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Reviewed, UniProtKB/Swiss-Prot Q9C168 (CAT1_NEUCR)

Last modified January 19, 2010. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Catalase-1
    EC=1.11.1.6
Gene names
Name: cat-1
ORF Names: NCU08791
OrganismNeurospora crassa [Complete proteome]
Taxonomic identifier5141 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

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Protein attributes

Sequence length736 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide By similarity.

Catalytic activity

2 H2O2 = O2 + 2 H2O. Ref.1 Ref.4

Cofactor

Heme group. Ref.5

Subunit structure

Homotetramer. Ref.4

Subcellular location

Secreted › cell wall. Note: Principally associated with the cell wall of conidia. Ref.4

Developmental stage

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

Induction

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

Post-translational modification

Glycosylated; with alpha-glucose and/or alpha-mannose. Ref.4

Sequence similarities

Belongs to the catalase family.

Biophysicochemical properties

pH dependence:

Active from pH 4 to 12.

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Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentCell wall
Secreted
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMGlycoprotein
Thioether bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processconidium formation Ref.4

Inferred from direct assay. Source: UniProtKB

hydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentascospore wall Ref.4

Inferred from direct assay. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatalase activity Ref.4

Inferred from direct assay. Source: UniProtKB

heme binding Ref.5

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 736736Catalase-1
PRO_0000084923

Sites

Active site921 Ref.5
Active site1651 Ref.5
Metal binding3791Iron (heme axial ligand)
Binding site891Heme
Binding site1291Heme
Binding site1781Heme
Binding site3751Heme
Binding site3861Heme

Amino acid modifications

Cross-link356 ↔ 3793-(S-cysteinyl)-tyrosine (Cys-Tyr)

Secondary structure

1 ............................................................................................................................. 736
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9C168-1 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 76AC6E3A51336299

FASTA73682,268
        10         20         30         40         50         60 
MSNIISQAGQ KAKEALTSAP SSKKVDDLKN EFKETDKSAR LTTDYGVKQT TADDWLRIVS 

        70         80         90        100        110        120 
DDKIGPSLLE DPFARERIMR FDHERIPERV VHARGSGAFG KFKVYESASD LTMAPVLTDT 

       130        140        150        160        170        180 
SRETPVFVRF STVLGSRGSA DTVRDVRGFA VKFYTEEGNW DLVGNNIPVF FIQDAIKFPD 

       190        200        210        220        230        240 
VIHAGKPEPH NEVPQAQSAH NNFWDFQFNH TEATHMFTWA MSDRAIPRSL RMMQGFGVNT 

       250        260        270        280        290        300 
YTLINAQGKR HFVKFHWTPE LGVHSLVWDE ALKLAGQDPD FHRKDLWEAI ENGAYPKWKF 

       310        320        330        340        350        360 
GIQAIAEEDE HKFDFDILDA TKIWPEDLVP VRYIGEMELN RNPDEFFPQT EQIAFCTSHV 

       370        380        390        400        410        420 
VNGIGFSDDP LLQGRNFSYF DTQISRLGVN FQELPINRPV CPVMNFNRDG AMRHTISRGT 

       430        440        450        460        470        480 
VNYYPNRFDA CPPASLKEGG YLEYAQKVAG IKARARSAKF KEHFSQAQLF YNSMSPIEKQ 

       490        500        510        520        530        540 
HMINAFGFEL DHCEDPVVYG RMVQRLADID LGLAQTIAEM VGGEAPTTTN HPNHGRKTIN 

       550        560        570        580        590        600 
LSQTEFPPAT PTIKSRRVAI IIADGYDNVA YDAAYAAISA NQAIPLVIGP RRSKVTAANG 

       610        620        630        640        650        660 
STVQPHHHLE GFRSTMVDAI FIPGGAKAAE TLSKNGRALH WIREAFGHLK AIGATGEAVD 

       670        680        690        700        710        720 
LVAKAIALPQ VTVSSEAEVH ESYGVVTLKK VKPESFTDAV KIAKGAAGFL GEFFYAIAQH 

       730 
RNWDRELDGL HSMIAY

« Hide

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References

« Hide 'large scale' references
[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: 12160934] [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. expand/collapse author list , 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: 12712197] [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: 11728803] [Abstract]
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, GLYCOSYLATION.
[5]"Unusual Cys-Tyr covalent bond in a large catalase."
Diaz A., Horjales E., Rudino-Pinera E., Arreola R., Hansberg W.
J. Mol. Biol. 342:971-985(2004) [PubMed: 15342250] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 22-736 IN COMPLEX WITH COFACTOR, ACTIVE SITE, CROSS-LINK.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY027545 Genomic DNA. Translation: AAK15808.2.
AABX02000017 Genomic DNA. Translation: EAA26998.1. Different initiation.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SY7X-ray1.75A/B22-736[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9C168.

Protein family/group databases

PeroxiBase5207. NcKat01.

Genome annotation databases

NMPDRfig|5141.1.peg.8841.

Phylogenomic databases

eggNOGfuNOG06986.
OrthoDBEOG9QNPCB.
PhylomeDBQ9C168.

Enzyme and pathway databases

BioCycNCRA-XX3-01:NCRA-XX3-01-003650-MONOMER.
BRENDA1.11.1.6. 266.

Family and domain databases

InterProIPR002226. Catalase.
IPR020835. Catalase-like_haem-dep.
IPR010582. Catalase-rel_immune_responsive.
IPR011614. Catalase_N.
IPR018028. Catalase_rel_subgroup.
IPR002818. ThiJ/PfpI.
[Graphical view]
Gene3DG3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHERPTHR11465. Catalase. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
PF01965. DJ-1_PfpI. 1 hit.
[Graphical view]
PRINTSPR00067. CATALASE.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCAT1_NEUCR
AccessionPrimary (citable) accession number: Q9C168
Secondary accession number(s): Q7RUZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: January 4, 2005
Last modified: January 19, 2010
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents