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Protein

Catalase-1

Gene

cat-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 5 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 annotation2 Publications

Cofactori

pH dependencei

Active from pH 4 to 12.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei89Heme1
Active sitei92PROSITE-ProRule annotation1 Publication1
Binding sitei129Heme1
Active sitei165PROSITE-ProRule annotation1 Publication1
Binding sitei178Heme1
Binding sitei375Heme1
Metal bindingi379Iron (heme axial ligand)1
Binding sitei386Heme1

GO - Molecular functioni

  • catalase activity Source: UniProtKB
  • heme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • conidium formation Source: UniProtKB
  • hydrogen peroxide catabolic process Source: GO_Central
  • response to hydrogen peroxide Source: GO_Central
  • response to oxidative stress Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.11.1.6. 3627.
SABIO-RKQ9C168.

Protein family/group databases

PeroxiBasei5207. NcKat01.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase-1 (EC:1.11.1.6)
Gene namesi
Name:cat-1
ORF Names:NCU08791
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:NCU08791.

Subcellular locationi

GO - Cellular componenti

  • ascospore wall Source: UniProtKB
  • cytosol Source: GO_Central
  • extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000849231 – 736Catalase-1Add BLAST736

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki356 ↔ 3793-(S-cysteinyl)-tyrosine (Cys-Tyr)

Post-translational modificationi

Glycosylated; with alpha-glucose and/or alpha-mannose.1 Publication

Keywords - PTMi

Glycoprotein, Thioether bond

Expressioni

Developmental stagei

Main catalase activity in conidia, during germination of conidia, and initial growth.1 Publication

Inductioni

During prestationary growth. By ethanol and in the presence of air by heat shock. Inactivated by isopropanol and 20 mM 3-amino-1,2,4-triazole.2 Publications

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

IntActiQ9C168. 1 interactor.
MINTiMINT-2515819.

Structurei

Secondary structure

1736
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi57 – 59Combined sources3
Beta strandi64 – 67Combined sources4
Helixi72 – 82Combined sources11
Beta strandi90 – 92Combined sources3
Beta strandi94 – 106Combined sources13
Turni109 – 111Combined sources3
Helixi115 – 117Combined sources3
Beta strandi124 – 131Combined sources8
Beta strandi133 – 135Combined sources3
Beta strandi143 – 145Combined sources3
Beta strandi148 – 155Combined sources8
Beta strandi158 – 169Combined sources12
Helixi175 – 177Combined sources3
Helixi178 – 185Combined sources8
Turni189 – 192Combined sources4
Helixi201 – 209Combined sources9
Helixi211 – 213Combined sources3
Helixi214 – 220Combined sources7
Helixi223 – 225Combined sources3
Beta strandi226 – 228Combined sources3
Helixi230 – 232Combined sources3
Beta strandi241 – 244Combined sources4
Beta strandi250 – 259Combined sources10
Helixi268 – 277Combined sources10
Helixi281 – 291Combined sources11
Beta strandi297 – 306Combined sources10
Helixi307 – 309Combined sources3
Beta strandi313 – 315Combined sources3
Turni326 – 328Combined sources3
Beta strandi332 – 341Combined sources10
Helixi346 – 349Combined sources4
Turni350 – 352Combined sources3
Helixi372 – 381Combined sources10
Helixi383 – 386Combined sources4
Helixi391 – 393Combined sources3
Turni395 – 397Combined sources3
Beta strandi423 – 425Combined sources3
Turni436 – 439Combined sources4
Helixi458 – 461Combined sources4
Helixi465 – 473Combined sources9
Helixi476 – 491Combined sources16
Helixi496 – 506Combined sources11
Turni507 – 509Combined sources3
Helixi511 – 521Combined sources11
Helixi543 – 545Combined sources3
Beta strandi549 – 551Combined sources3
Beta strandi557 – 561Combined sources5
Helixi568 – 580Combined sources13
Beta strandi584 – 590Combined sources7
Beta strandi595 – 597Combined sources3
Beta strandi606 – 608Combined sources3
Turni609 – 611Combined sources3
Helixi614 – 616Combined sources3
Beta strandi617 – 622Combined sources6
Helixi626 – 633Combined sources8
Helixi636 – 647Combined sources12
Beta strandi651 – 655Combined sources5
Helixi658 – 666Combined sources9
Beta strandi676 – 678Combined sources3
Beta strandi680 – 682Combined sources3
Beta strandi685 – 690Combined sources6
Turni693 – 697Combined sources5
Helixi709 – 718Combined sources10
Helixi723 – 727Combined sources5
Helixi731 – 733Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SY7X-ray1.75A/B22-736[»]
ProteinModelPortaliQ9C168.
SMRiQ9C168.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9C168.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

