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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: Annotation score: 4 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.PROSITE-ProRule annotation1 Publication

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei102PROSITE-ProRule annotation1
Active sitei175PROSITE-ProRule annotation1
Metal bindingi389Iron (heme axial ligand)By similarity1

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000001805 Componenti: Chromosome 3, Linkage Group III

Organism-specific databases

EuPathDBiFungiDB:NCU00355.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000000468719 – 301 PublicationAdd BLAST12
ChainiPRO_000000468831 – 719Catalase-3Add BLAST689

Proteomic databases

PRIDEiQ9C169.

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 interactor.
MINTiMINT-2515988.

Structurei

Secondary structure

1719
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi41 – 46Combined sources6
Beta strandi70 – 72Combined sources3
Helixi82 – 92Combined sources11
Beta strandi100 – 102Combined sources3
Beta strandi104 – 116Combined sources13
Turni119 – 121Combined sources3
Helixi125 – 127Combined sources3
Beta strandi133 – 141Combined sources9
Beta strandi143 – 145Combined sources3
Beta strandi153 – 155Combined sources3
Beta strandi158 – 165Combined sources8
Beta strandi168 – 179Combined sources12
Helixi185 – 187Combined sources3
Helixi188 – 195Combined sources8
Turni199 – 201Combined sources3
Helixi211 – 219Combined sources9
Helixi221 – 223Combined sources3
Helixi224 – 230Combined sources7
Helixi233 – 235Combined sources3
Beta strandi236 – 238Combined sources3
Helixi240 – 242Combined sources3
Beta strandi251 – 254Combined sources4
Beta strandi260 – 271Combined sources12
Helixi278 – 287Combined sources10
Helixi291 – 301Combined sources11
Beta strandi307 – 315Combined sources9
Helixi317 – 319Combined sources3
Beta strandi323 – 325Combined sources3
Turni336 – 338Combined sources3
Beta strandi342 – 351Combined sources10
Helixi356 – 359Combined sources4
Turni360 – 362Combined sources3
Helixi380 – 397Combined sources18
Beta strandi398 – 400Combined sources3
Helixi402 – 404Combined sources3
Turni406 – 408Combined sources3
Beta strandi427 – 429Combined sources3
Beta strandi434 – 436Combined sources3
Turni438 – 442Combined sources5
Beta strandi449 – 451Combined sources3
Beta strandi462 – 469Combined sources8
Helixi473 – 475Combined sources3
Helixi480 – 487Combined sources8
Helixi491 – 505Combined sources15
Helixi511 – 524Combined sources14
Helixi526 – 536Combined sources11
Helixi545 – 547Combined sources3
Beta strandi558 – 561Combined sources4
Beta strandi570 – 574Combined sources5
Beta strandi577 – 580Combined sources4
Helixi581 – 593Combined sources13
Turni594 – 596Combined sources3
Beta strandi598 – 605Combined sources8
Beta strandi611 – 613Combined sources3
Turni614 – 616Combined sources3
Helixi619 – 621Combined sources3
Beta strandi623 – 627Combined sources5
Helixi631 – 635Combined sources5
Helixi637 – 640Combined sources4
Helixi649 – 659Combined sources11
Beta strandi664 – 667Combined sources4
Helixi668 – 670Combined sources3
Helixi671 – 676Combined sources6
Beta strandi681 – 683Combined sources3
Beta strandi686 – 690Combined sources5
Helixi691 – 704Combined sources14
Helixi708 – 710Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9C169.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000087851.
InParanoidiQ9C169.
KOiK03781.
OrthoDBiEOG092C0NOX.

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

        10         20         30         40         50
MRVNALLPLS GLIGTALAAC PFADPSALGR RAEGGEVDAR QRLKEVEVDD
60 70 80 90 100
NGQFMTTDFG GNIEEQFSLK AGGRGSTLLE DFIFRQKLQH FDHERIPERV
110 120 130 140 150
VHARGAGAHG IFTSYGDWSN ITAASFLGAK DKQTPVFVRF STVAGSRGSA
160 170 180 190 200
DTARDVHGFA TRFYTDEGNF DIVGNNIPVF FIQDAIRFPD LIHSVKPSPD
210 220 230 240 250
NEVPQAATAH DSAWDFFSSQ PSALHTLFWA MSGNGIPRSY RHMDGFGIHT
260 270 280 290 300
FRLVTEDGKS KLVKWHWKTK QGKAALVWEE AQVLAGKNAD FHRQDLWDAI
310 320 330 340 350
ESGNAPSWEL AVQLIDEDKA QAYGFDLLDP TKFLPEEFAP LQVLGEMTLN
360 370 380 390 400
RNPMNYFAET EQISFQPGHI VRGVDFTEDP LLQGRLYSYL DTQLNRHRGP
410 420 430 440 450
NFEQLPINRP VSGVHNNHRD GQGQAWIHKN IHHYSPSYLN KGYPAQANQT
460 470 480 490 500
VGRGFFTTPG RTASGVLNRE LSATFDDHYT QPRLFFNSLT PVEQQFVINA
510 520 530 540 550
IRFEASHVTN EQVKKNVLEQ LNKISNDVAK RVAVALGLEA PQPDPTYYHN
560 570 580 590 600
NVTRGVSIFN ESLPTIATLR VGVLSTTKGG SLDKAKALKE QLEKDGLKVT
610 620 630 640 650
VIAEYLASGV DQTYSAADAT AFDAVVVAEG AERVFSGKGA MSPLFPAGRP
660 670 680 690 700
SQILTDGYRW GKPVAAVGSA KKALQSIGVE EKEAGVYAGA QDEVIKGVEE
710
GLKVFKFLER FAVDGDDEE
Length:719
Mass (Da):79,228
Last modified:June 1, 2001 - v1
Checksum:i72790DE3310B64D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY027544 Genomic DNA. Translation: AAK15807.1.
CM002238 Genomic DNA. Translation: EAA28590.1.
RefSeqiXP_957826.1. XM_952733.3.

Genome annotation databases

EnsemblFungiiEAA28590; EAA28590; NCU00355.
GeneIDi3873876.
KEGGincr:NCU00355.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY027544 Genomic DNA. Translation: AAK15807.1.
CM002238 Genomic DNA. Translation: EAA28590.1.
RefSeqiXP_957826.1. XM_952733.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9C169. 1 interactor.
MINTiMINT-2515988.

Protein family/group databases

PeroxiBasei5416. NcKat03.

Proteomic databases

PRIDEiQ9C169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAA28590; EAA28590; NCU00355.
GeneIDi3873876.
KEGGincr:NCU00355.

Organism-specific databases

EuPathDBiFungiDB:NCU00355.

Phylogenomic databases

HOGENOMiHOG000087851.
InParanoidiQ9C169.
KOiK03781.
OrthoDBiEOG092C0NOX.

Miscellaneous databases

EvolutionaryTraceiQ9C169.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 116 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.