Probable methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.

Conserved hypothetical protein. Homology to SMA1058 of S.meliloti of 48% (trembl:Q92ZB7). No domains predicted. No signal peptide. No TMHs.

Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity.

Probable rubredoxin. Homology to ruba of A. calcoaceticus of 42% (sprot|RUBR_ACIAD). Involved in the hydrocarbon hydroxylating system to convert dodecane to lauric acid, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase. Pfam: Rubredoxin no singal peptide no TMHs; Family membership.

Metallo-phosphoesterase, 50% identity(67% similarity) to TrEMBL;Q6N2S9. TrEMBL;Q885N2(53% identity). Has PF00149, Calcineurin-like phosphoesterase;IPR004843,M-pesterase:This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD P13457 or yeast MRE11 P32829. The most conserved regions in this superfamily centre around the metal chelating residues. The metallo-phosphoesterase motif is found in a large number of proteins [...]

AMP deaminase / 5-amino-6-(5-phosphoribosylamino)uracil reductase; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.

Conserved hypothetical transaminase; Region start changed from 3714581 to 3714479 (102 bases).

Putative iron sulfur binding protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family.