DB code: D00446
| CATH domain | 3.10.180.10 : 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1 | |
|---|---|---|
| 3.10.180.10 : 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1 | Catalytic domain | |
| E.C. | 1.13.11.2 | |
| CSA | 1mpy | |
| M-CSA | 1mpy | |
| MACiE | M0034 | |
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.10.180.10 : 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1 | D00447 D00448 S00540 S00185 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P06622 |
Metapyrocatechase
|
MPC
EC 1.13.11.2 CatO2ase Catechol 2,3-dioxygenase |
NP_542866.1
(Protein)
NC_003350.1 (DNA/RNA sequence) |
PF00903
(Glyoxalase)
[Graphical View] |
| KEGG enzyme name |
|---|
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catechol 2,3-dioxygenase
2,3-pyrocatechase catechol 2,3-oxygenase catechol oxygenase metapyrocatechase pyrocatechol 2,3-dioxygenase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P06622 | XYLE1_PSEPU | Catechol + O(2) = 2-hydroxymuconate semialdehyde. | Homotetramer. | Fe(2+) ion. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00362 | Benzoate degradation via hydroxylation | |
| MAP00622 | Toluene and xylene degradation | |
| MAP00627 | 1,4-Dichlorobenzene degradation | |
| MAP00629 | Carbazole degradation | |
| MAP00643 | Styrene degradation |
| Compound table | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||
| KEGG-id | C00023 | C00090 | C00007 | C00682 | ||||||
| E.C. | ||||||||||
| Compound | Iron | Catechol | O2 | 2-Hydroxymuconate semialdehyde | ||||||
| Type | heavy metal | aromatic ring (only carbon atom) | others | carbohydrate,carboxyl group | ||||||
| ChEBI |
18248 82664 18248 82664 |
18135 18135 |
15379 26689 27140 15379 26689 27140 |
67110 67110 |
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| PubChem |
23925 23925 |
289 289 |
977 977 |
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| 1mpyA01 |
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Unbound | Unbound | Unbound | Unbound | |
| 1mpyB01 |
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Unbound | Unbound | Unbound | Unbound | |
| 1mpyC01 |
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Unbound | Unbound | Unbound | Unbound | |
| 1mpyD01 |
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Unbound | Unbound | Unbound | Unbound | |
| 1mpyA02 |
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Bound:FE2 | Unbound | Unbound | Unbound | |
| 1mpyB02 |
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Bound:FE2 | Unbound | Unbound | Unbound | |
| 1mpyC02 |
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Bound:FE2 | Unbound | Unbound | Unbound | |
| 1mpyD02 |
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Bound:FE2 | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P06622 & literature [14] | ||
| Active-site residues | ||||||||||
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| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1mpyA01 |
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| 1mpyB01 |
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| 1mpyC01 |
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| 1mpyD01 |
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| 1mpyA02 |
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HIS 199 | HIS 153;HIS 214;GLU 265(Iron binding) | |||
| 1mpyB02 |
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HIS 199 | HIS 153;HIS 214;GLU 265(Iron binding) | |||
| 1mpyC02 |
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HIS 199 | HIS 153;HIS 214;GLU 265(Iorn binding) | |||
| 1mpyD02 |
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HIS 199 | HIS 153;HIS 214;GLU 265(Iron binding) | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
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[10]
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Fig.7, p.6656-6657 | 4 |
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[11]
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[14]
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Fig.1, p.32 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6245930 |
| Journal | FEBS Lett |
| Year | 1980 |
| Volume | 112 |
| Pages | 83-5 |
| Authors | Tatsuno Y, Saeki Y, Nozaki M, Otsuka S, Maeda Y |
| Title | Mossbauer spectra of metapyrocatechase. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6773944 |
| Journal | J Biol Chem |
| Year | 1980 |
| Volume | 255 |
| Pages | 8465-71 |
| Authors | Saeki Y, Nozaki M, Senoh S |
| Title | Cleavage of pyrogallol by non-heme iron-containing dioxygenases. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2997190 |
| Journal | J Biol Chem |
| Year | 1985 |
| Volume | 260 |
| Pages | 14035-44 |
