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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.

December 2004 / Pattern and text revised.

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

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

Consensus pattern: [GSTNAD]-x(2)-[GAS]-x-G-[GC]-[IM]-x-[STAG]-K-[LIVMCT]-x-[SAI]-[TCAGFS]-x(2)-[GALVCMI] Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00902 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00902 • Scan Swiss-Prot/TrEMBL entries against PS00902 • view ligand binding statistics

Matching PDB structures: 2J5T [ALL]

1	Authors	Li W., Brandriss M.C.
	Title	Proline biosynthesis in Saccharomyces cerevisiae: molecular analysis of the PRO1 gene, which encodes gamma-glutamyl kinase.
	Source	J. Bacteriol. 174:4148-4156(1992).
	PubMed ID	1350780

2	Authors	Hu C.-A.A., Delauney A.J., Verma D.P.S.
	Title	A bifunctional enzyme (delta 1-pyrroline-5-carboxylate synthetase) catalyzes the first two steps in proline biosynthesis in plants.
	Source	Proc. Natl. Acad. Sci. U.S.A. 89:9354-9358(1992).
	PubMed ID	1384052

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