2CDH

ARCHITECTURE OF THE THERMOMYCES LANUGINOSUS FUNGAL FATTY ACID SYNTHASE AT 5 ANGSTROM RESOLUTION.

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
Q [auth G]	d2cdhg1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	beta-keto acyl carrier protein reductase	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
R [auth H]	d2cdhh1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	beta-keto acyl carrier protein reductase	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
S [auth I]	d2cdhi1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	beta-keto acyl carrier protein reductase	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
T [auth J]	d2cdhj1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	beta-keto acyl carrier protein reductase	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
U [auth K]	d2cdhk1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	beta-keto acyl carrier protein reductase	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
V [auth L]	d2cdhl1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	beta-keto acyl carrier protein reductase	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
K [auth A]	d2cdha2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, C-terminal domain	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
K [auth A]	d2cdha1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, N-terminal domain	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
L [auth B]	d2cdhb2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, C-terminal domain	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
L [auth B]	d2cdhb1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, N-terminal domain	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
M [auth C]	d2cdhc2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, C-terminal domain	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
M [auth C]	d2cdhc1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, N-terminal domain	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
N [auth D]	d2cdhd2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, C-terminal domain	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
N [auth D]	d2cdhd1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, N-terminal domain	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
O [auth E]	d2cdhe2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, C-terminal domain	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
O [auth E]	d2cdhe1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, N-terminal domain	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
P [auth F]	d2cdhf2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, C-terminal domain	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
P [auth F]	d2cdhf1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, N-terminal domain	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
CA [auth S]	d2cdhs1	Low resolution protein structures	Fatty acid synthase	Fatty acid synthase	Fatty acid syntase	Fungal fatty acid syntase	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
Q [auth G]	SCOP2B Superfamily	SDR-like	8057092	3000038	SCOP2B (2022-06-29)
R [auth H]	SCOP2B Superfamily	SDR-like	8057092	3000038	SCOP2B (2022-06-29)
S [auth I]	SCOP2B Superfamily	SDR-like	8057092	3000038	SCOP2B (2022-06-29)
T [auth J]	SCOP2B Superfamily	SDR-like	8057092	3000038	SCOP2B (2022-06-29)
U [auth K]	SCOP2B Superfamily	SDR-like	8057092	3000038	SCOP2B (2022-06-29)
V [auth L]	SCOP2B Superfamily	SDR-like	8057092	3000038	SCOP2B (2022-06-29)
K [auth A]	SCOP2B Superfamily	Thiolase-like	8037437	3000122	SCOP2B (2022-06-29)
K [auth A]	SCOP2B Superfamily	Thiolase-like	8037440	3000122	SCOP2B (2022-06-29)
L [auth B]	SCOP2B Superfamily	Thiolase-like	8037440	3000122	SCOP2B (2022-06-29)
L [auth B]	SCOP2B Superfamily	Thiolase-like	8037437	3000122	SCOP2B (2022-06-29)
M [auth C]	SCOP2B Superfamily	Thiolase-like	8037437	3000122	SCOP2B (2022-06-29)
M [auth C]	SCOP2B Superfamily	Thiolase-like	8037440	3000122	SCOP2B (2022-06-29)
N [auth D]	SCOP2B Superfamily	Thiolase-like	8037437	3000122	SCOP2B (2022-06-29)
N [auth D]	SCOP2B Superfamily	Thiolase-like	8037440	3000122	SCOP2B (2022-06-29)
O [auth E]	SCOP2B Superfamily	Thiolase-like	8037437	3000122	SCOP2B (2022-06-29)
O [auth E]	SCOP2B Superfamily	Thiolase-like	8037440	3000122	SCOP2B (2022-06-29)
P [auth F]	SCOP2B Superfamily	Thiolase-like	8037440	3000122	SCOP2B (2022-06-29)
P [auth F]	SCOP2B Superfamily	Thiolase-like	8037437	3000122	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)
AA [auth Q]	F_UNCLASSIFIED	e2cdhQ1	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
AA [auth Q]	PF00698	e2cdhQ2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)
BA [auth R]	F_UNCLASSIFIED	e2cdhR1	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
BA [auth R]	PF00698	e2cdhR2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)
E [auth 4]	F_UNCLASSIFIED	e2cdh41	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
