31% HTH_9; 1. InterPro: IPR003725; ModE:Molybdenum-binding protein N-terminal. ModE are involved in molybdenum transport.These proteins acts both as a repressor and activator of the mod and moa operons,respectively, depending on the properties of the binding site; High confidence in function and specificity.

Putative formate dehydrogenase accessory protein; Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH. Belongs to the FdhD family.

Conserved hypothetical protein. Homology to ebA2947 of Azoarcus sp. EbN1 of 58% (gnl|keqq|eba:ebA2947(KEGG)). No domains predicted. No signal peptide. No TMHs.

Probable formate dehydrogenase alpha subunit. Homology to fdha of W. succinogenes of 44% (pir|S18213) The formate dehydrogenase 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 electrons are utilized mainly in the nitrate respiration by nitrate reductase InterPro: Prokaryotic molybdopterin oxidoreductases (IPR006655) Pfam: Molybdopterin oxidoreductase; Molydopterin dinucleotide binding domain singal peptide no TMHs; High confidence in function and specificity.

Putative Chaperone protein TorD. Homology to torD of E. coli of 23% (sprot|TORD_ECOLI). This family consists of several bacterial TorD proteins. Many prokaryotic molybdoenzymes, for example the TMAO reductase (TorA) of Escherichia coli, require the insertion of a bis(molybdopterin guanine dinucleotide) molybdenum (bis(MGD)Mo) cofactor in its catalytic site to be active and translocated to the periplasm. The TorD chaperone increases apoTorA activation up to four-fold, allowing maturation of most of the apoprotein. Therefore TorD is involved in the first step of TorA maturation to make i [...]

Putative formate dehydrogenase gamma subunit. Homology to fdhC of W. succinogenes of 21% (TREMBL:P28180). Formate dehydrogenase is a membrane-bound complex, formed of at least three different subunits; probable heterotetramer of two FDHA, one FDHB and one FDHC. FdhC probably anchors the enzyme in the membrane and IS PROBABLY THE CYTOCHROME B556(FDO) COMPONENT. no good domains signal peptide 5 TMHs; Family membership.

Probable formate dehydrogenase iron-sulfur subunit. Homology to fdhB of W. succinogenes of 63% (SWISSPROT:FDHB_WOLSU) THIS CHAIN IS AN ELECTRON TRANSFER UNIT CONTAINING 18 CYSTEINE RESIDUES 16 OF WHICH OCCUR IN THREE CLUSTERS. InterPro: 4Fe-4S ferredoxin iron-sulfur binding domain (IPR001450); 7Fe ferredoxin (IPR000813); 3Fe-4S ferredoxin (IPR001080) Pfam: 4Fe-4S binding domain no signal peptide no TMHs; High confidence in function and specificity.

Conserved hypothetical iron-sulfur binding protein. Homology to pb1470 of B. pertussis of 48% (trembl|Q7VY84). Transfer of electrons in a wide variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin iron-sulfur binding domain (IPR001450). Pfam: 4Fe-4S binding domain. no signal peptide. no TMHs; Family membership.

Probable aldehyde ferredoxin oxidoreductase. Homology to aorA of E. acidodaminophilum of 47% (trembl|Q93KC8) InterPro: Aldehyde ferredoxin oxidoreductase (IPR001203) Pfam: Aldehyde ferredoxin oxidoreductase, N-terminus; Aldeyhde ferredoxin oxidoreductase, damains 2&3 no TMHs no signal peptide; High confidence in function and specificity.