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PROSITE documentation PDOC00400

Nickel-dependent hydrogenases large subunit signatures





Description

Hydrogenases are enzymes that catalyze the reversible activation of hydrogen and which occur widely in prokaryotes as well as in some eukaryotes. There are various types of hydrogenases, but all of them seem to contain at least one iron-sulfur cluster. They can be broadly divided into two groups: hydrogenases containing nickel and, in some cases, also selenium (the [NiFe] and [NiFeSe] hydrogenases) and those lacking nickel (the [Fe] hydrogenases).

The [NiFe] and [NiFeSe] hydrogenases are heterodimer that consist of a small subunit that contains a signal peptide and a large subunit. All the known large subunits seem to be evolutionary related [1]; they contain two Cys-x-x-Cys motifs; one at their N-terminal end; the other at their C-terminal end. These four cysteines are involved in the binding of nickel [2]. In the [NiFeSe] hydrogenases the first cysteine of the C-terminal motif is a selenocysteine which has experimentally been shown to be a nickel ligand [3]. We have developed two patterns which are centered on the Cys-x-x-Cys motifs.

Alcaligenes eutrophus possess a NAD-reducing cytoplasmic hydrogenase (hoxS) [4]; this enzyme is composed of four subunits. Two of these subunits (β and delta) are responsible for the hydrogenase reaction and are evolutionary related to the large and small subunits of membrane-bound hydrogenases.

The α subunit of coenzyme F420 hydrogenase (EC 1.12.98.1) (FRH) from archaebacterial methanogens also belongs to this family.

Last update:

January 2008 / Pattern updated.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

NI_HGENASE_L_1, PS00507; Nickel-dependent hydrogenases large subunit signature 1  (PATTERN)

NI_HGENASE_L_2, PS00508; Nickel-dependent hydrogenases large subunit signature 2  (PATTERN)


References

1AuthorsMenon N.K. Robbins J. Peck H.D. Jr. Chatelus C.Y. Choi E.-S. Przybyla A.E.
TitleCloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames.
SourceJ. Bacteriol. 172:1969-1977(1990).
PubMed ID2180913

2AuthorsVolbeda A. Charon M.-H. Piras C. Hatchikian E.C. Frey M. Fontecilla-Camps J.C.
TitleCrystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.
SourceNature 373:580-587(1995).
PubMed ID7854413
DOI10.1038/373580a0;

3AuthorsEidsness M.K. Scott R.A. Prickrill B. der Vartaninan D.V. LeGall J. Moura I. Moura J.J.G. Peck H.D. Jr.
Titlevidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases from Desulfovibrio baculatus.
SourceProc. Natl. Acad. Sci. U.S.A. 86:147-151(1989).
PubMed ID2521386

4AuthorsTran-Betcke A. Warnecke U. Boecker C. Zaborosch C. Friedrich B.
TitleCloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16.
SourceJ. Bacteriol. 172:2920-2929(1990).
PubMed ID2188945



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