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Q9C169

- CAT3_NEUCR

UniProt

Q9C169 - CAT3_NEUCR

Protein

Catalase-3

Gene

cat-3

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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.By similarity

    Catalytic activityi

    2 H2O2 = O2 + 2 H2O.1 PublicationPROSITE-ProRule annotation

    Cofactori

    Heme group.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei102 – 1021PROSITE-ProRule annotation
    Active sitei175 – 1751PROSITE-ProRule annotation
    Metal bindingi389 – 3891Iron (heme axial ligand)By similarity

    GO - Molecular functioni

    1. catalase activity Source: UniProtKB-EC
    2. heme binding Source: InterPro
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. hydrogen peroxide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Protein family/group databases

    PeroxiBasei5416. NcKat03.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catalase-3 (EC:1.11.1.6)
    Gene namesi
    Name:cat-3
    ORF Names:NCU00355
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    ProteomesiUP000001805: Chromosome 3, Linkage Group III

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 30121 PublicationPRO_0000004687Add
    BLAST
    Chaini31 – 719689Catalase-3PRO_0000004688Add
    BLAST

    Expressioni

    Developmental stagei

    Activity is predominant during late exponential growth and at the start of the conidiation process.1 Publication

    Inductioni

    Induced under stress conditions, such as H2O2, paraquat, cadmium, heat shock, uric acid and nitrate treatment.1 Publication

    Interactioni

    Protein-protein interaction databases

    IntActiQ9C169. 1 interaction.
    MINTiMINT-2515988.
    STRINGi5141.NCU00355.1.

    Structurei

    Secondary structure

    1
    719
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi41 – 466
    Beta strandi70 – 723
    Helixi82 – 9211
    Beta strandi100 – 1023
    Beta strandi104 – 11613
    Turni119 – 1213
    Helixi125 – 1273
    Beta strandi133 – 1419
    Beta strandi143 – 1453
    Beta strandi153 – 1553
    Beta strandi158 – 1658
    Beta strandi168 – 17912
    Helixi185 – 1873
    Helixi188 – 1958
    Turni199 – 2013
    Helixi211 – 2199
    Helixi221 – 2233
    Helixi224 – 2307
    Helixi233 – 2353
    Beta strandi236 – 2383
    Helixi240 – 2423
    Beta strandi251 – 2544
    Beta strandi260 – 27112
    Helixi278 – 28710
    Helixi291 – 30111
    Beta strandi307 – 3159
    Helixi317 – 3193
    Beta strandi323 – 3253
    Turni336 – 3383
    Beta strandi342 – 35110
    Helixi356 – 3594
    Turni360 – 3623
    Helixi380 – 39718
    Beta strandi398 – 4003
    Helixi402 – 4043
    Turni406 – 4083
    Beta strandi427 – 4293
    Beta strandi434 – 4363
    Turni438 – 4425
    Beta strandi449 – 4513
    Beta strandi462 – 4698
    Helixi473 – 4753
    Helixi480 – 4878
    Helixi491 – 50515
    Helixi511 – 52414
    Helixi526 – 53611
    Helixi545 – 5473
    Beta strandi558 – 5614
    Beta strandi570 – 5745
    Beta strandi577 – 5804
    Helixi581 – 59313
    Turni594 – 5963
    Beta strandi598 – 6058
    Beta strandi611 – 6133
    Turni614 – 6163
    Helixi619 – 6213
    Beta strandi623 – 6275
    Helixi631 – 6355
    Helixi637 – 6404
    Helixi649 – 65911
    Beta strandi664 – 6674
    Helixi668 – 6703
    Helixi671 – 6766
    Beta strandi681 – 6833
    Beta strandi686 – 6905
    Helixi691 – 70414
    Helixi708 – 7103

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EJ6X-ray2.30A/B/C/D32-719[»]
    3ZJ4X-ray3.10A/B/C/D1-719[»]
    3ZJ5X-ray1.95A/B/C/D1-719[»]
    4AJ9X-ray1.85A/B/C/D38-719[»]
    4BIMX-ray2.95A/B/C/D1-719[»]
    ProteinModelPortaliQ9C169.
    SMRiQ9C169. Positions 40-714.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9C169.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the catalase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0753.
    HOGENOMiHOG000087851.
    KOiK03781.
    OrthoDBiEOG7K9KBN.

    Family and domain databases

    Gene3Di2.40.180.10. 1 hit.
    3.40.50.880. 1 hit.
    InterProiIPR018028. Catalase.
    IPR020835. Catalase-like_dom.
    IPR024708. Catalase_AS.
    IPR024712. Catalase_clade2.
    IPR011614. Catalase_core.
    IPR010582. Catalase_immune_responsive.
    IPR029062. Class_I_gatase-like.
    [Graphical view]
    PANTHERiPTHR11465. PTHR11465. 1 hit.
    PfamiPF00199. Catalase. 1 hit.
    PF06628. Catalase-rel. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038927. Catalase_clade2. 1 hit.
    PRINTSiPR00067. CATALASE.
    SMARTiSM01060. Catalase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56634. SSF56634. 1 hit.
    PROSITEiPS00438. 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.

