Probable bifunctional PutA protein; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family.

Glycine cleavage system P-protein; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.

Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.

Glutamate synthase (small chain) oxidoreductase; Glutamate synthase [NADPH] precursor (EC 1.4.1.13) (NADPH-GOGAT)small chain. TREMBL:Q8XV67-77% identity, 87% similarity InterPro:IPR006005- One pathway for the assimilation of ammonia and glutamate biosynthesis involves glutamate synthase (EC: 1.4.1.13) which transfers the amide group of glutamine to 2-oxoglutarate to yield two molecules of glutamate. 2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+ gid: gid protein Pfam:FAD binding domain,Thi family, 4Fe-4S binding domain,KTN-NAD binding domain, DUF127; High confidence [...]

Dihydrolipoamide dehydrogenase. Homology to lpdA of N. meningitides of 70% (trembl|Q59099). THE BRANCHED-CHAIN ALPHA-KETO DEHYDROGENASE COMPLEX CATALYZES THE OVERALL CONVERSION OF ALPHA-KETO ACIDS TO ACYL-COA AND CO(2). IT CONTAINS MULTIPLE COPIES OF 3 ENZYMATIC COMPONENTS: BRANCHED-CHAIN ALPHA-KETO ACID DECARBOXYLASE (E1) LIPOAMIDE ACYLTRANSFERASE (E2) AND LIPOAMIDE DEHYDROGENASE (E3) (BY SIMILARITY). InterPro: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (IPR001327); Pyridine nucleotide-disulphide oxidoreductase, classI (IPR001100); biotin/Lipoyl attachment (IPR000089) [...]

Putative glutamine amidotransferase; Hypothetical protein ycjL. TREMBL:Q890B8: 38% identity, 53% similarity. Glutamine amidotransferase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a pecific substrate, thus creating a new carbon-nitrogen group on the substrate. InterPro:IPR000991; GATase_1 PROSITE PS00442 GATASE_TYPE_I BLOCKS: BL00442 PFAM:PF00117 GATase; PF00310 GATase_2 trpG_papA: glutamine amidotransferase o No signal peptide (SignalP predicted) No transmembrane helices; High confidence in function and specificity.

Nitrogenase molybdenum-iron protein beta chain; This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation; Belongs to the NifD/NifK/NifE/NifN family.

Probable [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 si [...]

Benzoyl-CoA oxygenase component A. 84% 4Fe4S_ferredoxin. IPR001709; FPN_cyt_redctse. IPR001433; Oxred_FAD/NAD(P). Pfam:PF00037; Fer4; 2. PF00175; NAD_binding_1; 1; High confidence in function and specificity.