Literature summary for 1.5.5.2 extracted from

Cabassa-Hourton, C.; Schertl, P.; Bordenave-Jacquemin, M.; Saadallah, K.; Guivarch, A.; Lebreton, S.; Planchais, S.; Klodmann, J.; Eubel, H.; Crilat, E.; Lefebvre-De Vos, D.; Ghelis, T.; Richard, L.; Abdelly, C.; Carol, P.; Braun, H.P.; Savoure, A.
Proteomic and functional analysis of proline dehydrogenase 1 link proline catabolism to mitochondrial electron transport in Arabidopsis thaliana (2016), Biochem. J., 473, 2623-2634 .

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Protein Variants

Protein Variants	Comment	Organism
additional information	generation of an enzyme-deficient prodh1 mutant	Arabidopsis thaliana

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrial membrane	isozyme ProDH1 forms part of a low-molecular-mass (70-140 kDa) complex in the mitochondrial membrane, proteomic analysis	Arabidopsis thaliana	31966	-

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	P92983	-	-

Purification (Commentary)

Purification (Comment)	Organism
partially by isolation of mitochondria	Arabidopsis thaliana

Synonyms

Synonyms	Comment	Organism
ProDH1	-	Arabidopsis thaliana
proline dehydrogenase 1	-	Arabidopsis thaliana

Expression

Organism	Comment	Expression
Arabidopsis thaliana	ProDH activity is high for genotypes in which ProDH, most likely ProDH1, is strongly induced by L-proline	up

General Information

General Information	Comment	Organism
physiological function	L-proline accumulates in many plant species in response to environmental stresses. Upon relief from stress, proline is rapidly oxidized in mitochondria by proline dehydrogenase (ProDH) and then by pyrroline-5-carboxylate dehydrogenase (P5CDH, EC 1.2.1.88). ProDH1 has a role in oxidizing excess proline and transferring electrons to the respiratory chain	Arabidopsis thaliana

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Release 2023.1 (January 2023)