InterPro : IPR003814

Name  Formylmethanofuran dehydrogenase, subunit E domain Short Name  FwdEsu_dom
Type  Domain Description  Formylmethanofuran dehydrogenases (), found in methanogenic archaea, are molybdenum or tungsten iron-sulphur proteins containing a pterin dinucleotide cofactor. Formylmethanofuran dehydrogenase catalyses the reversible reduction of CO2and methanofuran via N-carboxymethanofuran (carbamate) to N-formylmethanofuran, the first and second steps in methanogenesis from CO2[]. There are two isoenzymes of formylmethanofuran dehydrogenase: a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The tungsten isoenzyme is constitutively transcribed, whereas transcription of the molybdenum operon is induced by molybdate [].This entry represents a domain found in subunit E of formylmethanofuran dehydrogenase (FmdE). It appears to be related to the Tubulin/FtsZ 2-layer sandwich domain.
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Proteins

InterPro protein domain ID --> Contigs

 

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1 Parent Features

Id Name Short Name Type
IPR018316 Tubulin/FtsZ, 2-layer sandwich domain Tubulin/FtsZ_2-layer-sand-dom Domain

2 Publications

First Author Title Year Journal Volume Pages
Hochheimer A The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme. 1998 Arch Microbiol 170 389-93
Hochheimer A The tungsten formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic for enzymes containing molybdopterin dinucleotide. 1995 Eur J Biochem 234 910-20



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)