PROSITE logo
Black ribbon
We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC00701
Glutamate 5-kinase signature


View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC00701

Description

Glutamate 5-kinase (EC 2.7.2.11) (γ-glutamyl kinase) (GK) is the enzyme that catalyzes the first step in the biosynthesis of proline from glutamate, the ATP-dependent phosphorylation of L-glutamate into L-glutamate 5-phosphate.

In eubacteria (gene proB) and yeast [1] (gene PRO1), GK is a monofunctional protein, while in plants and mammals, it is a bifunctional enzyme (P5CS) [2] that consists of two domains: a N-terminal GK domain and a C-terminal γ-glutamyl phosphate reductase domain (EC 1.2.1.41) (see <PDOC00940>).

As a signature pattern, we selected a highly conserved glycine-and alanine-rich region located in the central section of these enzymes.

Yeast hypothetical protein YHR033w is highly similar to GK.

Last update:

December 2004 / Pattern and text revised.

-------------------------------------------------------------------------------


Technical section

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

GLUTAMATE_5_KINASE, PS00902; Glutamate 5-kinase signature  (PATTERN)


References

1AuthorsLi W. Brandriss M.C.
TitleProline biosynthesis in Saccharomyces cerevisiae: molecular analysis of the PRO1 gene, which encodes gamma-glutamyl kinase.
SourceJ. Bacteriol. 174:4148-4156(1992).
PubMed ID1350780

2AuthorsHu 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



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.