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B4SII9 · B4SII9_STRM5

Function

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Features

Showing features for binding site.

139050100150200250300350
TypeIDPosition(s)Description
Binding site54pyridoxal 5'-phosphate 1 (UniProtKB | ChEBI)
Binding site56pyridoxal 5'-phosphate 1 (UniProtKB | ChEBI)
Binding site84pyridoxal 5'-phosphate 2 (UniProtKB | ChEBI)
Binding site84pyridoxal 5'-phosphate 1 (UniProtKB | ChEBI)
Binding site84pyridoxal 5'-phosphate 3 (UniProtKB | ChEBI)
Binding site85pyridoxal 5'-phosphate 2 (UniProtKB | ChEBI)
Binding site85pyridoxal 5'-phosphate 1 (UniProtKB | ChEBI)
Binding site85pyridoxal 5'-phosphate 3 (UniProtKB | ChEBI)
Binding site108pyridoxal 5'-phosphate 2 (UniProtKB | ChEBI)
Binding site108pyridoxal 5'-phosphate 1 (UniProtKB | ChEBI)
Binding site108pyridoxal 5'-phosphate 3 (UniProtKB | ChEBI)
Binding site156pyridoxal 5'-phosphate 1 (UniProtKB | ChEBI)
Binding site156pyruvate 2 (UniProtKB | ChEBI)
Binding site156pyruvate 1 (UniProtKB | ChEBI)
Binding site203pyridoxal 5'-phosphate 3 (UniProtKB | ChEBI)
Binding site203pyridoxal 5'-phosphate 2 (UniProtKB | ChEBI)
Binding site203pyridoxal 5'-phosphate 1 (UniProtKB | ChEBI)
Binding site205pyridoxal 5'-phosphate 3 (UniProtKB | ChEBI)
Binding site205pyridoxal 5'-phosphate 1 (UniProtKB | ChEBI)
Binding site205pyridoxal 5'-phosphate 2 (UniProtKB | ChEBI)
Binding site206pyridoxal 5'-phosphate 1 (UniProtKB | ChEBI); covalent
Binding site206pyridoxal 5'-phosphate 3 (UniProtKB | ChEBI)
Binding site206pyruvate 2 (UniProtKB | ChEBI)
Binding site206pyruvate 1 (UniProtKB | ChEBI)
Binding site216pyridoxal 5'-phosphate 2 (UniProtKB | ChEBI)
Binding site335pyruvate 2 (UniProtKB | ChEBI)
Binding site350pyruvate 2 (UniProtKB | ChEBI)
Binding site370pyruvate 2 (UniProtKB | ChEBI)
Binding site370pyruvate 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functioncystathionine gamma-lyase activity
Molecular Functioncystathionine gamma-synthase activity
Molecular FunctionL-cysteine desulfhydrase activity
Molecular FunctionL-cystine L-cysteine-lyase (deaminating)
Molecular Functionpyridoxal phosphate binding
Biological Processtranssulfuration

Keywords

Names & Taxonomy

Protein names

  • Submitted names
    • Cystathionine gamma-lyase
      (EC:4.4.1.1
      )

Gene names

    • Ordered locus names
      Smal_0489

Organism names

Accessions

  • Primary accession
    B4SII9

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue206N6-(pyridoxal phosphate)lysine

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the trans-sulfuration enzymes family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    390
  • Mass (Da)
    41,514
  • Last updated
    2008-09-23 v1
  • MD5 Checksum
    EF8179497A84CF197E5765041B3B6E72
MSNATSQDRALALATLAIHGGQSPDPSTGAVMPPIYATSTYAQSSPGEHQGFEYSRTHNPTRFAYERCVASLEGGTRGFAFASGMAASSTVIELLDAGSHVVAMDDIYGGSFRLFERVRRRTAGLDFSFVDLTDLAAFEASITPKTKMVWIETPTNPMLKIVDIAAVAAIAKRHGLIVVVDNTFASPMLQRPLELGADLVLHSATKYLNGHSDMVGGMVVVGDNAELAEQMAFLQNSVGGVQGPFDSFLALRGLKTLPLRMKAHCANALALAQWLEKHPAVEKVIYPGLASHPQHELAGKQMAGYGGIVSIVLKGGFDAAKRFCEKTELFTLAESLGGVESLVNHPAVMTHASIPVARREQLGISDALVRLSVGVEDLGDLQVDLGEALK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001111
EMBL· GenBank· DDBJ
ACF50194.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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