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- *************************************************
- * High potential iron-sulfur proteins signature *
- *************************************************
-
- High potential iron-sulfur proteins (HiPIP) [1] are a specific class of high-
- redox potential 4Fe-4S ferredoxins that functions in anaerobic electron
- transport and which occurs in photosynthetic bacteria and in Paracoccus
- denitrificans.
-
- The HiPIPs are small proteins which show significant variation in their
- sequences, their sizes (from 63 to 85 amino acids), and in their oxidation-
- reduction potentials. As shown in the following schematic representation the
- iron-sulfur cluster is bound by four conserved cysteine residues.
-
- [ 4Fe-4S cluster]
- | | | |
- xxxxxxxxxxxxxxxxxxxCxCxxxxxxxCxxxxxCxxxx
- ********
-
- 'C': conserved cysteine involved in the binding of the iron-sulfur cluster.
- '*': position of the pattern.
-
- -Consensus pattern: C-x(7,9)-[LIVM]-x(3)-G-[YW]-C-x(2)-[YW]
- [The two C's are 4Fe-4S ligands]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
- -Last update: December 1991 / First entry.
-
- [ 1] Breiter D.R., Meyer T.E., Rayment I., Holden H.M.
- J. Biol. Chem. 266:18660-18667(1991).
-