CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1150 | Aspartate Aminotransferase, domain 1 |
|
3.90.1150.10 | Aspartate Aminotransferase, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Aspartate Aminotransferase, domain 1 |
| Functional Family | Cysteine desulfurase |
Enzyme Information
| 2.8.1.7 |
Cysteine desulfurase.
based on mapping to UniProt P77444
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.
-!- The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. -!- The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin). -!- In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation.
|
| 4.4.1.16 |
Selenocysteine lyase.
based on mapping to UniProt P77444
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor.
-!- Dithiothreitol or 2-mercaptoethanol can act as the reducing agent in the reaction. -!- The enzyme from animals does not act on cysteine, serine or chloroalanine, while the enzyme from bacteria shows activity with cysteine (cf. EC 2.8.1.7).
|
UniProtKB Entries (1)
| P77444 |
SUFS_ECOLI
Escherichia coli K-12
Cysteine desulfurase
|
PDB Structure
| PDB | 1I29 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward
selenocysteine.
J.BIOCHEM.(TOKYO)
|
