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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891Heme
Active sitei92 – 921PROSITE-ProRule annotation1 Publication
Binding sitei129 – 1291Heme
Active sitei165 – 1651PROSITE-ProRule annotation1 Publication
Binding sitei178 – 1781Heme
Binding sitei375 – 3751Heme
Metal bindingi379 – 3791Iron (heme axial ligand)
Binding sitei386 – 3861Heme

GO - Molecular functioni

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

GO - Biological processi

  • cellular oxidant detoxification Source: GOC
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 736736Catalase-1PRO_0000084923Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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 interaction.
MINTiMINT-2515819.

Structurei

Secondary structure

1
736
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi57 – 593Combined sources
Beta strandi64 – 674Combined sources
Helixi72 – 8211Combined sources
Beta strandi90 – 923Combined sources
Beta strandi94 – 10613Combined sources
Turni109 – 1113Combined sources
Helixi115 – 1173Combined sources
Beta strandi124 – 1318Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi148 – 1558Combined sources
Beta strandi158 – 16912Combined sources
Helixi175 – 1773Combined sources
Helixi178 – 1858Combined sources
Turni189 – 1924Combined sources
Helixi201 – 2099Combined sources
Helixi211 – 2133Combined sources
Helixi214 – 2207Combined sources
Helixi223 – 2253Combined sources
Beta strandi226 – 2283Combined sources
Helixi230 – 2323Combined sources
Beta strandi241 – 2444Combined sources
Beta strandi250 – 25910Combined sources
Helixi268 – 27710Combined sources
Helixi281 – 29111Combined sources
Beta strandi297 – 30610Combined sources
Helixi307 – 3093Combined sources
Beta strandi313 – 3153Combined sources
Turni326 – 3283Combined sources
Beta strandi332 – 34110Combined sources
Helixi346 – 3494Combined sources
Turni350 – 3523Combined sources
Helixi372 – 38110Combined sources
Helixi383 – 3864Combined sources
Helixi391 – 3933Combined sources
Turni395 – 3973Combined sources
Beta strandi423 – 4253Combined sources
Turni436 – 4394Combined sources
Helixi458 – 4614Combined sources
Helixi465 – 4739Combined sources
Helixi476 – 49116Combined sources
Helixi496 – 50611Combined sources
Turni507 – 5093Combined sources
Helixi511 – 52111Combined sources
Helixi543 – 5453Combined sources
Beta strandi549 – 5513Combined sources
Beta strandi557 – 5615Combined sources
Helixi568 – 58013Combined sources
Beta strandi584 – 5907Combined sources
Beta strandi595 – 5973Combined sources
Beta strandi606 – 6083Combined sources
Turni609 – 6113Combined sources
Helixi614 – 6163Combined sources
Beta strandi617 – 6226Combined sources
Helixi626 – 6338Combined sources
Helixi636 – 64712Combined sources
Beta strandi651 – 6555Combined sources
Helixi658 – 6669Combined sources
Beta strandi676 – 6783Combined sources
Beta strandi680 – 6823Combined sources
Beta strandi685 – 6906Combined sources
Turni693 – 6975Combined sources
Helixi709 – 71810Combined sources
Helixi723 – 7275Combined sources
Helixi731 – 7333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SY7X-ray1.75A/B22-736[»]
ProteinModelPortaliQ9C168.
SMRiQ9C168. Positions 39-736.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9C168.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

HOGENOMiHOG000087851.
InParanoidiQ9C168.
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.
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 EAA26998.1 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

EnsemblFungiiEFNCRT00000004624; EFNCRP00000004624; EFNCRG00000004618.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1SY7X-ray1.75A/B22-736[»]
ProteinModelPortaliQ9C168.
SMRiQ9C168. Positions 39-736.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9C168. 1 interaction.
MINTiMINT-2515819.

Protein family/group databases

PeroxiBasei5207. NcKat01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000004624; EFNCRP00000004624; EFNCRG00000004618.
GeneIDi3872372.
KEGGincr:NCU08791.

Organism-specific databases

EuPathDBiFungiDB:NCU08791.

Phylogenomic databases

HOGENOMiHOG000087851.
InParanoidiQ9C168.
KOiK03781.
OrthoDBiEOG7K9KBN.

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...

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 48-60; 152-167 AND 254-266, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, INDUCTION.
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
    Tissue: Conidium.
  2. Michan S., Ebbole D., Hansberg W.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO N-TERMINUS.
  3. "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.
  4. "Molecular and kinetic study of catalase-1, a durable large catalase of Neurospora crassa."
    Diaz A., Rangel P., Montes de Oca Y., Lledias F., Hansberg W.
    Free Radic. Biol. Med. 31:1323-1333(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, GLYCOSYLATION.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 22-736 IN COMPLEX WITH COFACTOR, ACTIVE SITE, CROSS-LINK.

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: February 17, 2016
This is version 125 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.