Proline dehydrogenase/1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family.

Putative ornithine cyclodeaminase; Catalyzes the conversion of L-ornithine into L-proline with release of ammonia. Is likely involved in the L-ornithine degradation pathway that allows P.putida to utilize this compound as sole carbon and nitrogen source.

Gamma-glutamyl phosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family.

Putative enzyme with PLP binding domain; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.

Proline iminopeptidase; Function of strongly homologous gene; enzyme; Belongs to the peptidase S33 family.

Putative factor involved in shape determination; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component.

4-hydroxyproline epimerase; Catalyzes the reversible epimerization of cis-4-hydroxy-D- proline (c4DHyp) to trans-4-hydroxy-L-proline (t4LHyp). May be involved in a degradation pathway that allows P.putida strain KT2440 to grow on either epimer of 4-hydroxyproline, c4DHyp and t4LHyp, as the sole carbon and nitrogen source. Does not exhibit measureable racemase activity in vitro with any of the 19 natural chiral amino acid enantiomers.

Alanine racemase; Amino-acid racemase able to utilize a broad range of substrates. Reversibly racemizes 9 of the 19 natural chiral amino acids known, including both positively charged amino acids (Lys, Arg and His) and non-beta-branched aliphatic amino acids (Ala, Leu, Met, Ser, Gln and Asn). Among these amino acids, activity is the highest with lysine and arginine, and poor or very poor with the others. Plays a primary role in the catabolism of basic amino acid, that allows P.putida strain KT2440 to grow on L-Lys and L-Arg as the sole source of carbon and nitrogen, through conversion [...]

dITP/XTP pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.