5281. BtKat01.

    Proteomic databases

    PaxDbi P00432.
    PRIDEi P00432.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000027941 ; ENSBTAP00000027941 ; ENSBTAG00000020980 .
    GeneIDi 531682.
    KEGGi bta:531682.

    Organism-specific databases

    CTDi 847.

    Phylogenomic databases

    eggNOGi COG0753.
    GeneTreei ENSGT00390000018100.
    HOGENOMi HOG000087852.
    HOVERGENi HBG003986.
    InParanoidi P00432.
    KOi K03781.
    OMAi EVEQMAY.
    OrthoDBi EOG7V7660.
    TreeFami TF300540.

    Enzyme and pathway databases

    Reactomei REACT_204534. Detoxification of Reactive Oxygen Species.
    REACT_214112. Purine catabolism.
    SABIO-RK P00432.

    Miscellaneous databases

    EvolutionaryTracei P00432.
    NextBioi 20875507.

    Family and domain databases

    Gene3Di 2.40.180.10. 1 hit.
    InterProi IPR018028. 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 ]
    PANTHERi PTHR11465. PTHR11465. 1 hit.
    Pfami PF00199. Catalase. 1 hit.
    PF06628. Catalase-rel. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038928. Catalase_clade1-3. 1 hit.
    PRINTSi PR00067. CATALASE.
    SMARTi SM01060. Catalase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56634. SSF56634. 1 hit.
    PROSITEi PS00437. CATALASE_1. 1 hit.
    PS00438. CATALASE_2. 1 hit.
    PS51402. CATALASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. Cited for: SIMILARITY TO P.VITALE CATALASE.

    Entry informationi

    Entry nameiCATA_BOVIN
    AccessioniPrimary (citable) accession number: P00432
    Secondary accession number(s): Q3SZ80
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3