Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).

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                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1417861449   1 KIHAGPKFASYLTFS-PSEVKSLQTEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTED 61
Cdd:cd07079   281 ELRGDEETLAILPGAkPATEEDWGTEYLDLILAVKVVDSLDEAIAHINRYGSGHTEAIVTEN 342

Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl phosphate reductase is part of the Pathway/BioSystem: Proline biosynthesis

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                  ....*....|....*....|....*....|....*...
gi 1417861449  24 TEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTED 61
Cdd:COG0014   308 TEYLDLILAVKVVDSLDEAIAHINRYGSGHTEAIVTED 345

Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).

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                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1417861449   1 KIHAGPKFASYLTFS-PSEVKSLQTEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTED 61
Cdd:cd07079   281 ELRGDEETLAILPGAkPATEEDWGTEYLDLILAVKVVDSLDEAIAHINRYGSGHTEAIVTEN 342

delta-1-pyrroline-5-carboxylate synthase

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                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1417861449   1 KIHAGPKFASYLTFSpsEVKSLQTEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTED 61
Cdd:PLN02418  575 TLYGGPRASKLLNIP--EAQSFHHEYSSLACTVEIVDDVHAAIDHIHRHGSAHTDCIVTED 633

gamma-glutamyl phosphate reductase; Provisional

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                  ....*....|....*....|....*....|....*...
gi 1417861449  24 TEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTED 61
Cdd:PRK00197  311 TEYLDLILAVKVVDSLDEAIAHINRYGSGHTEAIVTED 348

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.

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                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1417861449   7 KFASYLTFSPSEVKSLQTEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTED 61
Cdd:cd06534   254 KLVTVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRD 308