A0A060ZSR0 · A0A060ZSR0_9ACTN

  • Protein
    2-deoxy-scyllo-inosamine dehydrogenase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    2/5

Function

function

Catalyzes the oxidation of 2-deoxy-scyllo-inosamine (DOIA) with NAD+ or NADP+, forming 3-amino-2,3-dideoxy-scyllo-inosose (amino-DOI).

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Pathway

Antibiotic biosynthesis.
Metabolic intermediate biosynthesis; 2-deoxystreptamine biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 3/4.

GO annotations

AspectTerm
Molecular Functionoxidoreductase activity
Molecular Functionzinc ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    2-deoxy-scyllo-inosamine dehydrogenase
  • EC number

Gene names

    • ORF names
      SIRAN3330

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces > Streptomyces violaceusniger group

Accessions

  • Primary accession
    A0A060ZSR0

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-340Enoyl reductase (ER)

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    342
  • Mass (Da)
    35,722
  • Last updated
    2014-09-03 v1
  • Checksum
    C30C0B7D9012D2B4
MKAVRVHAYGEPARIESVPDPVVRGPLEVLVEINAAGVCRTDLHILEGQWADKSGVTLPYTIGHENAGTVREVGSAVSGVRPGDKVILHPLVTCGLCRPCRSGDDVHCENSSFPGIDTDGGMAELMLTNARSVVRLSEQLAPADVAALADAGLTAYHAVRKAVPSLYPGTHAVVIGAGGLGHIGLQALLALTPARTIVVDRSPEVLRLAGELGAHHTVHADGSQVDAVRDLTRGAGAQVVLDFVGEHGTESDGIAMTRDAGSYFVIGYGGRVDVPTIDIISREINVIGNLVGSYNDLDELMTLTAQGKVALRTRTYPLDAALDALADLDANRIPGGRAILVP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LK022848
EMBL· GenBank· DDBJ
CDR06436.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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