Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

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EB_dh Ethylbenzene dehydrogenase

SMART accession number:	SM00887
Description:	Eythylbenzene dehydrogenase is a heterotrimer of three subunits that catalyses the anaerobic degradation of hydrocarbons. The alpha subunit contains the catalytic centre as a Molybdenum cofactor-complex. This removes an electron-pair from the hydrocarbon and passes it along an electron transport system involving iron-sulphur complexes held in the beta subunit and a Haem b molecule contained in the gamma subunit. The electron-pair is then subsequently passed to an as yet unknown receiver. The enzyme is found in a variety of different bacteria.
Interpro abstract (IPR019020):	This entry represents a haem-binding domain found in cytochromes b558/566 (subunit A), c-551 and c-552, as well as in members of the type-II members of the microbial dimethyl sulphoxide (DMSO) reductase family. The DMSO reductase family is a large and rapidly expanding group of enzymes found in bacteria and archaea that share a common form of molybdenum cofactor known as bis(molybdopterin guanine dinucleotide)Mo [ (PUBMED:15311335) ]. In addition to the molybdopterin subunit, these enzymes also contain an iron-sulphur subunit. These include two distinct but very closely related periplasmic proteins of anaerobic respiration: selenate reductase and chlorate reductase [ (PUBMED:15866716) ]. Other proteins containing this subunit include dimethyl sulphide dehydrogenase and ethylbenzene dehydrogenase [ (PUBMED:11294876) (PUBMED:12067345) (PUBMED:16030201) ]. One member of the DMSO reductase family is eythylbenzene dehydrogenase, which is a heterotrimer of three subunits that catalyses the anaerobic degradation of hydrocarbons (alpha, beta and gamma subunits). This entry matches the gamma subunit, whose structure is known [ (PUBMED:16962969) ]. The alpha subunit contains the catalytic centre as a Molybdenum cofactor-complex. This removes an electron-pair from the hydrocarbon and passes it along an electron transport system involving iron-sulphur complexes held in the beta subunit and a Haem b molecule contained in the gamma subunit. The electron-pair is then subsequently passed to an as yet unknown receiver. The enzyme is found in a variety of different bacteria.
GO function:	heme binding (GO:0020037)
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 1002 EB_dh domains in 995 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing EB_dh domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with EB_dh domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing EB_dh domain in the selected taxonomic class.

• Cellular role (predicted cellular role)

• Cellular role: metabolism
  

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Kloer DP, Hagel C, Heider J, Schulz GE
  • Crystal structure of ethylbenzene dehydrogenase from Aromatoleumaromaticum.
  • Structure. 2006; 14: 1377-88
  • Display abstract

  • Anaerobic degradation of hydrocarbons was discovered a decade ago, andethylbenzene dehydrogenase was one of the first characterized enzymesinvolved. The structure of the soluble periplasmic 165 kDa enzyme wasestablished at 1.88 A resolution. It is a heterotrimer. The alpha subunitcontains the catalytic center with a molybdenum held by twomolybdopterin-guanine dinucleotides, one with an open pyran ring, and aniron-sulfur cluster with a histidine ligand. During catalysis, electronsproduced by substrate oxidation are transferred to a heme in the gammasubunit and then presumably to a separate cytochrome involved in nitraterespiration. The beta subunit contains four iron-sulfur clusters and isstructurally related to ferredoxins. The gamma subunit is the first knownprotein with a methionine and a lysine as axial heme ligands. Thecatalytic product was modeled into the active center, showing the reactiongeometry. A mechanism consistent with activity and inhibition data ofethylbenzene-related compounds is proposed.

• Structure (3D structures containing this domain)

• 3D Structures of EB_dh domains in PDB

  PDB code	Main view	Title
  2ivf		Ethylbenzene dehydrogenase from Aromatoleum aromaticum

• Links (links to other resources describing this domain)

• INTERPRO	IPR019020
  PFAM	EB_dh

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