The major biotinyl protein from Pisum sativum seeds covalently binds biotin at a novel site

Plant Mol Biol. 1994 Oct;26(1):265-73. doi: 10.1007/BF00039537.


Seeds of Pisum sativum contain a biotinyl polypeptide called SBP65 that behaves as a putative sink for the free vitamin, representing more than 90% of the total protein-bound biotin in mature seeds. A cDNA encoding SBP65 was cloned and sequenced. The deduced primary structure of the protein was confirmed by protein sequencing. Peptide sequencing also indicated binding of the biotin to lysine 103. The biotinylation domain of SBP65 differs markedly from that of presently known biotin enzymes. Molecular analysis of the protein sequence reveals an extremely hydrophilic protein containing several repeated motifs. These properties, as well as the temporal and spatial patterns of expression of this protein, suggest that SBP65 belongs to the LEA (late embryogenesis-abundant) group of proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • Biotin / metabolism*
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Gene Library
  • Genes, Plant / genetics*
  • Molecular Sequence Data
  • Molecular Weight
  • Peas / genetics*
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • Seeds / genetics*
  • Sequence Analysis
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid


  • DNA, Complementary
  • Plant Proteins
  • SBP65 protein, Pisum sativum
  • Biotin

Associated data

  • GENBANK/X75880