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	PROSITE documentation PDOC00642 [for PROSITE entry PS00814]

Adrenodoxin family, iron-sulfur binding region signature

Ferredoxins [1] are a group of iron-sulfur proteins which mediate electron transfer in a wide variety of metabolic reactions. Ferredoxins can be divided into several subgroups depending upon the physiological nature of the iron sulfur cluster(s) and according to sequence similarities. One family of ferredoxins groups together the following proteins that all bind a single 2Fe-2S iron-sulfur cluster:

• Adrenodoxin (ADX) (adrenal ferredoxin), a vertebrate mitochondrial protein which transfers electrons from adrenodoxin reductase to cytochrome P450scc, which is involved in cholesterol side chain cleavage.
• Putidaredoxin (PTX), a Pseudomonas putida protein which transfers electrons from putidaredoxin reductase to cytochrome P450-cam, which is involved in the oxidation of camphor.
• Terpredoxin [2], a Pseudomonas protein which transfers electrons from terpredoxin reductase to cytochrome P450-terp, which is involved in the oxidation of α-terpineol.
• Rhodocoxin [3], a Rhodococcus protein which transfers electrons from rhodocoxin reductase to cytochrome CYP116 (thcB), which is involved in the degradation of thiocarbamate herbicides.
• Escherichia coli ferredoxin (gene fdx) [4] whose exact function is not yet known.
• Rhodobacter capsulatus ferredoxin VI [5], which may transfer electrons to a yet uncharacterized oxygenase.
• Caulobacter crescentus ferredoxin (gene fdxB) [6].

In these proteins, four cysteine residues bind the iron-sulfur cluster. Three of these cysteines are clustered together in the same region of the protein. Our signature pattern spans that iron-sulfur binding region.

Last update:

May 2004 / Text revised.

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

ADX, PS00814; Adrenodoxin family, iron-sulfur binding region signature  (PATTERN)

• Consensus pattern:
  C-x(2)-[STAQ]-x-[STAMV]-C-[STA]-T-C-[HR]
  The 3 C's are 2Fe-2S ligands
• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 43
  • detected by PS00814: 38 (true positives)
  • undetected by PS00814: 5 (5 false negatives and 0 'partial')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS00814:
  NONE.
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00814
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00814
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS00814
• View ligand binding statistics of PS00814
• Matching PDB structures: 1AYF 1B9R 1CJE 1E6E ... [ALL]

1	Authors	Meyer J.
	Source	Trends Ecol. Evol. 3:222-226(1988).

2	Authors	Peterson J.A., Lu J.-Y., Geisselsoder J., Graham-Lorence S., Carmona C., Witney F., Lorence M.C.
	Title	Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon.
	Source	J. Biol. Chem. 267:14193-14203(1992).
	PubMed ID	1629218

3	Authors	Nagy I., Schoofs G., Compernolle F., Proost P., Vanderleyden J., de Mot R.
	Title	Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase.
	Source	J. Bacteriol. 177:676-687(1995).
	PubMed ID	7836301

4	Authors	Ta D.T., Vickery L.E.
	Title	Cloning, sequencing, and overexpression of a [2Fe-2S] ferredoxin gene from Escherichia coli.
	Source	J. Biol. Chem. 267:11120-11125(1992).
	PubMed ID	1317854

5	Authors	Naud I., Vincon M., Garin J., Gaillard J., Forest E., Jouanneau Y.
	Title	Purification of a sixth ferredoxin from Rhodobacter capsulatus. Primary structure and biochemical properties.
	Source	Eur. J. Biochem. 222:933-939(1994).
	PubMed ID	8026503

6	Authors	Wang S.P., Chen Y.P., Ely B.
	Title	A ferredoxin, designated FdxP, stimulates p-hydroxybenzoate hydroxylase activity in Caulobacter crescentus.
	Source	J. Bacteriol. 177:2908-2911(1995).
	PubMed ID	7751304

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