E [auth 4]	PF00698	e2cdh42	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)
F [auth 5]	F_UNCLASSIFIED	e2cdh51	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
F [auth 5]	PF00698	e2cdh52	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)
G [auth 6]	F_UNCLASSIFIED	e2cdh61	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
G [auth 6]	PF00698	e2cdh62	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)
H [auth 7]	F_UNCLASSIFIED	e2cdh71	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
H [auth 7]	PF00698	e2cdh72	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)
I [auth 8]	F_UNCLASSIFIED	e2cdh81	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
I [auth 8]	PF00698	e2cdh82	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)
J [auth 9]	F_UNCLASSIFIED	e2cdh91	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
J [auth 9]	PF00698	e2cdh92	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)
W [auth M]	F_UNCLASSIFIED	e2cdhM1	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
W [auth M]	PF00698	e2cdhM2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)
X [auth N]	F_UNCLASSIFIED	e2cdhN1	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
X [auth N]	PF00698	e2cdhN2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)
Y [auth O]	F_UNCLASSIFIED	e2cdhO1	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
Y [auth O]	PF00698	e2cdhO2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)
Z [auth P]	F_UNCLASSIFIED	e2cdhP1	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
Z [auth P]	PF00698	e2cdhP2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)
Q [auth G]	PF00106	e2cdhG1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF00106	ECOD (1.6)
R [auth H]	PF00106	e2cdhH1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF00106	ECOD (1.6)
S [auth I]	PF00106	e2cdhI1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF00106	ECOD (1.6)
T [auth J]	PF00106	e2cdhJ1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF00106	ECOD (1.6)
U [auth K]	PF00106	e2cdhK1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF00106	ECOD (1.6)
V [auth L]	PF00106	e2cdhL1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF00106	ECOD (1.6)
A [auth 0]	PF01070	e2cdh01	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF01070	ECOD (1.6)
B [auth 1]	PF01070	e2cdh11	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF01070	ECOD (1.6)
C [auth 2]	PF01070	e2cdh21	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF01070	ECOD (1.6)
D [auth 3]	PF01070	e2cdh31	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF01070	ECOD (1.6)
IA [auth Y]	PF01070	e2cdhY1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF01070	ECOD (1.6)
JA [auth Z]	PF01070	e2cdhZ1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF01070	ECOD (1.6)
K [auth A]	PF00109	e2cdhA1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00109	ECOD (1.6)
K [auth A]	PF02801	e2cdhA2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02801	ECOD (1.6)
L [auth B]	PF00109	e2cdhB1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00109	ECOD (1.6)
L [auth B]	PF02801	e2cdhB2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02801	ECOD (1.6)
M [auth C]	PF00109	e2cdhC1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00109	ECOD (1.6)
M [auth C]	PF02801	e2cdhC2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02801	ECOD (1.6)
N [auth D]	PF00109	e2cdhD1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00109	ECOD (1.6)
N [auth D]	PF02801	e2cdhD2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02801	ECOD (1.6)
O [auth E]	PF00109	e2cdhE1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00109	ECOD (1.6)
O [auth E]	PF02801	e2cdhE2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02801	ECOD (1.6)
P [auth F]	PF00109	e2cdhF1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00109	ECOD (1.6)
P [auth F]	PF02801	e2cdhF2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02801	ECOD (1.6)
CA [auth S]	PF01575	e2cdhS1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF01575	ECOD (1.6)
CA [auth S]	PF22622	e2cdhS2	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF22622	ECOD (1.6)
DA [auth T]	PF01575	e2cdhT1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF01575	ECOD (1.6)
DA [auth T]	PF22622	e2cdhT2	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF22622	ECOD (1.6)
EA [auth U]	PF01575	e2cdhU1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF01575	ECOD (1.6)
EA [auth U]	PF22622	e2cdhU2	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF22622	ECOD (1.6)
FA [auth V]	PF01575	e2cdhV1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF01575	ECOD (1.6)
FA [auth V]	PF22622	e2cdhV2	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF22622	ECOD (1.6)
GA [auth W]	PF01575	e2cdhW1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF01575	ECOD (1.6)
GA [auth W]	PF22622	e2cdhW2	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF22622	ECOD (1.6)
HA [auth X]	PF01575	e2cdhX1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF01575	ECOD (1.6)
