CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1170 | Aldehyde Oxidoreductase; domain 3 |
|
3.90.1170.40 | Molybdopterin biosynthesis MoaE subunit |
Domain Context
CATH Clusters
| Superfamily | Molybdopterin biosynthesis MoaE subunit |
| Functional Family | Molybdopterin synthase catalytic subunit MoaE |
Enzyme Information
| 2.8.1.12 |
Molybdopterin synthase.
based on mapping to UniProt P30749
Cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + H(2)O = molybdopterin + 2 [molybdopterin- synthase sulfur-carrier protein].
-!- Catalyzes the synthesis of molybdopterin from cyclic pyranopterin phosphate. -!- Two sulfur atoms are transferred to cyclic pyranopterin phosphate in order to form the characteristic ene-dithiol group found in the molybdenum cofactor. -!- Molybdopterin synthase consists of two large subunits forming a central dimer and two small subunits (molybdopterin-synthase sulfur- carrier proteins) that are thiocarboxylated at the C-terminus by EC 2.8.1.11, molybdopterin synthase sulfurtransferase. -!- The reaction occurs in prokaryotes and eukaryotes.
|
UniProtKB Entries (1)
| P30748 |
MOAD_ECOLI
Escherichia coli K-12
Molybdopterin synthase sulfur carrier subunit
|
PDB Structure
| PDB | 3BII |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of a molybdopterin synthase-precursor Z complex: insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency.
Biochemistry
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