|Function||formate dehydrogenase, alpha subunit|
|Domain Trusted Cutoff||666.25|
|Domain Noise Cutoff||610.65|
|Gene Ontology Term||GO:0008863: formate dehydrogenase (NAD+) activity molecular_function|
| ||GO:0009326: formate dehydrogenase complex cellular_component|
| ||GO:0015942: formate metabolic process biological_process|
|Entry Date||Jul 18 2002 10:30AM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||This HMM describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (PF01568 and PF00384, respectively). The holo-enzyme also contains beta and gamma subunits.
The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances  and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized) .
This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.|
RM MUID: 87008493
RT Cloning, expression, and nucleotide sequence of the formate dehydrogenase genes from Methanobacterium formicicum.
RA Shuber A.P., Orr E.C., Recny M.A., Schendel P.F., May H.D., Schauer N.L., Ferry J.G.
RL J. Biol. Chem. 261:12942-12947(1986).
RM MUID: 97190104
RT Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster.
RA Boyington J.C., Gladyshev V.N., Khangulov S.V., Stadtman T.C., Sun P.D.
RL Science 275:1305-1308(1997).|
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