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- * Cytochrome b5 family, heme-binding domain signature *
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-
- Cytochrome b5 is a membrane-bound hemoprotein which acts as an electron
- carrier for several membrane-bound oxygenases [1]. There are two homologous
- forms of b5, one found in microsomes and one found in the outer membrane of
- mitochondria. Two conserved histidine residues serve as axial ligands for the
- heme group. The structure of a number of oxidoreductases consists of the
- juxtaposition of a heme-binding domain homologous to that of b5 and either a
- flavodehydrogenase or a molybdopterin domain. These enzymes are:
-
- - Lactate dehydrogenase (EC 1.1.2.3) [2], an enzyme that consists of a
- flavodehydrogenase domain and a heme-binding domain called cytochrome b2.
- - Nitrate reductase (EC 1.6.6.1), a key enzyme involved in the first step of
- nitrate assimilation in plants, fungi and bacteria [3,4]. Consists of a
- molybdopterin domain, a heme-binding domain called cytochrome b557, as well
- as a cytochrome reductase domain.
- - Sulfite oxidase (EC 1.8.3.1) [5], which catalyzes the terminal reaction in
- the oxidative degradation of sulfur-containing amino acids. Also consists
- of a molybdopterin domain and a heme-binding domain.
-
- This family of proteins also includes TU-36B, a Drosophila muscle protein of
- unknown function [6].
-
- We used a segment which includes the first of the two histidine heme ligands,
- as a signature pattern for the heme-binding domain of cytochrome b5 family.
-
- -Consensus pattern: [FY]-[LIV]-x(2)-H-P-G-G
- [H is a heme axial ligand]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: Yeast acyl-CoA desaturase 1 (OLE1).
-
- -Expert(s) to contact by email: Rouze P.
- pirou@gengenp.rug.ac.be
-
- -Last update: June 1994 / Pattern and text revised.
-
- [ 1] Ozols J.
- Biochim. Biophys. Acta 997:121-130(1989).
- [ 2] Guiard B.
- EMBO J. 4:3265-3272(1985).
- [ 3] Calza R., Huttner E., Vincentz M., Rouze P., Galangau F., Vaucheret H.,
- Cherel I., Meyer C., Kronenberger J., Caboche M.
- Mol. Gen. Genet. 209:552-562(1987).
- [ 4] Crawford N.M., Smith M., Bellissimo D., Davis R.W.
- Proc. Natl. Acad. Sci. U.S.A. 85:5006-5010(1988).
- [ 5] Guiard B., Lederer F.
- Eur. J. Biochem. 100:441-453(1979).
- [ 6] Levin R.J., Boychuk P.L., Croniger C.M., Kazzaz J.A., Rozek C.E.
- Nucleic Acids Res. 17:6349-6367(1989).
-