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PROSITE documentation PDOC00940

Gamma-glutamyl phosphate reductase signature

Description:

γ-glutamyl phosphate reductase (EC 1.2.1.41) (GPR) is the enzyme that catalyzes the second step in the biosynthesis of proline from glutamate, the NADP-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate.

In eubacteria (gene proA) and yeast [1] (gene PRO2), GPR is a monofunctional protein, while in plants and mammals, it is a bifunctional enzyme (P5CS) [2] that consists of two domains: a N-terminal glutamate 5-kinase domain (EC 2.7.2.11) (see <PDOC00701>) and a C-terminal GPR domain.

As a signature pattern, we selected a conserved region that contains two histidine residues. This region is located in the last third of GPR.

Last update:

April 2006 / Pattern revised.

Technical section:

PROSITE method (with tools and information) covered by this documentation:

PROA, PS01223Gamma-glutamyl phosphate reductase signature  (PATTERN)
Consensus pattern: [VA] - x(5) - A - [LIVAMTCK] - x - [HWFY] - [IM] - x(2) - [HYWNRFT] - [GSNT] - [STAG] - x(0,1) - H - [ST] - [DE] - x(1,2) - I
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE
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Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS01223
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01223
Scan Swiss-Prot/TrEMBL entries against PS01223
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Matching PDB structures: 1O20 1VLU 2H5G [ALL]

References:

1 AuthorsPearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A., Schweizer M.
TitleSequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII.
SourceYeast 12:1021-1031(1996).
PubMed ID8896266
DOI10.1002/(SICI)1097-0061(199609)12:10B<1021::AID-YEA981>3.0.CO;2-7
2 AuthorsHu C.-A.A., Delauney A.J., Verma D.P.S.
TitleA bifunctional enzyme (delta 1-pyrroline-5-carboxylate synthetase) catalyzes the first two steps in proline biosynthesis in plants.
SourceProc. Natl. Acad. Sci. U.S.A. 89:9354-9358(1992).
PubMed ID1384052

Copyright:

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