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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1qsga1 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)
Ad1qsga2 Artifacts Tags Tags Tags N-terminal Tags (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Bd1qsgb1 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)
Bd1qsgb2 Artifacts Tags Tags Tags N-terminal Tags (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Cd1qsgc1 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)
Cd1qsgc2 Artifacts Tags Tags Tags N-terminal Tags (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Dd1qsgd1 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)
Dd1qsgd2 Artifacts Tags Tags Tags N-terminal Tags (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Ed1qsge1 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)
Ed1qsge2 Artifacts Tags Tags Tags N-terminal Tags (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Fd1qsgf1 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)
Fd1qsgf2 Artifacts Tags Tags Tags N-terminal Tags (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Gd1qsgg1 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)
Gd1qsgg2 Artifacts Tags Tags Tags N-terminal Tags (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Hd1qsgh1 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)
Hd1qsgh2 Artifacts Tags Tags Tags N-terminal Tags (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyShort-chain dehydrogenases/reductases, SDR 8057187 4000029 SCOP2 (2022-06-29)
ASCOP2 SuperfamilySDR-like 8057189 3000038 SCOP2 (2022-06-29)
BSCOP2B SuperfamilySDR-like 8057189 3000038 SCOP2B (2022-06-29)
CSCOP2B SuperfamilySDR-like 8057189 3000038 SCOP2B (2022-06-29)
DSCOP2B SuperfamilySDR-like 8057189 3000038 SCOP2B (2022-06-29)
ESCOP2B SuperfamilySDR-like 8057189 3000038 SCOP2B (2022-06-29)
FSCOP2B SuperfamilySDR-like 8057189 3000038 SCOP2B (2022-06-29)
GSCOP2B SuperfamilySDR-like 8057189 3000038 SCOP2B (2022-06-29)
HSCOP2B SuperfamilySDR-like 8057189 3000038 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
Aadh_short_C2_1e1qsgA1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
Badh_short_C2_1e1qsgB1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
Cadh_short_C2_1e1qsgC1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
Dadh_short_C2_1e1qsgD1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
Eadh_short_C2_1e1qsgE1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
Fadh_short_C2_1e1qsgF1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
Gadh_short_C2_1e1qsgG1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
Hadh_short_C2_1e1qsgH1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D, E
PF13561Enoyl-(Acyl carrier protein) reductase (adh_short_C2)Enoyl-(Acyl carrier protein) reductaseThis domain is found in Enoyl-(Acyl carrier protein) reductases.Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D, E
ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A, B, C, D, E
IPR002347Short-chain dehydrogenase/reductase SDRFamily
A, B, C, D, E
IPR014358Enoyl-[acyl-carrier-protein] reductase (NADH)Family
A, B, C, D, E
IPR036291NAD(P)-binding domain superfamilyHomologous Superfamily

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

ChainsEnzyme NameDescriptionCatalytic Residues
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]
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