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Reviewed, UniProtKB/Swiss-Prot P29756 (CATA1_SOYBN)

Last modified February 9, 2010. Version 66. 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-1/2
    EC=1.11.1.6
Gene names
Name: CAT1
AND
Name: CAT2
OrganismGlycine max (Soybean)
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycine

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
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.

Subunit structure

Homotetramer.

Subcellular location

Peroxisome By similarity. Glyoxysome By similarity.

Sequence similarities

Belongs to the catalase family.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentGlyoxysome
Peroxisome
   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 componentglyoxysome

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 – 492492Catalase-1/2
PRO_0000084963

Sites

Active site651 By similarity
Active site1381 By similarity
Metal binding3481Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
P29756-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: CE8AFE8BEEA483C6

FASTA49256,847
        10         20         30         40         50         60 
MDPYKNRPSS AFNSPFWTTN SGAPIWNNNS SLTVGSRGPI LLEDYHLVEK LANFDRERIP 

        70         80         90        100        110        120 
ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPLI VRFSTVIHER GSPETLRDPR 

       130        140        150        160        170        180 
GFAVKFYTRE GNFDLVGNNF PVFFVRDGLK FPDMVHALKP NPKSHIQENW RILDFFSHHP 

       190        200        210        220        230        240 
ESLHMFSFLF DDVGIPQDYR HMDGFGVNTY TLINKAGKAL YVKFHWKTTS GEKSLLDDEA 

       250        260        270        280        290        300 
IRVGGSNHSH ATQDLYDSIA AGNYPEWKLY IQTLDPENED RLDFDPLDVT KTWPEDVLPL 

       310        320        330        340        350        360 
QPVGRMVLNK NIDNFFAENE QLAFCPAIIV PGVYYSDDKL LQTRVFSYAD TQRHRLGPNY 

       370        380        390        400        410        420 
LQLPANAPKC AHHNNHHDGF MNFMHRDEEV NYFPSRYDPV RHAEKVPVPP RILGGKREKC 

       430        440        450        460        470        480 
MIEKENNFKQ PGERYRSWPS DRQERFVRRW VDALSDPRVT HEIRSIWISY WSQADRSLGQ 

       490 
KIASHLNLKP SI 

« Hide

References

[1]"Isolation and characterization of a pea catalase cDNA."
Isin S.H., Allen R.D.
Plant Mol. Biol. 17:1263-1265(1991) [PubMed: 1932700] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. D&PL 415.
[2]Su H., Hardy K.A., Hermsmeier D., Baum T.J.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. Corsoy 79.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z12021 Genomic DNA. Translation: CAA78056.1.
AF035252 mRNA. Translation: AAB88169.1.
AF035253 mRNA. Translation: AAB88170.1.
PIRCSSY. S20999.
UniGeneGma.28718

3D structure databases

SMRP29756. Positions 17-490.
ModBaseSearch...

Protein family/group databases

PeroxiBase6260. GmKat01.

Enzyme and pathway databases

BRENDA1.11.1.6. 299.

Gene expression databases

GenevestigatorP29756.

Family and domain databases

InterProIPR002226. Catalase.
IPR020835. Catalase-like_haem-dep.
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.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATA1_SOYBN
AccessionPrimary (citable) accession number: P29756
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: February 9, 2010
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant 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