5XI0

Crystal structure of FabV, a new class of enyl-acyl carrier protein reductase from Vibrio fischeri

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
A	0051287	molecular_function	NAD binding
B	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
B	0051287	molecular_function	NAD binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01838","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01838","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"Plays an important role in discriminating NADH against NADPH","evidences":[{"source":"HAMAP-Rule","id":"MF_01838","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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