1VLU

Crystal structure of Gamma-glutamyl phosphate reductase (yor323c) from Saccharomyces cerevisiae at 2.40 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004350	molecular_function	glutamate-5-semialdehyde dehydrogenase activity
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006561	biological_process	obsolete proline biosynthetic process
A	0008652	biological_process	amino acid biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0050661	molecular_function	NADP binding
A	0055129	biological_process	L-proline biosynthetic process
B	0004350	molecular_function	glutamate-5-semialdehyde dehydrogenase activity
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006561	biological_process	obsolete proline biosynthetic process
B	0008652	biological_process	amino acid biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0050661	molecular_function	NADP binding
B	0055129	biological_process	L-proline biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS01223
Number of Residues	22
Details	PROA Gamma-glutamyl phosphate reductase signature. VtstesAIqHIntHSSrHTDa.I

Chain	Residue	Details
A	VAL339-ILE360

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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