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Q5MZ99 (KATG_SYNP6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Catalase-peroxidase

Short name=CP
EC=1.11.1.21
Alternative name(s):
Peroxidase/catalase
Gene names
Name:katG
Ordered Locus Names:syc2431_d
OrganismSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP]
Taxonomic identifier269084 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechococcus

Protein attributes

Sequence length720 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Ref.1 Ref.3

Catalytic activity

Donor + H2O2 = oxidized donor + 2 H2O. HAMAP MF_01961

2 H2O2 = O2 + 2 H2O. HAMAP MF_01961

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per dimer. Ref.1

Enzyme regulation

Inhibited by cyanide. Ref.1

Subunit structure

Homodimer. Ref.1 Ref.3

Subcellular location

Cytoplasmcytosol Ref.3.

Post-translational modification

The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. HAMAP MF_01961

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=4.3 mM for H2O2 for the catalase reaction Ref.3

pH dependence:

Optimum pH is 6.5-7.5 for both the catalase and the peroxidase reaction.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentCytoplasm
   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

   Cellular componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 720720Catalase-peroxidase HAMAP MF_01961
PRO_0000354941

Sites

Active site951Proton acceptor By similarity
Metal binding2631Iron (heme axial ligand) By similarity
Site911Transition state stabilizer By similarity

Amino acid modifications

Cross-link94 ↔ 222Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-248) By similarity
Cross-link222 ↔ 248Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-94) By similarity

Experimental info

Sequence conflict51Q → R in AAF05841. Ref.1
Sequence conflict3581V → I in AAF05841. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5MZ99 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 93A4C2E9990F1A2F

FASTA72080,078
        10         20         30         40         50         60 
MTATQGKCPV MHGGATTVNI STAEWWPKAL NLDILSQHDR KTNPMGPDFN YQEEVKKLDV 

        70         80         90        100        110        120 
AALKQDLQAL MTDSQDWWPA DWGHYGGLMI RLTWHAAGTY RIADGRGGAG TGNQRFAPLN 

       130        140        150        160        170        180 
SWPDNTNLDK ARRLLWPIKQ KYGNKLSWAD LIAYAGTIAY ESMGLKTFGF AFGREDIWHP 

       190        200        210        220        230        240 
EKDIYWGPEK EWVPPSTNPN SRYTGDRELE NPLAAVTMGL IYVNPEGVDG NPDPLKTAHD 

       250        260        270        280        290        300 
VRVTFARMAM NDEETVALTA GGHTVGKCHG NGNAALLGPE PEGADVEDQG LGWINKTQSG 

       310        320        330        340        350        360 
IGRNAVTSGL EGAWTPHPTQ WDNGYFRMLL NYDWELKKSP AGAWQWEPIN PREEDLPVDV 

       370        380        390        400        410        420 
EDPSIRRNLV MTDADMAMKM DPEYRKISER FYQDPAYFAD VFARAWFKLT HRDMGPKARY 

       430        440        450        460        470        480 
IGPDVPQEDL IWQDPIPAGN RNYDVQAVKD RIAASGLSIS ELVSTAWDSA RTYRNSDKRG 

       490        500        510        520        530        540 
GANGARIRLA PQKDWEGNEP DRLAKVLAVL EGIAAATGAS VADVIVLAGN VGVEQAARAA 

       550        560        570        580        590        600 
GVEIVLPFAP GRGDATAEQT DTESFAVLEP IHDGYRNWLK QDYAATPEEL LLDRTQLLGL 

       610        620        630        640        650        660 
TAPEMTVLIG GLRVLGTNHG GTKHGVFTDR EGVLTNDFFV NLTDMNYLWK PAGKNLYEIC 

       670        680        690        700        710        720 
DRKTNQVKWT ATRVDLVFGS NSILRAYSEL YAQDDNKEKF VRDFVAAWTK VMNADRFDLD 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence analysis, overexpression in Escherichia coli and kinetic characterization of Anacystis nidulans catalase-peroxidase."
Engleder M., Regelsberger G., Jakopitsch C., Furtmueller P.G., Rueker F., Peschek G.A., Obinger C.
Biochimie 82:211-219(2000) [PubMed: 10863004] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, HEME-BINDING, ENZYME REGULATION.
[2]"Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
Photosyn. Res. 93:55-67(2007) [PubMed: 17211581] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.
[3]"Purification and characterization of a homodimeric catalase-peroxidase from the cyanobacterium Anacystis nidulans."
Obinger C., Regelsberger G., Strasser G., Burner U., Peschek G.A.
Biochem. Biophys. Res. Commun. 235:545-552(1997) [PubMed: 9207193] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF197161 Genomic DNA. Translation: AAF05841.1.
AP008231 Genomic DNA. Translation: BAD80621.1.
RefSeqYP_173141.1. NC_006576.1.

3D structure databases

HSSPHSSP built from PDB template 1ITK based on UniProtKB O59651.
ProteinModelPortalQ5MZ99.
SMRQ5MZ99. Positions 21-720.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5MZ99.

Protein family/group databases

PeroxiBase3578. SeCP01_PCC6301.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3199022.
GenomeReviewsGene locus syc2431_d in contig AP008231_GR.
KEGGsyc:syc2431_d.
PATRIC32491070. VBISynElo117686_2765.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0376.
HOGENOMHBG285610.
OMAIRLTWHA.
PhylomeDBQ5MZ99.
ProtClustDBPRK15061.

Enzyme and pathway databases

BioCycSELO269084:SYC2431_D-MONOMER.

Family and domain databases

HAMAPMF_01961. Catal-peroxid.
[Tree]
InterProIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
KOK03782.
PfamPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 2 hits.
TIGRFAMsTIGR00198. Cat_per_HPI. 1 hit.
PROSITEPS00435. PEROXIDASE_1. False negative.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG_SYNP6
AccessionPrimary (citable) accession number: Q5MZ99
Secondary accession number(s): Q9R6S9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: February 1, 2005
Last modified: January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families