Reviewed,
UniProtKB/Swiss-Prot A1K9V0 (KATG_AZOSB)
Last modified
November 3, 2009.
Version 21.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Catalase-peroxidase Short name=CP EC=1.11.1.6 EC=1.11.1.7 Alternative name(s): Peroxidase/catalase | ||||
| Gene names |
| ||||
| Organism | Azoarcus sp. (strain BH72) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 62928 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Azoarcus |
Protein attributes
| Sequence length | 733 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity By similarity. |
| Catalytic activity | 2 H2O2 = O2 + 2 H2O. HAMAP MF_01961 Donor + H2O2 = oxidized donor + 2 H2O. HAMAP MF_01961 |
| Cofactor | Binds 1 heme B (iron-protoporphyrin IX) group per dimer By similarity. |
| Subunit structure | Homodimer or homotetramer By similarity. |
| Post-translational modification | The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. |
| Sequence similarities | Belongs to the peroxidase family. Peroxidase/catalase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hydrogen peroxide |
| Domain | Signal |
| 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 oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | catalase activity Inferred from electronic annotation. Source: HAMAP 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | Potential | ||||||||
| Chain | 24 – 733 | 710 | Catalase-peroxidase HAMAP MF_01961 | PRO_0000354722 | |||||||
Sites | |||||||||||
| Active site | 97 | 1 | Proton acceptor By similarity | ||||||||
| Metal binding | 265 | 1 | Iron (heme axial ligand) By similarity | ||||||||
| Site | 93 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 96 ↔ 224 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-250) By similarity | |||||||||
| Cross-link | 224 ↔ 250 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-96) By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. strain BH72." Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., Weidner S. Goesmann A.Nat. Biotechnol. 24:1385-1391(2006) [PubMed: 17057704] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AM406670 Genomic DNA. Translation: CAL95605.1. | |
| RefSeq | YP_934492.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A1K9V0. |
Genome annotation databases | |
| GeneID | 4608482. |
| GenomeReviews | Gene locus azo2989 in contig AM406670_GR. |
| KEGG | azo:azo2989. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | KTGEPRW. |
Family and domain databases | |
| HAMAP | MF_01961. [Tree] |
| InterPro | IPR000763. Catalase_proxase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view] |
| Pfam | PF00141. peroxidase. 2 hits. [Graphical view] |
| PRINTS | PR00460. BPEROXIDASE. PR00458. PEROXIDASE. |
| TIGRFAMs | TIGR00198. cat_per_HPI. 1 hit. |
| PROSITE | PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KATG_AZOSB | ||||||||
| Accession | Primary (citable) accession number: A1K9V0 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


