Polyhydroxyalkanoic acid synthase, putative; PHA synt Hase,PHB polymerase, poly-beta-hydroxybutyrate polymerase; identified by match to protein family HMM PF00441 match to protein family HMM PF02770 match to protein family HMM PF08028.

acetoacetyl-CoA reductase; Identified by match to protein family HMM PF04333.

Polyhydroxyalkanoate synthesis repressor PhaR.

Transglutaminase-like domain protein; Identified by match to protein family HMM PF00270 match to protein family HMM PF00271.

Transglutaminase-like domain protein; Identified by match to protein family HMM PF01979 match to protein family HMM PF07969.

Transcriptional regulatory protein FlbD (LafK); Contains PF00158.

Glutamate-ammonia-ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...]

Alpha-glucosidase, putative; Identified by match to protein family HMM PF00383.

protein-P-II uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.