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| PROSITE documentation PDOC00493 |
Bacterial ring hydroxylating dioxygenases alpha-subunit signature
Bacterial ring hydroxylating dioxygenases are multicomponent enzymatic complexes composed of a hydroxylase component and an electron transfer component. The hydroxylase component is itself composed of two subunits: an α-subunit of about 50 Kd, and a β-subunit of about 20 Kd. The electron transfer component is either composed of two subunits: a ferredoxin and a ferredoxin reductase or by a single bifunctional ferredoxin/reductase subunit.
The α-subunit of hydroxylase components are evolutionary related [1]. The currently known members of this family are listed below.
- Benzene 1,2-dioxygenase (EC 1.14.12.3) (gene bnzA) from Pseudomonas putida.
- phthalate 4,5-dioxygenase (EC 1.14.12.7) (gene pht3) from Pseudomonas.
- Benzoate 1,2-dioxygenase (EC 1.14.12.10) (gene benA) from Acinetobacter calcoaceticus.
- Naphthalene 1,2-dioxygenase (EC 1.14.12.12) (gene ndoC) from Pseudomonas.
- 3-chlorobenzoate-3,4-dioxygenase (EC 1.14.12-.-) (gene cbaA) from Alcaligenes.
- Biphenyl dioxygenase (EC 1.14.99.-) (gene bphA) from Pseudomonas.
- Toluate 1,2-dioxygenase (EC 1.14.12.-) (gene xylX) from Pseudomonas putida.
- Toluene 2,3-dioxygenase (EC 1.14.12.-) (gene todC1) from Pseudomonas putida.
The α-subunit of the hydroxylase components bind both a 2Fe-2S type iron-sulfur center and an iron atom. There is, in the N-terminal section of these proteins, a conserved region of 24 residues which contains two cysteines and two histidines which have been shown [2] to be involved in the binding of the iron-sulfur center. We have used this region has a signature pattern.
Expert(s) to contact by email: Last update:December 2004 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Neidle E.L. Hartnett C. Ornston L.N. Bairoch A. Rekik M. Harayama S. |
| Title | Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases. | |
| Source | J. Bacteriol. 173:5385-5395(1991). | |
| PubMed ID | 1885518 |
| 2 | Authors | Kauppi B. Lee K. Carredano E. Parales R.E. Gibson D.T. Eklund H. Ramaswamy S. |
| Title | Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase. | |
| Source | Structure 6:571-586(1998). | |
| PubMed ID | 9634695 |
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