Q5MZ99 (KATG_SYNP6) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 53.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Catalase-peroxidase Short name=CP EC=1.11.1.21 Alternative name(s): Peroxidase/catalase | ||||
| Gene names |
| ||||
| Organism | Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 269084 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Chroococcales › Synechococcus |
Protein attributes
| Sequence length | 720 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 | |
| Subcellular location | |
| 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 process | Hydrogen peroxide |
| Cellular component | Cytoplasm |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase Peroxidase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | catalase activity Inferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 720 | 720 | Catalase-peroxidase HAMAP MF_01961 | PRO_0000354941 | |||||||
Sites | |||||||||||
| Active site | 95 | 1 | Proton acceptor By similarity | ||||||||
| Metal binding | 263 | 1 | Iron (heme axial ligand) By similarity | ||||||||
| Site | 91 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 94 ↔ 222 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-248) By similarity | |||||||||
| Cross-link | 222 ↔ 248 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-94) By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 5 | 1 | Q → R in AAF05841. Ref.1 | ||||||||
| Sequence conflict | 358 | 1 | V → I in AAF05841. Ref.1 | ||||||||
Sequences
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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. |
| RefSeq | YP_173141.1. NC_006576.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ITK based on UniProtKB O59651. |
| ProteinModelPortal | Q5MZ99. |
| SMR | Q5MZ99. Positions 21-720. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q5MZ99. |
Protein family/group databases | |
| PeroxiBase | 3578. SeCP01_PCC6301. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3199022. |
| GenomeReviews | Gene locus syc2431_d in contig AP008231_GR. |
| KEGG | syc:syc2431_d. |
| PATRIC | 32491070. VBISynElo117686_2765. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0376. |
| HOGENOM | HBG285610. |
| OMA | IRLTWHA. |
| PhylomeDB | Q5MZ99. |
| ProtClustDB | PRK15061. |
Enzyme and pathway databases | |
| BioCyc | SELO269084:SYC2431_D-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01961. Catal-peroxid. [Tree] |
| InterPro | IPR000763. Catalase_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. [Graphical view] |
| KO | K03782. |
| Pfam | PF00141. peroxidase. 2 hits. [Graphical view] |
| PRINTS | PR00460. BPEROXIDASE. PR00458. PEROXIDASE. |
| SUPFAM | SSF48113. Peroxidase_super. 2 hits. |
| TIGRFAMs | TIGR00198. Cat_per_HPI. 1 hit. |
| PROSITE | PS00435. PEROXIDASE_1. False negative. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KATG_SYNP6 | ||||||||
| Accession | Primary (citable) accession number: Q5MZ99 Secondary accession number(s): Q9R6S9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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