HOGENOMiHOG000087851.
InParanoidiQ9C168.
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.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
IPR029062. Class_I_gatase-like.
IPR002818. DJ-1/PfpI.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
PF01965. DJ-1_PfpI. 1 hit.
[Graphical view]
PIRSFiPIRSF038927. Catalase_clade2. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9C168-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNIISQAGQ KAKEALTSAP SSKKVDDLKN EFKETDKSAR LTTDYGVKQT
60 70 80 90 100
TADDWLRIVS DDKIGPSLLE DPFARERIMR FDHERIPERV VHARGSGAFG
110 120 130 140 150
KFKVYESASD LTMAPVLTDT SRETPVFVRF STVLGSRGSA DTVRDVRGFA
160 170 180 190 200
VKFYTEEGNW DLVGNNIPVF FIQDAIKFPD VIHAGKPEPH NEVPQAQSAH
210 220 230 240 250
NNFWDFQFNH TEATHMFTWA MSDRAIPRSL RMMQGFGVNT YTLINAQGKR
260 270 280 290 300
HFVKFHWTPE LGVHSLVWDE ALKLAGQDPD FHRKDLWEAI ENGAYPKWKF
310 320 330 340 350
GIQAIAEEDE HKFDFDILDA TKIWPEDLVP VRYIGEMELN RNPDEFFPQT
360 370 380 390 400
EQIAFCTSHV VNGIGFSDDP LLQGRNFSYF DTQISRLGVN FQELPINRPV
410 420 430 440 450
CPVMNFNRDG AMRHTISRGT VNYYPNRFDA CPPASLKEGG YLEYAQKVAG
460 470 480 490 500
IKARARSAKF KEHFSQAQLF YNSMSPIEKQ HMINAFGFEL DHCEDPVVYG
510 520 530 540 550
RMVQRLADID LGLAQTIAEM VGGEAPTTTN HPNHGRKTIN LSQTEFPPAT
560 570 580 590 600
PTIKSRRVAI IIADGYDNVA YDAAYAAISA NQAIPLVIGP RRSKVTAANG
610 620 630 640 650
STVQPHHHLE GFRSTMVDAI FIPGGAKAAE TLSKNGRALH WIREAFGHLK
660 670 680 690 700
AIGATGEAVD LVAKAIALPQ VTVSSEAEVH ESYGVVTLKK VKPESFTDAV
710 720 730
KIAKGAAGFL GEFFYAIAQH RNWDRELDGL HSMIAY
Length:736
Mass (Da):82,268
Last modified:January 4, 2005 - v2
Checksum:i76AC6E3A51336299
GO

Sequence cautioni

The sequence EAA26998 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY027545 Genomic DNA. Translation: AAK15808.2.
CM002238 Genomic DNA. Translation: EAA26998.1. Different initiation.
RefSeqiXP_956234.1. XM_951141.3.

Genome annotation databases

EnsemblFungiiEAA26998; EAA26998; NCU08791.
GeneIDi3872372.
KEGGincr:NCU08791.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY027545 Genomic DNA. Translation: AAK15808.2.
CM002238 Genomic DNA. Translation: EAA26998.1. Different initiation.
RefSeqiXP_956234.1. XM_951141.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SY7X-ray1.75A/B22-736[»]
ProteinModelPortaliQ9C168.
SMRiQ9C168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9C168. 1 interactor.
MINTiMINT-2515819.

Protein family/group databases

PeroxiBasei5207. NcKat01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAA26998; EAA26998; NCU08791.
GeneIDi3872372.
KEGGincr:NCU08791.

Organism-specific databases

EuPathDBiFungiDB:NCU08791.

Phylogenomic databases

HOGENOMiHOG000087851.
InParanoidiQ9C168.
KOiK03781.
OrthoDBiEOG092C0NOX.

Enzyme and pathway databases

BRENDAi1.11.1.6. 3627.
SABIO-RKQ9C168.

Miscellaneous databases

EvolutionaryTraceiQ9C168.

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.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
IPR029062. Class_I_gatase-like.
IPR002818. DJ-1/PfpI.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
PF01965. DJ-1_PfpI. 1 hit.
[Graphical view]
PIRSFiPIRSF038927. Catalase_clade2. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAT1_NEUCR
AccessioniPrimary (citable) accession number: Q9C168
Secondary accession number(s): Q7RUZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: January 4, 2005
Last modified: November 2, 2016
This is version 129 of the entry and version 2 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.