P0C2X9
uniprot
P0C2X9
canonical
amino_acid_sequence
MLPPALLRRSLLSYAWRGSGLRWKHASSLKVANEPILAFTQGSPERDALQKALNDLKDQTEAIPCVVGDEEVWTSDVRYQLSPFNHGHKVAKFCYADKALLNKAIEAAVLARKEWDLKPVADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKFAVELEGEQPISVPPSTNHVVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNVIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTFPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPQSLWPQIKGRLLEEHSRIKVGNPAEDFGTFFSAVIDAKAFARIKKWLEHARSSPSLSILAGGQCNESVGYFVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDEKYRETLQLVDSTTSYGLTGAVFAQDKTIVQEATRMLRNAAGNFYINDKSTGSVVGQQPFGGARASGERDIPGQPRLVQLWTEPPFTPLAVSPPLGDWRYSYMQ
uniprot
proteins
ec_number
1.2.1.88
uniprot
proteins
function
FUNCTION: Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes (By similarity). {ECO:0000250}.
uniprot
proteins
mass_dalton
61869
uniprot
proteins
pathway_participation
PATHWAY: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.
uniprot
proteins
protein_family
Aldehyde dehydrogenase family
uniprot
proteins
pubmed
15057822
uniprot
proteins
sequence_length
563
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
uniprot
proteins