    Q9C169-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRVNALLPLS GLIGTALAAC PFADPSALGR RAEGGEVDAR QRLKEVEVDD    50
    NGQFMTTDFG GNIEEQFSLK AGGRGSTLLE DFIFRQKLQH FDHERIPERV 100
    VHARGAGAHG IFTSYGDWSN ITAASFLGAK DKQTPVFVRF STVAGSRGSA 150
    DTARDVHGFA TRFYTDEGNF DIVGNNIPVF FIQDAIRFPD LIHSVKPSPD 200
    NEVPQAATAH DSAWDFFSSQ PSALHTLFWA MSGNGIPRSY RHMDGFGIHT 250
    FRLVTEDGKS KLVKWHWKTK QGKAALVWEE AQVLAGKNAD FHRQDLWDAI 300
    ESGNAPSWEL AVQLIDEDKA QAYGFDLLDP TKFLPEEFAP LQVLGEMTLN 350
    RNPMNYFAET EQISFQPGHI VRGVDFTEDP LLQGRLYSYL DTQLNRHRGP 400
    NFEQLPINRP VSGVHNNHRD GQGQAWIHKN IHHYSPSYLN KGYPAQANQT 450
    VGRGFFTTPG RTASGVLNRE LSATFDDHYT QPRLFFNSLT PVEQQFVINA 500
    IRFEASHVTN EQVKKNVLEQ LNKISNDVAK RVAVALGLEA PQPDPTYYHN 550
    NVTRGVSIFN ESLPTIATLR VGVLSTTKGG SLDKAKALKE QLEKDGLKVT 600
    VIAEYLASGV DQTYSAADAT AFDAVVVAEG AERVFSGKGA MSPLFPAGRP 650
    SQILTDGYRW GKPVAAVGSA KKALQSIGVE EKEAGVYAGA QDEVIKGVEE 700
    GLKVFKFLER FAVDGDDEE 719
    Length:719
    Mass (Da):79,228
    Last modified:June 1, 2001 - v1
    Checksum:i72790DE3310B64D0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY027544 Genomic DNA. Translation: AAK15807.1.
    CM002238 Genomic DNA. Translation: EAA28590.1.
    RefSeqiXP_957826.1. XM_952733.2.
    UniGeneiNcr.16984.

    Genome annotation databases

    EnsemblFungiiEFNCRT00000000465; EFNCRP00000000465; EFNCRG00000000465.
    GeneIDi3873876.
    KEGGincr:NCU00355.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY027544 Genomic DNA. Translation: AAK15807.1 .
    CM002238 Genomic DNA. Translation: EAA28590.1 .
    RefSeqi XP_957826.1. XM_952733.2.
    UniGenei Ncr.16984.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EJ6 X-ray 2.30 A/B/C/D 32-719 [» ]
    3ZJ4 X-ray 3.10 A/B/C/D 1-719 [» ]
    3ZJ5 X-ray 1.95 A/B/C/D 1-719 [» ]
    4AJ9 X-ray 1.85 A/B/C/D 38-719 [» ]
    4BIM X-ray 2.95 A/B/C/D 1-719 [» ]
    ProteinModelPortali Q9C169.
    SMRi Q9C169. Positions 40-714.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9C169. 1 interaction.
    MINTi MINT-2515988.
    STRINGi 5141.NCU00355.1.

    Protein family/group databases

    PeroxiBasei 5416. NcKat03.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFNCRT00000000465 ; EFNCRP00000000465 ; EFNCRG00000000465 .
    GeneIDi 3873876.
    KEGGi ncr:NCU00355.

    Phylogenomic databases

    eggNOGi COG0753.
    HOGENOMi HOG000087851.
    KOi K03781.
    OrthoDBi EOG7K9KBN.

    Miscellaneous databases

    EvolutionaryTracei Q9C169.

    Family and domain databases

    Gene3Di 2.40.180.10. 1 hit.
    3.40.50.880. 1 hit.
    InterProi IPR018028. Catalase.
    IPR020835. Catalase-like_dom.
    IPR024708. Catalase_AS.
    IPR024712. Catalase_clade2.
    IPR011614. Catalase_core.
    IPR010582. Catalase_immune_responsive.
    IPR029062. Class_I_gatase-like.
    [Graphical view ]
    PANTHERi PTHR11465. PTHR11465. 1 hit.
    Pfami PF00199. Catalase. 1 hit.
    PF06628. Catalase-rel. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038927. Catalase_clade2. 1 hit.
    PRINTSi PR00067. CATALASE.
    SMARTi SM01060. Catalase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56634. SSF56634. 1 hit.
    PROSITEi PS00438. CATALASE_2. 1 hit.
    PS51402. CATALASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Regulation and oxidation of two large monofunctional catalases."
      Michan S., Lledias F., Baldwin J.D., Natvig D.O., Hansberg W.
      Free Radic. Biol. Med. 33:521-532(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-58 AND 638-656, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, INDUCTION.
      Strain: 74-ORS23-1A.
      Tissue: Mycelium.
    2. "The genome sequence of the filamentous fungus Neurospora crassa."
      Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
      , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
      Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

    Entry informationi

    Entry nameiCAT3_NEUCR
    AccessioniPrimary (citable) accession number: Q9C169
    Secondary accession number(s): Q7RV04
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal 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