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Q9C169

- CAT3_NEUCR

UniProt

Q9C169 - CAT3_NEUCR

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Protein
Catalase-3
Gene
cat-3, NCU00355
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

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 Publication

Cofactori

Heme group.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei102 – 1021 By similarity
Active sitei175 – 1751 By similarity
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
Complete GO annotation...

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 – 1818 Reviewed prediction
Add
BLAST
Propeptidei19 – 3012
PRO_0000004687Add
BLAST
Chaini31 – 719689Catalase-3
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiQ9C169.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 98 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

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