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InterPro: IPR012134 Glutamate-5-semialdehyde dehydrogenase
Protein matches
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UniProtKB Matches: 1552 proteins |
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Accession
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IPR012134 Glu-5-SA_DH |
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Type
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Family |
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Signatures
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InterPro Relationships
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Parent
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IPR000965 Gamma-glutamyl phosphate reductase GPR
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Contains
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IPR016162 Aldehyde dehydrogenase, N-terminal
IPR016163 Aldehyde dehydrogenase, C-terminal
IPR020593 Gamma-glutamyl phosphate reductase GPR, conserved site
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GO Term annotation
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Process
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GO:0006561 proline biosynthetic process
GO:0055114 oxidation reduction
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Function
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GO:0004350 glutamate-5-semialdehyde dehydrogenase activity
GO:0050661 NADP or NADPH binding
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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Gamma-glutamyl phosphate reductase (GPR), also known as glutamate-5-semialdehyde dehydrogenase, catalyses the second step of proline biosynthesis, the NADPH-dependent reversible reduction of gamma-glutamyl phosphate to glutamate-5-semialdehyde as shown below.
L-glutamyl 5-phosphate + NADPH + H(+) = L-glutamate 5-semialdehyde + phosphate + NADP(+)
In bacteria and yeast, GPR is a monofunctional protein, while in plants and mammals, it is part of a bifunctional enzyme that consists of two domains, an N-terminal glutamate 5-kinase domain (EC:2.7.2.11) and a C-terminal GPR domain [1, 2, 3].
This entry represents the monofunctional gamma-glutamyl phosphate reductase found in bacteria and yeasts. Structural studies indicate that this protein is composed of three domains and belongs to the aldehyde dehydrogenase structural family [4]. The first two domains, the catalytic and cofactor binding domains respectively, both form a similar three layered alpha-beta-alpha fold, and are thought to close around the NADPH and gamma-glutamyl-phosphate ligands upon binding in order to orient a conserved cysteine residue for catalysis. The third domain is the oligomerisation domain which forms an antiparallel beta sheet. The biological oligomerisation state of the protein is not currently known, but like most members of the aldehyde dehydrogenase family it is expected to be either a dimer or a tetramer.
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Structural links
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Database links
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Publications
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1.
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Sleator RD, Gahan CG, Hill C.
Identification and disruption of the proBA locus in Listeria monocytogenes: role of proline biosynthesis in salt tolerance and murine infection.
Appl. Environ. Microbiol. 67 2571-7 2001
[PubMed: 11375165]
http://dx.doi.org/10.1128/AEM.67.6.2571-2577.2001
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2.
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Pearson BM, Hernando Y, Payne J, Wolf SS, Kalogeropoulos A, Schweizer M.
Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII.
Yeast 12 1021-31 1996
[PubMed: 8896266]
http://dx.doi.org/10.1002/(SICI)1097-0061(199609)12:10B<1021::AID-YEA981>3.3.CO;2-Z
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3.
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Hu CA, Delauney AJ, Verma DP.
A bifunctional enzyme (delta 1-pyrroline-5-carboxylate synthetase) catalyzes the first two steps in proline biosynthesis in plants.
Proc. Natl. Acad. Sci. U.S.A. 89 9354-8 1992
[PubMed: 1384052]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=1384052
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4.
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Page R, Nelson MS, von Delft F, Elsliger MA, Canaves JM, Brinen LS, Dai X, Deacon AM, Floyd R, Godzik A, Grittini C, Grzechnik SK, Jaroszewski L, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Robb A, Rodrigues K, Schwarzenbacher R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Hodgson KO, Wooley J, Wilson IA.
Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 A resolution.
Proteins 54 157-61 2004
[PubMed: 14705032]
http://dx.doi.org/10.1002/prot.10562
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InterPro 23.1
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