DB code: M00138
| CATH domain | -.-.-.- : | |
|---|---|---|
| -.-.-.- : | ||
| 3.90.56.10 : Phenol Hydroxylase P2 Protein | ||
| -.-.-.- : | ||
| -.-.-.- : | ||
| -.-.-.- : | ||
| E.C. | 1.14.13.7 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam |
|---|---|---|---|
| P19731 |
Phenol hydroxylase P2 protein
|
EC
1.14.13.7
Phenol 2-monooxygenase P2 component |
PF02406
(MmoB_DmpM)
[Graphical View] |
| KEGG enzyme name |
|---|
|
phenol 2-monooxygenase
phenol hydroxylase phenol o-hydroxylase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P19731 | DMPM_PSEUF | Phenol + NADPH + O(2) = catechol + NADP(+) + H(2)O. | The multicomponent enzyme phenol hydroxylase is formed by P0, P1, P2, P3, P4 and P5 polypeptides. | FAD. Fe(2+). |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00361 | gamma-Hexachlorocyclohexane degradation | |
| MAP00622 | Toluene and xylene degradation | |
| MAP00626 | Naphthalene and anthracene degradation |
| Compound table | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | ||||||||||
| KEGG-id | C00016 | C00146 | C00005 | C00007 | C00090 | C00006 | C00001 | ||||||
| E.C. | |||||||||||||
| Compound | FAD | Phenol | NADPH | O2 | Catechol | NADP+ | H2O | ||||||
| Type | amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide | aromatic ring (only carbon atom) | amide group,amine group,nucleotide | others | aromatic ring (only carbon atom) | amide group,amine group,nucleotide | H2O | ||||||
| ChEBI |
16238 16238 |
15882 15882 |
16474 16474 |
15379 26689 27140 15379 26689 27140 |
18135 18135 |
18009 18009 |
15377 15377 |
||||||
| PubChem |
643975 643975 |
20488062 996 20488062 996 |
5884 5884 |
977 977 |
289 289 |
5886 5886 |
22247451 962 22247451 962 |
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| 1hqiA |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1hqiA |
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| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8145253 |
| Journal | J Mol Biol |
| Year | 1994 |
| Volume | 238 |
| Pages | 128-30 |
| Authors | Enroth C, Huang W, Waters S, Neujahr H, Lindqvist Y, Schneider G |
| Title | Crystallization and preliminary X-ray analysis of phenol hydroxylase from Trichosporon cutaneum. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | STRUCTURE BY NMR |
| Medline ID | 97164903 |
| PubMed ID | 9012665 |
| Journal | Biochemistry |
| Year | 1997 |
| Volume | 36 |
| Pages | 495-504 |
| Authors | Qian H, Edlund U, Powlowski J, Shingler V, Sethson I |
| Title | Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy. |
| Related PDB | 1hqi |
| Related UniProtKB | P19731 |
| Comments |
|---|
|
This enzyme is composed of six different chains, |
| Created | Updated |
|---|---|
| 2004-02-04 | 2009-02-26 |