Due to scheduled maintenance work, this service may not be available on Monday January 22nd between 08.00 am and 9.00 am CEST.
To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https
PROSITE documentation PDOC00701

Glutamate 5-kinase signature


Glutamate 5-kinase (EC (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 (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)


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 copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)