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Reviewed, UniProtKB/Swiss-Prot Q9C169 (CAT3_NEUCR)

Last modified November 4, 2008. Version 55. 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

Names and origin

Protein namesRecommended name:
    Catalase-3
    EC=1.11.1.6
Gene names
Name: cat-3
ORF Names: NCU00355
OrganismNeurospora crassa [Complete proteome]
Taxonomic identifier5141 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length719 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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 H(2)O(2) = O(2) + 2 H(2)O.

Cofactor

Heme group.

Developmental stage

Activity is predominant during late exponential growth and at the start of the conidiation process.

Induction

Induced under stress conditions, such as H(2)O(2), paraquat, cadmium, heat shock, uric acid and nitrate treatment.

Sequence similarities

Belongs to the catalase family.

Ontologies

Keywords

   Biological processHydrogen peroxide
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Direct protein sequencing

Gene Ontology (GO)

   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 3012
PRO_0000004687
Chain31 – 719689Catalase-3
PRO_0000004688

Sites

Active site1021 By similarity
Active site1751 By similarity
Metal binding3891Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9C169-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 72790DE3310B64D0

FASTA71979,228
        10         20         30         40         50         60 
MRVNALLPLS GLIGTALAAC PFADPSALGR RAEGGEVDAR QRLKEVEVDD NGQFMTTDFG 

        70         80         90        100        110        120 
GNIEEQFSLK AGGRGSTLLE DFIFRQKLQH FDHERIPERV VHARGAGAHG IFTSYGDWSN 

       130        140        150        160        170        180 
ITAASFLGAK DKQTPVFVRF STVAGSRGSA DTARDVHGFA TRFYTDEGNF DIVGNNIPVF 

       190        200        210        220        230        240 
FIQDAIRFPD LIHSVKPSPD NEVPQAATAH DSAWDFFSSQ PSALHTLFWA MSGNGIPRSY 

       250        260        270        280        290        300 
RHMDGFGIHT FRLVTEDGKS KLVKWHWKTK QGKAALVWEE AQVLAGKNAD FHRQDLWDAI 

       310        320        330        340        350        360 
ESGNAPSWEL AVQLIDEDKA QAYGFDLLDP TKFLPEEFAP LQVLGEMTLN RNPMNYFAET 

       370        380        390        400        410        420 
EQISFQPGHI VRGVDFTEDP LLQGRLYSYL DTQLNRHRGP NFEQLPINRP VSGVHNNHRD 

       430        440        450        460        470        480 
GQGQAWIHKN IHHYSPSYLN KGYPAQANQT VGRGFFTTPG RTASGVLNRE LSATFDDHYT 

       490        500        510        520        530        540 
QPRLFFNSLT PVEQQFVINA IRFEASHVTN EQVKKNVLEQ LNKISNDVAK RVAVALGLEA 

       550        560        570        580        590        600 
PQPDPTYYHN NVTRGVSIFN ESLPTIATLR VGVLSTTKGG SLDKAKALKE QLEKDGLKVT 

       610        620        630        640        650        660 
VIAEYLASGV DQTYSAADAT AFDAVVVAEG AERVFSGKGA MSPLFPAGRP SQILTDGYRW 

       670        680        690        700        710 
GKPVAAVGSA KKALQSIGVE EKEAGVYAGA QDEVIKGVEE GLKVFKFLER FAVDGDDEE 

« Hide

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 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. 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.

Cross-references

Sequence databases

AY027544 Genomic DNA. Translation: AAK15807.1.
AABX02000001 Genomic DNA. Translation: EAA28590.1.
RefSeqXP_957826.1.

3D structure databases

HSSPHSSP built from PDB template 1CF9 based on UniProtKB P21179.
ModBaseSearch...

Protein family/group databases

PeroxiBase5416. NcKat03.

Genome annotation databases

GeneID3873876.
KEGGncr:NCU00355.
NMPDRfig|5141.1.peg.374.

Enzyme and pathway databases

BioCycNCRA-XX3-01:NCRA-XX3-01-004065-MON.

Family and domain databases

InterProIPR002226. Catalase.
IPR010582. Catalase-rel.
IPR011614. Catalase_N.
[Graphical view]
Gene3DG3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHERPTHR11465. Catalase. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PRINTSPR00067. CATALASE.
ProDomPD000510. Catalase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00437. CATALASE_1. False negative.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Entry information

Entry nameCAT3_NEUCR
AccessionPrimary (citable) accession number: Q9C169
Secondary accession number(s): Q7RV04
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: June 1, 2001
Last modified: November 4, 2008
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

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