Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe | Hmd holoenzyme is comprised of 2 iron atoms, each iron atom coordinates the reduction of methenyltetrahydromethanopterin and oxidation of H2 while bound to both Hmd and a cofactor molecule | Methanocaldococcus jannaschii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
38000 | - |
the Hmd holoenzyme is comprised of a homodimer of 38 kDa subunits, 2 pyridone derivative cofactor molecules and 2 iron atoms | Methanocaldococcus jannaschii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
5,10-methenyltetrahydromethanopterin + H2 | Methanocaldococcus jannaschii | Hmd catalyzes a step in the hydrogenotrophic methanogenesis pathway in class I methanogens | 5,10-methylenetetrahydromethanopterin + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methanocaldococcus jannaschii | Q58194 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
5,10-methenyltetrahydromethanopterin + H2 | Hmd catalyzes a step in the hydrogenotrophic methanogenesis pathway in class I methanogens | Methanocaldococcus jannaschii | 5,10-methylenetetrahydromethanopterin + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 38000, structural modeling of Hmd enzyme reveals a common structural arrangement comprised of one large N-terminal domain containing alpha-helices and beta-sheets and one smaller C-terminal domain containing only alpha-helices | Methanocaldococcus jannaschii |
Synonyms | Comment | Organism |
---|---|---|
H2-forming methylenetetrahydromethanopterin dehydrogenase | - |
Methanocaldococcus jannaschii |
Hmd | - |
Methanocaldococcus jannaschii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
coenzyme F420 | - |
Methanocaldococcus jannaschii |