Summary: FdhD/NarQ family
FdhD/NarQ family Provide feedback
A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ,  and FdhD (P32177) are required for formate dehydrogenase activity. Structurally, they possess a deaminase fold with a characteristic binding pocket, suggesting that they might bind a nucleotide or related molecule allosterically to regulate the formate dehydrogenase catalytic subunit .
Glaser P, Danchin A, Kunst F, Zuber P, Nakano MM; , J Bacteriol 1995;177:1112-1115.: Identification and isolation of a gene required for nitrate assimilation and anaerobic growth of Bacillus subtilis. PUBMED:7860592 EPMC:7860592
Iyer LM, Zhang D, Rogozin IB, Aravind L;, Nucleic Acids Res. 2011; [Epub ahead of print]: Evolution of the deaminase fold and multiple origins of eukaryotic editing and mutagenic nucleic acid deaminases from bacterial toxin systems. PUBMED:21890906 EPMC:21890906
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003786
Formate dehydrogenase is required for nitrate inducible formate dehydrogenase activity. In Wolinella succinogenes it is a membranous molybdo-enzyme which is involved in phosphorylative electron transport. The functional formate dehydrogenase may be made up of three or four different subunits [PUBMED:1781728]. In Escherichia coli, FdhD is required for the formation of active formate dehydrogenases.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||formate dehydrogenase complex (GO:0009326)|
|Molecular function||formate dehydrogenase (NAD+) activity (GO:0008863)|
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Curation and family details
|Author:||Mian N, Bateman A, Iyer LM, Zhang D, Aravind, L|
|Number in seed:||203|
|Number in full:||2755|
|Average length of the domain:||230.20 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||86.35 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||10|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the FdhD-NarQ domain has been found. There are 4 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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