TIGRFAM: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; KEGG: sse:Ssed_3164 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family.

Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]

Diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine.

Dihydrodipicolinate synthetase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).

Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan.

biotin--acetyl-CoA-carboxylase ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.

poly(A) polymerase; Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control. Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.

TIGRFAM: carbamoyl-phosphate synthase, large subunit; PFAM: ATP-dependent carboxylate-amine ligase domain protein ATP-grasp; protein of unknown function DUF201; Carbamoyl-phosphate synthase L chain ATP-binding; Carbamoyl-phosphate synthetase large chain oligomerisation; Carbamoyl-phosphate synthetase large chain domain protein; MGS domain protein; KEGG: sse:Ssed_3403 carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family.

Polynucleotide adenylyltransferase/metal dependent phosphohydrolase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.