2CVO

Crystal structure of putative N-acetyl-gamma-glutamyl-phosphate reductase (AK071544) from rice (Oryza sativa)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003942	molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity
A	0006526	biological_process	L-arginine biosynthetic process
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0051287	molecular_function	NAD binding
A	0070401	molecular_function	NADP+ binding
B	0003942	molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity
B	0006526	biological_process	L-arginine biosynthetic process
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0051287	molecular_function	NAD binding
B	0070401	molecular_function	NADP+ binding
C	0003942	molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity
C	0006526	biological_process	L-arginine biosynthetic process
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0051287	molecular_function	NAD binding
C	0070401	molecular_function	NADP+ binding
D	0003942	molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity
D	0006526	biological_process	L-arginine biosynthetic process
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0051287	molecular_function	NAD binding
D	0070401	molecular_function	NADP+ binding

Functional Information from PROSITE/UniProt

site_id	PS01224
Number of Residues	17
Details	ARGC N-acetyl-gamma-glutamyl-phosphate reductase active site. VAnPGCYPTSiqlPLvP

Chain	Residue	Details
A	VAL214-PRO230

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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