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| PROSITE documentation PDOC00170 |
Cytochrome b5 family, heme-binding domain signature and profile
Description
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 1.7.1.-), a key enzyme involved in the first step of
nitrate assimilation in plants, fungi and bacteria [3,4]. Consists of a
molybdopterin domain (see <PDOC00484>), 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.
- Yeast acyl-CoA desaturase 1 (EC 1.14.19.1) (gene OLE1). This enzyme
contains a C-termainal heme-binding domain.
This family of proteins also includes:
- TU-36B, a Drosophila muscle protein of unknown function [6].
- Fission yeast hypothetical protein SpAC1F12.10c.
- Yeast hypothetical protein YMR073c.
- Yeast hypothetical protein YMR272c.
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.
Rouze P.
December 2004 / Pattern and text revised.
Technical section
PROSITE methods (with tools and information) covered by this documentation:
| CYTOCHROME_B5_2, PS50255; Cytochrome b5 family, heme-binding domain profile (MATRIX) |
| Sequences known to belong to this class detected by the profile: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
|
|
|
| Matching PDB structures:
1AQA 1AW3 1AWP 1AXX ... [ALL] |
| CYTOCHROME_B5_1, PS00191; Cytochrome b5 family, heme-binding domain signature (PATTERN) |
| Consensus pattern: |
[FY]-[LIVMK]-{I}-{Q}-H-P-[GA]-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: |
7. |
|
|
|
| Matching PDB structures:
1AQA 1AW3 1AWP 1AXX ... [ALL] |
References
| 1 |
Authors |
Ozols J. |
| Title |
Structure of cytochrome b5 and its topology in the microsomal membrane. |
| Source |
Biochim. Biophys. Acta 997:121-130(1989). |
| PubMed ID |
2752049 |
| 2 |
Authors |
Guiard B. |
| Title |
Structure, expression and regulation of a nuclear gene encoding a mitochondrial protein: the yeast L(+)-lactate cytochrome c oxidoreductase (cytochrome b2). |
| Source |
EMBO J. 4:3265-3272(1985). |
| PubMed ID |
3004948 |
| 3 |
Authors |
Calza R., Huttner E., Vincentz M., Rouze P., Galangau F., Vaucheret H., Cherel I., Meyer C., Kronenberger J., Caboche M. |
| Source |
Mol. Gen. Genet. 209:552-562(1987). |
| 4 |
Authors |
Crawford N.M., Smith M., Bellissimo D., Davis R.W. |
| Title |
Sequence and nitrate regulation of the Arabidopsis thaliana mRNA encoding nitrate reductase, a metalloflavoprotein with three functional domains. |
| Source |
Proc. Natl. Acad. Sci. U.S.A. 85:5006-5010(1988). |
| PubMed ID |
3393528 |
| 5 |
Authors |
Guiard B., Lederer F. |
| Title |
Amino acid sequence of the 'b5-like' heme-binding domain from chicken sulfite oxidase. |
| Source |
Eur. J. Biochem. 100:441-453(1979). |
| PubMed ID |
510290 |
| 6 |
Authors |
Levin R.J., Boychuk P.L., Croniger C.M., Kazzaz J.A., Rozek C.E. |
| Title |
Structure and expression of a muscle specific gene which is adjacent to the Drosophila myosin heavy-chain gene and can encode a cytochrome b related protein. |
| Source |
Nucleic Acids Res. 17:6349-6367(1989). |
| PubMed ID |
2549511 |
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