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 converting factor subunit 2 |
Enzyme Information
2.8.1.12 |
Molybdopterin synthase.
based on mapping to UniProt P65401
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.
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UniProtKB Entries (1)
Q7A441 |
MOAD_STAAN
Staphylococcus aureus subsp. aureus N315
Molybdopterin synthase sulfur carrier subunit
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PDB Structure
PDB | 2Q5W |
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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