Annotations: 1QSG

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1qsga1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1qsga2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1qsgc1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1qsgc2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1qsgd1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1qsgd2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
H	d1qsgh1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
H	d1qsgh2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1qsgb1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1qsgb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
E	d1qsge1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
E	d1qsge2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
F	d1qsgf1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
F	d1qsgf2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
G	d1qsgg1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
G	d1qsgg2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Short-chain dehydrogenases/reductases, SDR	8057187	4000029	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	SDR-like	8057189	3000038	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	SDR-like	8057189	3000038	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	SDR-like	8057189	3000038	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	SDR-like	8057189	3000038	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	SDR-like	8057189	3000038	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	SDR-like	8057189	3000038	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	SDR-like	8057189	3000038	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	SDR-like	8057189	3000038	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	adh_short_C2_1	e1qsgA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)
C	adh_short_C2_1	e1qsgC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)
D	adh_short_C2_1	e1qsgD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)
H	adh_short_C2_1	e1qsgH1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)
B	adh_short_C2_1	e1qsgB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)
E	adh_short_C2_1	e1qsgE1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)
F	adh_short_C2_1	e1qsgF1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)
G	adh_short_C2_1	e1qsgG1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
C	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
D	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
H	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
E	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
F	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
G	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	PF13561	Enoyl-(Acyl carrier protein) reductase (adh_short_C2)	Enoyl-(Acyl carrier protein) reductase	This domain is found in Enoyl-(Acyl carrier protein) reductases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H	ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE	NAD binding NADH binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding heterocyclic compound binding small molecule binding enoyl-[acyl-carrier-protein] reductase (NADH) activity oxidoreductase activity NAD binding NADH binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding heterocyclic compound binding small molecule binding enoyl-[acyl-carrier-protein] reductase (NADH) activity oxidoreductase activity enoyl-[acyl-carrier-protein] reductase activity (NAD(P)H) oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-CH group of donors catalytic activity identical protein binding protein binding	fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process fatty acid elongation carboxylic acid biosynthetic process biosynthetic process small molecule metabolic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process fatty acid elongation carboxylic acid biosynthetic process biosynthetic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process lipid metabolic process response to stimulus response to chemical response to antibiotic protein-containing complex organization protein homotetramerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein tetramerization protein-containing complex assembly protein homooligomerization cellular component organization or biogenesis water-soluble vitamin biosynthetic process biotin metabolic process vitamin biosynthetic process amide biosynthetic process biotin biosynthetic process vitamin metabolic process sulfur compound biosynthetic process sulfur compound metabolic process amide metabolic process water-soluble vitamin metabolic process	cellular anatomical structure membrane intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR002347	Short-chain dehydrogenase/reductase SDR	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR014358	Enoyl-[acyl-carrier-protein] reductase (NADH)	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	enoyl-[acyl-carrier-protein] reductase (NADH) M-CSA #606	Enoyl ACP reductase catalyses the last step in fatty acid biosynthesis. Therefore it is a potential target for antibacterial agent development. It catalyses the NAD(P)H-dependent reduction of enoyl acyl carrier protein. The bacterial form of the enzyme is different from the human form as it exists as a free globular protein rather than a part of a multienzyme complex. EACPR's show homology, and similarity to hydroxysteroid dehydrogenase, and also beta-keto reductase, suggesting divergent evolution has played a role in the development of the pathway of lipid biosynthesis.	Defined by 2 residues: TYR:A-159 [auth A-156]LYS:A-166 [auth A-163] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.3.1.9 (PDB Primary Data) Search M-CSA Motif + EC 1.3.1.9

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.