| Authors | Arciero DM, Orville AM, Lipscomb JD |
| Title |
17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3015028 |
| Journal | Arch Biochem Biophys |
| Year | 1986 |
| Volume | 248 |
| Pages | 130-7 |
| Authors | Pascal RA Jr, Huang DS |
| Title | Reactions of 3-ethylcatechol and 3-(methylthio)catechol with catechol dioxygenases. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3365096 |
| Journal | Arch Microbiol |
| Year | 1988 |
| Volume | 149 |
| Pages | 188-97 |
| Authors | Engesser KH, Cain RB, Knackmuss HJ |
| Title | Bacterial metabolism of side chain fluorinated aromatics: cometabolism of 3-trifluoromethyl(TFM)-benzoate by Pseudomonas putida (arvilla) mt-2 and Rhodococcus rubropertinctus N657. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8075079 |
| Journal | Biochemistry |
| Year | 1994 |
| Volume | 33 |
| Pages | 10777-84 |
| Authors | Bertini I, Briganti F, Mangani S, Nolting HF, Scozzafava A |
| Title | X-ray absorption studies on catechol 2,3-dioxygenase from Pseudomonas putida mt2. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8163017 |
| Journal | FEBS Lett |
| Year | 1994 |
| Volume | 343 |
| Pages | 56-60 |
| Authors | Bertini I, Briganti F, Scozzafava A |
| Title | Aliphatic and aromatic inhibitors binding to the active site of catechol 2,3-dioxygenase from Pseudomonas putida mt-2. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8180697 |
| Journal | Microbiology |
| Year | 1994 |
| Volume | 140 |
| Pages | 321-30 |
| Authors | Candidus S, van Pee KH, Lingens F |
| Title |
The catechol 2,3-dioxygenase gene of Rhodococcus rhodochrous CTM: nucleotide sequence, |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7710322 |
| Journal | Arch Microbiol |
| Year | 1995 |
| Volume | 163 |
| Pages | 65-9 |
| Authors | Winkler J, Eltis LD, Dwyer DF, Rohde M |
| Title | Tetrameric structure and cellular location of catechol 2,3-dioxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7756296 |
| Journal | Biochemistry |
| Year | 1995 |
| Volume | 34 |
| Pages | 6649-59 |
| Authors | Shu L, Chiou YM, Orville AM, Miller MA, Lipscomb JD, Que L Jr |
| Title |
X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9056848 |
| Journal | Biochem Soc Trans |
| Year | 1997 |
| Volume | 25 |
| Pages | 81-5 |
| Authors | Bugg TD, Sanvoisin J, Spence EL |
| Title | Exploring the catalytic mechanism of the extradiol catechol dioxygenases. |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9276689 |
| Journal | J Biochem (Tokyo) |
| Year | 1997 |
| Volume | 122 |
| Pages | 201-4 |
| Authors | Kita A, Kita S, Inaka K, Ishida T, Horiike K, Nozaki M, Miki K |
| Title | Crystallization and preliminary X-ray diffraction studies of expressed Pseudomonas putida catechol 2,3-dioxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9545294 |
| Journal | J Biol Chem |
| Year | 1998 |
| Volume | 273 |
| Pages | 9622-9 |
| Authors | Hugo N, Armengaud J, Gaillard J, Timmis KN, Jouanneau Y |
| Title | A novel -2Fe-2S- ferredoxin from Pseudomonas putida mt2 promotes the reductive reactivation of catechol 2,3-dioxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [14] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) |
| Medline ID | 99148110 |
| PubMed ID | 10368270 |
| Journal | Structure Fold Des |
| Year | 1999 |
| Volume | 7 |
| Pages | 25-34 |
| Authors | Kita A, Kita S, Fujisawa I, Inaka K, Ishida T, Horiike K, Nozaki M, Miki K |
| Title | An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Ppseudomonas putida mt-2. |
| Related PDB | 1mpy |
| Related UniProtKB | P06622 |
| [15] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11565853 |
| Journal | J Biomol Struct Dyn |
| Year | 2001 |
| Volume | 19 |
| Pages | 75-83 |
| Authors | Dai L, Ji C, Gao D, Wang J, Jiang T, Bi A, Sheng X, Mao Y |
| Title | Modeling and analysis of the structure of the thermostable catechol 2,3-dioxygenase from Bacillus Stearothermophilus. |
| Related PDB | |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12519074 |
| Journal | Biochem J |
| Year | 2003 |
| Volume | 371 |
| Pages | 557-64 |
| Authors | Okuta A, Ohnishi K, Yagame S, Harayama S |
| Title | Intersubunit interaction and catalytic activity of catechol 2,3-dioxygenases. |
| Related PDB | |
| Related UniProtKB | |
| [17] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14769058 |
| Journal | J Biomol Struct Dyn |
| Year | 2004 |
| Volume | 21 |
| Pages | 657-62 |
| Authors | Zhang JH, Zhang LL, Zhou LX |
| Title | Thermostability of protein studied by molecular dynamics simulation. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
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| Created | Updated |
|---|---|
| 2004-10-28 | 2009-03-16 |