HA [auth X]	PF22622	e2cdhX2	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF22622	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
Q [auth G], R [auth H], S [auth I], T [auth J], U [auth K], Q [auth G], R [auth H], S [auth I], T [auth J], U [auth K], V [auth L]	PF00106	short chain dehydrogenase (adh_short)	short chain dehydrogenase	This family contains a wide variety of dehydrogenases.	Domain
K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], P [auth F]	PF02801	Beta-ketoacyl synthase, C-terminal domain (Ketoacyl-synt_C)	Beta-ketoacyl synthase, C-terminal domain	The structure of beta-ketoacyl synthase is similar to that of the thiolase family (Pfam:PF00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.	Domain
K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], P [auth F]	PF00109	Beta-ketoacyl synthase, N-terminal domain (ketoacyl-synt)	Beta-ketoacyl synthase, N-terminal domain	The structure of beta-ketoacyl synthase is similar to that of the thiolase family (Pfam:PF00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains m ...	The structure of beta-ketoacyl synthase is similar to that of the thiolase family (Pfam:PF00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
AA [auth Q], BA [auth R], E [auth 4], F [auth 5], G [auth 6], AA [auth Q], BA [auth R], E [auth 4], F [auth 5], G [auth 6], H [auth 7], I [auth 8], J [auth 9], W [auth M], X [auth N], Y [auth O], Z [auth P]	MALONYL/PALMITOYL TRANSFERASE	-	-	-
Q [auth G], R [auth H], S [auth I], T [auth J], U [auth K], Q [auth G], R [auth H], S [auth I], T [auth J], U [auth K], V [auth L]	KETOACYL REDUCTASE	NAD binding binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding small molecule binding 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors catalytic activity	fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process biosynthetic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process biosynthetic process organic substance biosynthetic process cellular lipid metabolic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process lipid metabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure plastid organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle chloroplast
A [auth 0], B [auth 1], C [auth 2], D [auth 3], IA [auth Y], A [auth 0], B [auth 1], C [auth 2], D [auth 3], IA [auth Y], JA [auth Z]	ENOYL REDUCTASE	-	-	-
K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], P [auth F]	KETOACYL SYNTHASE	acyltransferase activity 3-oxoacyl-[acyl-carrier-protein] synthase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity	oxoacid metabolic process cellular biosynthetic process lipid biosynthetic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process oxoacid metabolic process cellular biosynthetic process lipid biosynthetic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process primary metabolic process fatty acid biosynthetic process monounsaturated fatty acid biosynthetic process biosynthetic process cellular lipid metabolic process monounsaturated fatty acid metabolic process metabolic process cellular process monocarboxylic acid metabolic process lipid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol
CA [auth S], DA [auth T], EA [auth U], FA [auth V], GA [auth W], CA [auth S], DA [auth T], EA [auth U], FA [auth V], GA [auth W], HA [auth X]	DEHYDRATASE	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
Q [auth G], R [auth H], S [auth I], T [auth J], U [auth K], Q [auth G], R [auth H], S [auth I], T [auth J], U [auth K], V [auth L]	IPR011284	3-oxoacyl-(acyl-carrier-protein) reductase	Family
Q [auth G], R [auth H], S [auth I], T [auth J], U [auth K], Q [auth G], R [auth H], S [auth I], T [auth J], U [auth K], V [auth L]	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
Q [auth G], R [auth H], S [auth I], T [auth J], U [auth K], Q [auth G], R [auth H], S [auth I], T [auth J], U [auth K], V [auth L]	IPR002347	Short-chain dehydrogenase/reductase SDR	Family
Q [auth G], R [auth H], S [auth I], T [auth J], U [auth K], Q [auth G], R [auth H], S [auth I], T [auth J], U [auth K], V [auth L]	IPR020904	Short-chain dehydrogenase/reductase, conserved site	Conserved Site
K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], P [auth F]	IPR016039	Thiolase-like	Homologous Superfamily
K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], P [auth F]	IPR014031	Beta-ketoacyl synthase, C-terminal	Domain
K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], P [auth F]	IPR000794	Beta-ketoacyl synthase	Family
K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], P [auth F]	IPR018201	Beta-ketoacyl synthase, active site	Active Site
K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], P [auth F]	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain	Domain
K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], K [auth A], L [auth B], M [auth C], N [auth D], O [auth E], P [auth F]	IPR014030	Beta-ketoacyl synthase, N-terminal	Domain