8RJA

Crystal structure of the F420-reducing formylmethanofuran dehydrogenase complex from the ethanotroph Candidatus Ethanoperedens thermophilum

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B	0015948	biological_process	methanogenesis
B	0016491	molecular_function	oxidoreductase activity
B	0018493	molecular_function	formylmethanofuran dehydrogenase activity
C	0015948	biological_process	methanogenesis
C	0016491	molecular_function	oxidoreductase activity
C	0018493	molecular_function	formylmethanofuran dehydrogenase activity
C	0046914	molecular_function	transition metal ion binding
D	0016491	molecular_function	oxidoreductase activity
D	0043546	molecular_function	molybdopterin cofactor binding
E	0016491	molecular_function	oxidoreductase activity
E	0052592	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor
F	0016491	molecular_function	oxidoreductase activity
G	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
H	0015948	biological_process	methanogenesis
H	0016491	molecular_function	oxidoreductase activity
H	0018493	molecular_function	formylmethanofuran dehydrogenase activity
I	0015948	biological_process	methanogenesis
I	0016491	molecular_function	oxidoreductase activity
I	0018493	molecular_function	formylmethanofuran dehydrogenase activity
I	0046914	molecular_function	transition metal ion binding
J	0016491	molecular_function	oxidoreductase activity
J	0043546	molecular_function	molybdopterin cofactor binding
K	0016491	molecular_function	oxidoreductase activity
K	0052592	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor
L	0016491	molecular_function	oxidoreductase activity

Functional Information from PROSITE/UniProt

site_id	PS00198
Number of Residues	12
Details	4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CvSCGnCAaVCP

Chain	Residue	Details
E	CYS18-PRO29
E	CYS58-PRO69
F	CYS16-PRO27
F	CYS61-PRO72

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