Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot P78574 (CATA_ASPFU)

Last modified November 25, 2008. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 A
    EC=1.11.1.6
Alternative name(s):
    Fast catalase
Gene names
Name: catA
ORF Names: AFUA_6G03890
OrganismAspergillus fumigatus (Sartorya fumigata) [Complete proteome]
Taxonomic identifier5085 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length750 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Heme group.

Sequence similarities

Belongs to the catalase family.

Ontologies

Keywords

   Biological processHydrogen peroxide
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 750750Catalase A
PRO_0000084915

Sites

Active site931 By similarity
Active site1661 By similarity
Metal binding3801Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict3281D → N in AAB47761. Ref.1
Sequence conflict4621S → N in AAB47761. Ref.1
Sequence conflict5771F → S in AAB47761. Ref.1
Sequence conflict604 – 6052DG → T in AAB47761. Ref.1
Sequence conflict6811D → H in AAB47761. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P78574-1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 95AA8090D28BA007

FASTA75084,633
        10         20         30         40         50         60 
MATKIAGGLH RAQEVLQNTS SKSKKLVDLE RDTADAHTQQ PLTTDHGVRV SNTDQWLRVT 

        70         80         90        100        110        120 
NDRRTGPSLL EDQIAREKIH RFDHERIPER VVHARGTGAF GNFKLKESIE DLTYAGVLTD 

       130        140        150        160        170        180 
TSRNTPVFVR FSTVQGSRGS ADTVRDVRGF AVKFYTDEGN WDIVGNNIPV FFIQDAVKFP 

       190        200        210        220        230        240 
DFVHAVKPEP HNEVPQAQTA HNNFWDFVYL HPEATHMFMW AMSDRAIPRS YRMMQGFGVN 

       250        260        270        280        290        300 
TFALVNKEGK RHFVKFHWIP HLGVHSLVWD EALKLGGQDP DFHRKDLMEA IDNKAYPKWD 

       310        320        330        340        350        360 
FAIQVIPEEK QDDFEFDILD ATKIWPEDLV PLRVIGELEL NRNVDEFFPQ TEQVAFCTSH 

       370        380        390        400        410        420 
IVPGIDFTDD PLLQGRNFSY FDTQISRLGI NWEELPINRP VCPVLNHNRD GQMRHRITQG 

       430        440        450        460        470        480 
TVNYWPNRFE AVPPTGTKGS GVGGGFTTYP QRVEGIKNRA LSDKFREHHN QAQLFYNSMS 

       490        500        510        520        530        540 
EHEKLHMKKA FSFELDHCDD PTVYERLAGH RLAEIDLELA QKVAEMVGAP IPAKALKQNH 

       550        560        570        580        590        600 
GRRAPHLSQT EFIPKNPTIA SRRIAIIIGD GYDPVAFTGL KTAIKAASAL PFIIGTKRSA 

       610        620        630        640        650        660 
IYADGEDKTS SKGIIPDHHY DGQRSTMFDA TFIPGGPHVA TLRQNGQIKY WISETFGHLK 

       670        680        690        700        710        720 
ALGATGEAVD LVKETLSGTL DVQVASSQSP EPVEWYGVVT AGGKQKPESF KESVQILKGA 

       730        740        750 
TDFVGKFFYQ ISQHRNYQRE LDGLASTIAF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing and characterization of Aspergillus fumigatus catalase genes."
Wysong D.R., Diamond R.D., Robbins P.W.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

U87630 Genomic DNA. Translation: AAB47761.1.
AAHF01000012 Genomic DNA. Translation: EAL85650.1.
RefSeqXP_747688.1.

3D structure databases

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

Protein family/group databases

PeroxiBase5205. AfumKat01.

Genome annotation databases

GeneID3505035.
KEGGafm:AFUA_6G03890.

Phylogenomic databases

HOGENOMP78574.

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. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATA_ASPFU
AccessionPrimary (citable) accession number: P78574
Secondary accession number(s): Q4WD88
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 6, 2005
Last modified: November 25, 2008
This is version 53 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

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