Reviewed,
UniProtKB/Swiss-Prot Q9KH19 (MHPB_RHOSO)
Last modified
January 19, 2010.
Version 30.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase EC=1.13.11.16 | ||||
| Gene names |
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| Organism | Rhodococcus sp. | ||||
| Taxonomic identifier | 1831 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus |
Protein attributes
| Sequence length | 314 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively. Also catalyzes the cleavage of catechol. HAMAP MF_01653 |
| Catalytic activity | 3-(2,3-dihydroxyphenyl)propanoate + O2 = 2-hydroxy-6-oxonona-2,4-diene-1,9-dioate. Ref.1 2,3-dihydroxicinnamic acid + O2 = 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate. Ref.1 |
| Cofactor | Fe2+ ion By similarity. HAMAP MF_01653 |
| Pathway | Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP MF_01653 |
| Subunit structure | Homotetramer By similarity. HAMAP MF_01653 |
| Sequence similarities | Belongs to the ligB/mhpB extradiol dioxygenase family. |
| Biophysicochemical properties | Kinetic parameters: KM=30 µM for 3-(2,3-dihydroxyphenyl) propionic acid (at pH 8.1 and 8 degrees Celsius) HAMAP MF_01653 KM=47 µM for catechol (at pH 8.1 and 8 degrees Celsius) KM=62 µM for 3-methylcatechol (at pH 8.1 and 8 degrees Celsius) |
Ontologies
| Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism |
| Ligand | Iron |
| Molecular function | Dioxygenase Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | aromatic compound catabolic process Inferred from electronic annotation. Source: HAMAP oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 2,3-dihydroxy-phenylpropionate 1,2-dioxygenase activity Inferred from electronic annotation. Source: HAMAP 3-carboxyethylcatechol 2,3-dioxygenase activityInferred from electronic annotation. Source: EC ferrous iron 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 – 314 | 314 | 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase HAMAP MF_01653 | PRO_0000337667 | |||||
Sites | |||||||||
| Active site | 115 | 1 | Proton donor By similarity | ||||||
| Active site | 179 | 1 | Proton acceptor By similarity | ||||||
Sequences
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References
| [1] | "Molecular characterisation of a Rhodococcus ohp operon." Powell J.A., Archer J.A. Antonie Van Leeuwenhoek 74:175-188(1998) [PubMed: 10068799] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. Strain: ATCC 19070 / V49. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF274045 Genomic DNA. Translation: AAF81826.1. |
3D structure databases | |
| SMR | Q9KH19. Positions 4-307. |
| ModBase | Search... |
Family and domain databases | |
| HAMAP | MF_01653. MhpB. [Tree] |
| InterPro | IPR004183. Xdiol_dOase_3B. [Graphical view] |
| Pfam | PF02900. LigB. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MHPB_RHOSO | ||||||||
| Accession | Primary (citable) accession number: Q9KH19 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


