Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P49315 (CATA1_NICPL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length485 AA.
Sequence statusFragment.
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.

Catalytic activity

2 H2O2 = O2 + 2 H2O.

Cofactor

Heme group.

Subunit structure

Homotetramer By similarity.

Subcellular location

Peroxisome Potential.

Induction

By paraquat and 3-aminotriazole.

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

   Cellular_componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncatalase activity

Inferred from electronic annotation. Source: UniProtKB-EC

heme binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 485›485Catalase isozyme 1
PRO_0000084949

Sites

Active site581 By similarity
Active site1311 By similarity
Metal binding3411Iron (heme axial ligand) By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P49315 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 00BA53BEF7699A13

FASTA48555,850
        10         20         30         40         50         60 
PSSAFNSPFC TTNSGAPVFN NNSSLTVGAR GPVLLEDYHL VEKLANFDRE RVPERVVHAR 

        70         80         90        100        110        120 
GASAKGFFEV THDITHLTCA DFLRAPGVQT PVIVRFSTVI HERGSPETLR DPRGFAVKFY 

       130        140        150        160        170        180 
TREGNFDLVG NNFPVFFIRD GMKFPDMVHA LKPNPKSHIQ ENWRVLDFFS HVPESLHMFT 

       190        200        210        220        230        240 
FLFDDIGIPQ DYRHMDGSGV HTFTLINKAG KSTYVKFHWK PTCGVKSLLE DEAARVGGAN 

       250        260        270        280        290        300 
HSHATQDLYD SIAAGNYPEW KLFIQTMDPD HEDRFDFDPL DVTKTWPEDI LPLQPVGRLV 

       310        320        330        340        350        360 
LNKNIDNFSN ENEQLAFCPS IVVPGVYYSD DKMLQTRIFS YSDTQRYRLG PNYLQLPANA 

       370        380        390        400        410        420 
PKCAHHNNHY DGSMNFMHRD EEIDYFPSRY DPVRHAEKYP IPSTMCTGKR EKCVIQKENN 

       430        440        450        460        470        480 
FKQPGERYRS FTPDRQERFI RRWVETLSDP RITYEIRSIW ISYWSQADKS LGQKLASRLN 


VRPSI 

« Hide

References

[1]"Molecular identification of catalases from Nicotiana plumbaginifolia (L.)."
Willekens H., Villarroel R., van Montagu M., Inze D., van Camp W.
FEBS Lett. 352:79-83(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z36975 mRNA. Translation: CAA85424.1.
PIRS48650.

3D structure databases

ProteinModelPortalP49315.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP49315.
ProMEXP49315.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.180.10. 1 hit.
InterProIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERPTHR11465. PTHR11465. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSPR00067. CATALASE.
SMARTSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMSSF56634. SSF56634. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATA1_NICPL
AccessionPrimary (citable) accession number: P49315
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families