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Reviewed, UniProtKB/Swiss-Prot P90682 (CATA_ASCSU)

Last modified June 16, 2009. Version 46. 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
    EC=1.11.1.6
Gene names
Name: CAT
OrganismAscaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifier6253 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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 H2O2 = O2 + 2 H2O.

Cofactor

Heme group By similarity.

Subcellular location

Peroxisome By similarity.

Sequence similarities

Belongs to the catalase family.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentPeroxisome
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: EC

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 541541Catalase
PRO_0000084908

Sites

Active site741 By similarity
Active site1471 By similarity
Metal binding3571Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
P90682-1 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: 70890E1AECA170B0

FASTA54161,962
        10         20         30         40         50         60 
MPQTKGKPHE EQLEQYKNSQ TKPFVLTTSN GAPIFNKKAS LTVGPRGPLL LQDVVFLDEM 

        70         80         90        100        110        120 
AHFDRERIPE RVVHAKGGGA HGFFEVTDDI TKYCKADVFS TIGKRTPIFI RFSTVGGELG 

       130        140        150        160        170        180 
SADTQRDPRG FAIKFYTEEG NWDLVGNNTP IFFIRDPIFF PNFIHTQKRN PVTHLKDPNM 

       190        200        210        220        230        240 
MWDFFSLRPE TTHQVMILFG DRGIPDGFRH MDGFGSHTFK LVNKDGNAVY CKFHIKTAQG 

       250        260        270        280        290        300 
IRNLPPDVAI KLAGEDPDYS IRDLYDSIEN GNYPVWRLMI QVMTFEEAAN YRFNPFDITK 

       310        320        330        340        350        360 
VWSHKEFPLI LVGKIVLNKN PTNYFAEVEQ IAFAPSHVVP GIEFSPDKML QGRLFAYPDT 

       370        380        390        400        410        420 
QFHRLGPNYV QLPINCPYRS RAHNTQRDGC FALDYNQGGM PTYHPNSFNG AIERTDVKES 

       430        440        450        460        470        480 
AWSVSGDVDR FNGDDEDNFS QPRDLWLKVM DETERARLVD NIADSLKYCK AFIQERAINN 

       490        500        510        520        530        540 
FTQVHQDFGN ALRNALQKAN EAMQKKREEE AEFNAKESVM MPCAIDDRMK NISNLAKYCK 


Y 

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References

[1]Eckelt V.H.O.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

Y10611 mRNA. Translation: CAA71618.1.

3D structure databases

HSSPHSSP built from PDB template 1F4J based on UniProtKB P04040.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.11.1.6. 649.

Family and domain databases

InterProIPR002226. Catalase.
IPR010582. Catalase-rel_immune_responsive.
IPR011614. Catalase_N.
IPR018028. Catalase_rel_subgroup.
[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. 2 hits.
[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_ASCSU
AccessionPrimary (citable) accession number: P90682
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: June 16, 2009
This is version 46 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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