Q6L739 · GLDSA_STRKN

  • Protein
    L-glutamine:2-deoxy-scyllo-inosose aminotransferase
  • Gene
    kanB
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

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.
Antibiotic biosynthesis; kanamycin 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
      kanB
    • Synonyms
      kanS1

Organism names

  • Taxonomic identifier
  • Strains
    • ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM Ac-837
    • 21-18
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    Q6L739

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002330191-427L-glutamine:2-deoxy-scyllo-inosose aminotransferase
Modified residue205N6-(pyridoxal phosphate)lysine

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-20Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    427
  • Mass (Da)
    45,870
  • Last updated
    2004-07-05 v1
  • Checksum
    F2F738CC5AD4C7B2
MPLQSSRLAVDNGTPVRGKPWPVWPQPTDGTLDALSRVLRSGRWAISGPYRGVESAERRFARRFADYHRIAHCVPASSGTASLMLALEACGVGAGDEVILPGVTWVASASTVVGVNAVPVFADIDPDTLCLDPDAVEAAITPATKAIVVVHLYAAVADLTRLKEVADRHGIVLIEDCAQAHGAEFEGHKVGTFGAVGTFSMQQSKVLTSGEGGAAITADPVLARRMEHLRADGRCYRDQAPPSGHMELVETGELMGSNRCISEFQAAVLTEQLGELDRFNALRRHNAELLDALLTDVGYRPQRSTPGTTARTYYTYVAELPDAELPGADITKVTEALTAELGFPVAPAYSPLNANPLYDPASRSRFALGPQHEKLIDPARFVLPVSGRLTRRLVTFHHAALLGDESDMRDIAEAFTKVLQHRAVLAA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ582817
EMBL· GenBank· DDBJ
CAE46938.1
EMBL· GenBank· DDBJ
Genomic DNA
AB164642
EMBL· GenBank· DDBJ
BAD20758.1
EMBL· GenBank· DDBJ
Genomic DNA
AJ628422
EMBL· GenBank· DDBJ
CAF31588.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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