{PDOC00493} {PS00570; RING_HYDROXYL_ALPHA} {BEGIN} ********************************************************************* * 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 alpha-subunit of about 50 Kd, and a beta-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 alpha-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 alpha-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. -Consensus pattern: C-x-H-R-[GAR]-x(7,8)-[GEKVI]-[NERAQ]-x(4,5)-C-x-[FY]-H [The 2 C's and the 2 H's are 2Fe-2S ligands] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Expert(s) to contact by email: Harayama S.; sharayam@ddbj.nig.ac.jp -Last update: December 2004 / Pattern and text revised. [ 1] Neidle E.L., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S. "Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases." J. Bacteriol. 173:5385-5395(1991). PubMed=1885518 [ 2] Kauppi B., Lee K., Carredano E., Parales R.E., Gibson D.T., Eklund H., Ramaswamy S. "Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase." Structure 6:571-586(1998). PubMed=9634695 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}