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.

Expert(s) to contact by email:

Rouze P.

Last update:

December 2004 / Pattern and text revised.

Technical section

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

CYTOCHROME_B5_2, PS50255Cytochrome 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.
Domain architecture view of Swiss-Prot proteins matching PS50255
PS50255
• Retrieve an alignment of 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 tree view of all Swiss-Prot/TrEMBL entries matching PS50255
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS50255
Scan Swiss-Prot/TrEMBL entries against PS50255
view ligand binding statistics
Matching PDB structures: 1AQA 1AW3 1AWP 1AXX ... [ALL]
CYTOCHROME_B5_1, PS00191Cytochrome 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.
• Retrieve an alignment of 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 tree view of all Swiss-Prot/TrEMBL entries matching PS00191
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00191
Scan Swiss-Prot/TrEMBL entries against PS00191
view ligand binding statistics
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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