spacer
spacer

Jump to: InterProScan Databases Documentation FTP site Help Advanced search

InterPro: IPR017550 Formylmethanofuran dehydrogenase subunit C

Protein matchesHelp
UniProtKB
Matches:
91 proteins
AccessionHelp IPR017550 Formylmethanofuran_DH_suC
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR002489 Glutamate synthase, alpha subunit, C-terminal
Found in IPR012048 Formylmethanofuran dehydrogenase, fused subunit C/D
GO Term annotationHelp
Process GO:0015948 methanogenesis
GO:0055114 oxidation reduction
Function GO:0018493 formylmethanofuran dehydrogenase activity
GO:0046914 transition metal ion binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This entry represents the C subunit of formylmethanofuran dehydrogenase (EC:1.2.99.5), which is involved in methane biosynthesis from carbon dioxide [1, 2]. This oxygen-labile enzyme catalyses the reversible oxidation of carbon dioxide and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). There is a tungsten-containing (Fwd) form of this enzyme and a molybdenum-containing (Fmd) form; this entry includes both forms [3]. Formylmethanofuran dehydrogenase is composed of 5-7 subunits, of which subunit C (FwdC or FmdC) is one. The enzymes in this entry are largely from archaeal species. Nomenclature in some bacteria may reflect inclusion of the formyltransferase described by IPR014053 as part of the complex.

Database linksHelp
Enzyme: EC:1.2.99.5

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR017550 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O27002 Molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR017550 Formylmethanofuran dehydrogenase subunit C
IPR009010 Aspartate decarboxylase-like fold
IPR006657 Molydopterin dinucleotide-binding domain
IPR012048 Formylmethanofuran dehydrogenase, fused subunit C/D
IPR002489 Glutamate synthase, alpha subunit, C-terminal
SWISS-MODEL
ModBase

PublicationsHelp
1. Deppenmeier U.
The unique biochemistry of methanogenesis.
Prog. Nucleic Acid Res. Mol. Biol. 71 223-83 2002 [PubMed: 12102556]
http://dx.doi.org/10.1016/S0079-6603(02)71045-3
2. Pomper BK, Vorholt JA.
Characterization of the formyltransferase from Methylobacterium extorquens AM1.
Eur. J. Biochem. 268 4769-75 2001 [PubMed: 11532013]
http://dx.doi.org/10.1046/j.1432-1327.2001.02401.x
3. Vorholt JA, Thauer RK.
Molybdenum and tungsten enzymes in C1 metabolism.
39 571-619 2002 [PubMed: 11913137]

Additional ReadingHelp
Hochheimer A, Linder D, Thauer RK, Hedderich R.
The molybdenum formylmethanofuran dehydrogenase operon and the tungsten formylmethanofuran dehydrogenase operon from Methanobacterium thermoautotrophicum. Structures and transcriptional regulation.
Eur. J. Biochem. 242 1996 156-62 [PubMed: 8954165]
http://dx.doi.org/10.1111/j.1432-1033.1996.0156r.x
spacer
spacer
InterPro 23.1