8X7F

CryoEM structure of the trifunctional NAD biosynthesis/regulator protein NadR in complex with NAD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000309	molecular_function	nicotinamide-nucleotide adenylyltransferase activity
A	0003824	molecular_function	catalytic activity
A	0009058	biological_process	biosynthetic process
A	0009435	biological_process	NAD+ biosynthetic process
A	0050262	molecular_function	ribosylnicotinamide kinase activity
D	0000309	molecular_function	nicotinamide-nucleotide adenylyltransferase activity
D	0003824	molecular_function	catalytic activity
D	0009058	biological_process	biosynthetic process
D	0009435	biological_process	NAD+ biosynthetic process
D	0050262	molecular_function	ribosylnicotinamide kinase activity
G	0000309	molecular_function	nicotinamide-nucleotide adenylyltransferase activity
G	0003824	molecular_function	catalytic activity
G	0009058	biological_process	biosynthetic process
G	0009435	biological_process	NAD+ biosynthetic process
G	0050262	molecular_function	ribosylnicotinamide kinase activity
J	0000309	molecular_function	nicotinamide-nucleotide adenylyltransferase activity
J	0003824	molecular_function	catalytic activity
J	0009058	biological_process	biosynthetic process
J	0009435	biological_process	NAD+ biosynthetic process
J	0050262	molecular_function	ribosylnicotinamide kinase activity

Functional Information from PROSITE/UniProt

site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GESSGKST

Chain	Residue	Details
A	GLY239-THR246

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	720
Details	Region: {"description":"Ribosylnicotinamide kinase"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	108
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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