D1AB74 · LTP2_THECD

Function

function

Probably involved in bile acid degradation (Probable). In vitro, when associated with the ChsH1/ChsH2 hydratase, catalyzes the retroaldol cleavage of 17-hydroxy-3-oxo-4-pregnene-20-carboxyl-CoA (17-HOPC-CoA), forming androst-4-ene-3,17-dione and propionyl-CoA (PubMed:31209106).
The in vivo substrate is probably a closely analogous bile acid degradation metabolite (Probable)

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
2.4 μM17-HOPC-CoAin the presence of ChsH2-DUF35
kcat is 7.1 sec-1.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site294Proton acceptor
Active site344Proton donor

GO annotations

AspectTerm
Molecular Functionacyltransferase activity, transferring groups other than amino-acyl groups
Molecular Functionlyase activity
Biological Processbile acid catabolic process
Biological Processlipid catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Steroid side-chain-cleaving aldolase
  • EC number
  • Alternative names
    • 3-oxo-23,24-bisnorchol-4-en-17-ol-22-oyl-CoA lyase

Gene names

    • Name
      ltp2
    • Ordered locus names
      Tcur_3479

Organism names

Accessions

  • Primary accession
    D1AB74

Proteomes

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis82Almost loss of activity.
Mutagenesis294Almost loss of activity. Loss of activity; when associated with F-344.
Mutagenesis29613-fold decrease in catalytic efficiency.
Mutagenesis344322-fold decrease in catalytic efficiency. Loss of activity; when associated with F-294.
Mutagenesis34611-fold decrease in catalytic efficiency.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004522441-391Steroid side-chain-cleaving aldolase

Interaction

Subunit

Homodimer (PubMed:31209106).
Interacts with the ChsH1/ChsH2 hydratase via the DUF35 C-terminal region of ChsH2 (ChsH2-DUF35) (PubMed:31209106).

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the thiolase-like superfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    391
  • Mass (Da)
    41,404
  • Last updated
    2010-01-19 v1
  • Checksum
    FEE8D313CF0D8894
MSVLPGAAAIAGIGATEFSKNSGRSELQLACEAVLAAIADAGLEPSDVDGLVTFTADTSSEIHVARNTGIGELKFFSRVGYGGGAACGTVQQAAMAVATGIAEVVVCYRAFNERSGVRYGLGQAGRQMDQGADSAAYAWLLPFGLNTPAQWVAMFARRYMHEYGATSEDFGRVAVVDRKHAATNPKAWFYQRPITLEDHQNSRWIVEPLHLLDCCQESDGGQALVVVSTERARDLPHPPALIWGAAQGSGYDQHMMTSYYRSEITGIPEMGLVGQQLYAQSGLNPSDIGAAILYDHFTPLVLPQLEELGFCARGEAKDFIADGNLEIGGRLPCNTHGGQLGEAYIHGMNGIAEAVRLVRGTSVNQPGDVTNVLVTAGTGVPTSGLILGADR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001738
EMBL· GenBank· DDBJ
ACY99017.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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