| High potential iron-sulfur protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Structure of the oxidized high-potential iron-sulfur protein.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | HIPIP | ||||||||
| Pfam | PF01355 | ||||||||
| InterPro | IPR000170 | ||||||||
| PROSITE | PDOC00515 | ||||||||
| SCOP | 1hpi | ||||||||
| OPM family | 124 | ||||||||
| OPM protein | 1hpi | ||||||||
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High potential iron-sulfur proteins (HIPIP)[2] 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.
This article incorporates text from the public domain Pfam and InterPro IPR000170