Q2MFP2 · GLDSA_STREY

Function

function

Catalyzes the PLP-dependent transamination of 2-deoxy-scyllo-inosose (2-DOI) to form 2-deoxy-scyllo-inosamine (2-DOIA) using L-glutamine as the amino donor. Also catalyzes the transamination of 3-amino-2,3-dideoxy-scyllo-inosose (keto-2-DOIA) into 2-deoxystreptamine (2-DOS).

Catalytic activity

Cofactor

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

Pathway

Metabolic intermediate biosynthesis; 2-deoxystreptamine biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 2/4.
Metabolic intermediate biosynthesis; 2-deoxystreptamine biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 4/4.
Antibiotic biosynthesis; paromomycin biosynthesis.

GO annotations

AspectTerm
Molecular Functionpyridoxal phosphate binding
Molecular Functiontransaminase activity
Biological Processantibiotic biosynthetic process
Biological Processpolysaccharide biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    L-glutamine:2-deoxy-scyllo-inosose aminotransferase
  • EC number
  • Short names
    L-glutamine:DOI aminotransferase
  • Alternative names
    • L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase (L-glutamine:amino-DOI aminotransferase) (EC:2.6.1.101
      ) . EC:2.6.1.101 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      parS

Organism names

Accessions

  • Primary accession
    Q2MFP2

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00002330221-424L-glutamine:2-deoxy-scyllo-inosose aminotransferase
Modified residue202N6-(pyridoxal phosphate)lysine

Structure

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    424
  • Mass (Da)
    45,105
  • Last updated
    2006-02-21 v1
  • Checksum
    6D7C86696A5496DF
MTRSLAVQGGSPVRTRPWPLWPQPAPGAVRALDGVLTSGRWSISGPYRGAASQERRFAQAFAAYNGVEHCVPAASGTASLMLAMEACGIGAGDEVIVPGLSWVASGSTVLGVNAVPVFCDVDPDTLCLDPAAVESALTERTKAIVVVHLYSAVAAMDALRALADRHGLPLLEDCAQAHGAEYRGVKVGALATAGTFSMQHSKVLTSGEGGAVITRDAEFARRVEHLRADGRCLAGQPVGDGQMELVETGELMGSNRCVSEFQAALLVEQLGVLDEQNERRRRNAALLDKLLADEGYRPQTTSEGTSTRTYYTYAARLPEGELTHVDAAAVGEALTAELGFPVAPCYAPITRNRLYDPRSRGRFALGVQHESRIDPKRFELPVCEEAARRTVTVHHAALLGDESDMHDIATAFGKVVRHGALLTG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ628955
EMBL· GenBank· DDBJ
CAF32373.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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