2NQT

Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis at 1.58 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003942	molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0006526	biological_process	L-arginine 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	0051287	molecular_function	NAD binding
A	0070401	molecular_function	NADP+ binding
B	0003942	molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0006526	biological_process	L-arginine 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	0051287	molecular_function	NAD binding
B	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. IAvPGCYPTAallALfP

Chain	Residue	Details
A	ILE153-PRO169

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00150","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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