A0A0M8X8V6 · A0A0M8X8V6_9ACTN

Function

function

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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Pathway

Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2.
Antibiotic biosynthesis.
Metabolic intermediate biosynthesis; 2-deoxystreptamine biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 3/4.

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site35Zn2+ 1 (UniProtKB | ChEBI); catalytic
Active site37Charge relay system
Active site40Charge relay system
Binding site60Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site61Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site90Zn2+ 2 (UniProtKB | ChEBI)
Binding site93Zn2+ 2 (UniProtKB | ChEBI)
Binding site96Zn2+ 2 (UniProtKB | ChEBI)
Binding site104Zn2+ 2 (UniProtKB | ChEBI)
Site145Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atom
Binding site172NAD+ (UniProtKB | ChEBI)
Binding site192NAD+ (UniProtKB | ChEBI)
Binding site197NAD+ (UniProtKB | ChEBI)
Binding site259-261NAD+ (UniProtKB | ChEBI)
Binding site283-284NAD+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionL-threonine 3-dehydrogenase activity
Molecular Functionzinc ion binding
Biological ProcessL-threonine catabolic process to glycine

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    L-threonine 3-dehydrogenase
  • EC number
  • Short names
    TDH

Gene names

    • Name
      tdh
    • ORF names
      ADK65_19745

Organism names

  • Taxonomic identifier
  • Strain
    • NRRL B-1140
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A0M8X8V6

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-335Enoyl reductase (ER)

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    339
  • Mass (Da)
    36,241
  • Last updated
    2015-12-09 v1
  • Checksum
    0C80869BA11E2284
MVKQKAEPGLWLADVPEPTVGPKDVLIRVLRTGICGTDLHIRAWDGWARQAISTPLVVGHEFVGEVVETGRDVTDISVGDRVSGEGHLVCGKCRNCLAGRRHLCRATVGLGVGRDGAFAEYVALPAGNVWVHRVPVDLDVAAIFDPFGNAVHTALSFPLVGEDVLVTGAGPIGLMAAAVAKHAGARNVVITDVSEERLELARKIGVSLALNVSEATIADGQRTLGLREGFDIGLEMSGRPEAMRDMIANMTHGGRIAMLGLPAQEFPVDWARVVTSMITIKGIYGREMFETWYAMSVLLEAGLDLAPVITGRYSHRDFEAAFEDAASGRGGKVILDWTA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LGEA01000099
EMBL· GenBank· DDBJ
KOV99183.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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