P0ABR9 · MHPB_ECOLI
- Protein2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase
- GenemhpB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids314 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
Catalytic activity
- 3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-dienedioate + H+
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
26 μM | 2,3-dihydroxyphenylpropionic acid | 8 | 20 | |||
36 μM | 2,3-dihydroxycinnamic acid | 8 | 20 | |||
37 μM | methyl-2,3-dihydroxyphenylpropionate | 8 | 20 | |||
90 μM | 3-methylcatechol | 8 | 20 | |||
94 μM | 3-phenethylcatechol | 8 | 20 | |||
154 μM | 3-propylcatechol | 8 | 20 | |||
185 μM | 3-ethylcatechol | 8 | 20 | |||
300 μM | 2,3-dihydroxyphenoxyacetic acid | 8 | 20 | |||
700 μM | catechol | 8 | 20 |
Pathway
Aromatic compound metabolism; 3-phenylpropanoate degradation.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 115 | Proton donor | ||||
Sequence: H | ||||||
Active site | 179 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3-carboxyethylcatechol 2,3-dioxygenase activity | |
Molecular Function | ferrous iron binding | |
Biological Process | 3-(3-hydroxy)phenylpropionate catabolic process | |
Biological Process | 3-phenylpropionate catabolic process | |
Biological Process | phenylpropanoid catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended name2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0ABR9
- Secondary accessions
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 114 | Complete loss of extradiol cleavage activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 114 | Low level of catalytic activity, 600-fold lower than the wild-type enzyme. More than 8000-fold decrease in affinity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 115 | Complete loss of extradiol cleavage activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 115 | Complete loss of activity. | ||||
Sequence: H → Q | ||||||
Mutagenesis | 115 | Complete loss of activity. | ||||
Sequence: H → Y | ||||||
Mutagenesis | 179 | Complete loss of activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 179 | Complete loss of activity. | ||||
Sequence: H → Q | ||||||
Mutagenesis | 179 | Complete loss of activity. | ||||
Sequence: H → Y | ||||||
Mutagenesis | 181 | More than 2-fold decrease in catalytic activity and 100-fold decrease in affinity. | ||||
Sequence: P → A | ||||||
Mutagenesis | 181 | More than 60-fold decrease in catalytic activity and affinity. | ||||
Sequence: P → H |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000085103 | 1-314 | 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase | |||
Sequence: MHAYLHCLSHSPLVGYVDPAQEVLDEVNGVIASARERIAAFSPELVVLFAPDHYNGFFYDVMPPFCLGVGATAIGDFGSAAGELPVPVELAEACAHAVMKSGIDLAVSYCMQVDHGFAQPLEFLLGGLDKVPVLPVFINGVATPLPGFQRTRMLGEAIGRFTSTLNKRVLFLGSGGLSHQPPVPELAKADAHMRDRLLGSGKDLPASERELRQQRVISAAEKFVEDQRTLHPLNPIWDNQFMTLLEQGRIQELDAVSNEELSAIAGKSTHEIKTWVAAFAAISAFGNWRSEGRYYRPIPEWIAGFGSLSARTEN |
Proteomic databases
Structure
Sequence
- Sequence statusComplete
- Length314
- Mass (Da)34,196
- Last updated2005-11-08 v1
- ChecksumE1D5A8574E5DFE05
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 138-140 | in Ref. 1; BAA13053 | ||||
Sequence: ING → NKA | ||||||
Sequence conflict | 152 | in Ref. 1; BAA13053 | ||||
Sequence: R → H | ||||||
Sequence conflict | 157 | in Ref. 1; BAA13053 | ||||
Sequence: A → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D86239 EMBL· GenBank· DDBJ | BAA13053.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y09555 EMBL· GenBank· DDBJ | CAA70748.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U73857 EMBL· GenBank· DDBJ | AAB18072.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC73451.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76130.1 EMBL· GenBank· DDBJ | Genomic DNA |