Sodium/pantothenate symporter; Catalyzes the sodium-dependent uptake of extracellular pantothenate. pass membrane protein (TC 2.A.21) family; sp|P44963|PANF_HAEIN;evalue=9e-017; PctID=22.96; score=89.0; Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.

Phenylacetate-coenzyme A ligase; Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA). Involved in the phenylalanine metabolism. + phenylacetyl-CoA. Kinetic parameters: KM=6 uM for ATP (at 50 degrees Celsius and pH 7.5); KM=30 uM for CoA (at 50 degrees Celsius and pH 7.5); KM=50 uM for PA (at 50 degrees Celsius and pH 7.5); Temperature dependence: Optimum temperature is 75 degrees Celsius. The enzyme is heat stable; sp|Q72K16|PAAK_THET2;evalue=1e-033; PctID=30.18; score=144.

Phenylacetate-coenzyme A ligase; Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA). Involved in the phenylalanine metabolism. Can also use CTP and UTP as substrate. + phenylacetyl-CoA. mercury) and by the sulfhydryl reagents 5,5-dithiobis(2-nitrobenzoic acid), N-ethylmaleimide and p-chloromercuribenzoate. Kinetic parameters: KM=9.7 mM for ATP (at 30 degrees Celsius and pH 8.2); KM=1 mM for CoA (at 30 degrees Celsius and pH 8.2); KM=16.5 mM for PA (at 30 degrees Celsius and pH 8.2); pH dependence: Optimum pH is 8.2; Temperature dependence: Optimum temperatu [...]

Phenylacetate-coenzyme A ligase; Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA). Involved in the phenylalanine metabolism. + phenylacetyl-CoA. presence of a 1 mM of the divalent cations zinc, copper, and nickel. Kinetic parameters: KM=14 uM for PA (aerobically at 37 degrees Celsius); KM=45 uM for CoA (aerobically at 37 degrees Celsius); KM=60 uM for ATP (aerobically at 37 degrees Celsius); pH dependence: Optimum pH is between 8 and 8.5,with a dramatic drop of activity (55%) at pH 9. Less than 10% activity is observed a pH 6, and half the maximal activit [...]

Putative acyl-CoA synthetase YngI; sp|O31826|YNGI_BACSU;evalue=4e-167; PctID=52.16; score=588.

1,3-propanediol dehydrogenase; Most active with substrates containing two primary alcohol groups separated by one or two carbon atoms. In the physiological direction, 3-hydroxypropionaldehyde is the preferred substrate. + NADH. Name=Fe cation; Xref=ChEBI:CHEBI:24875; family; sp|P45513|DHAT_CITFR;evalue=4e-074; PctID=37.20; score=278.

Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (omega=0); sp|P35137|PPIB_BACSU;evalue=9e-041; PctID=60.28; score=165.

Putative ribitol-5-phosphate cytidylyltransferase; Provides activated ribitol phosphate for teichoic acid synthesis. CDP-ribitol. acid biosynthesis; sp|Q8RKI9|TARI_BACPZ;evalue=1e-075; PctID=56.22; score=282.

Fumarate reductase (CoM/CoB) subunit A; {ECO:0000305}; Catalyzes the reduction of fumarate with reduced coenzyme M (CoM-S-H) and coenzyme B (CoB-S-H). In vitro, is able to reduces fumarate with reduced benzyl viologen,oxidize CoM-S-H and CoB-S-H to CoM-S-S-CoB with methylene blue, and reduce CoM-S-S-CoB with reduced benzyl viologen. The enzyme has specificity for the two thiol compounds as the CoB-CoM heterodisulfide reductase. The enzyme is very sensitive to oxygen. CoB. Name=an oxidized flavin; Xref=ChEBI:CHEBI:60531; Evidence=; Note=Binds 1 flavin covalently per subunit; Kinetic par [...]