2CDH

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


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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
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)
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)
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

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
K [auth A]SCOP2B SuperfamilyThiolase-like8037437 3000122 SCOP2B (2022-06-29)
K [auth A]SCOP2B SuperfamilyThiolase-like8037440 3000122 SCOP2B (2022-06-29)
L [auth B]SCOP2B SuperfamilyThiolase-like8037440 3000122 SCOP2B (2022-06-29)
L [auth B]SCOP2B SuperfamilyThiolase-like8037437 3000122 SCOP2B (2022-06-29)
M [auth C]SCOP2B SuperfamilyThiolase-like8037437 3000122 SCOP2B (2022-06-29)
M [auth C]SCOP2B SuperfamilyThiolase-like8037440 3000122 SCOP2B (2022-06-29)
N [auth D]SCOP2B SuperfamilyThiolase-like8037437 3000122 SCOP2B (2022-06-29)
N [auth D]SCOP2B SuperfamilyThiolase-like8037440 3000122 SCOP2B (2022-06-29)
O [auth E]SCOP2B SuperfamilyThiolase-like8037437 3000122 SCOP2B (2022-06-29)
O [auth E]SCOP2B SuperfamilyThiolase-like8037440 3000122 SCOP2B (2022-06-29)
P [auth F]SCOP2B SuperfamilyThiolase-like8037440 3000122 SCOP2B (2022-06-29)
P [auth F]SCOP2B SuperfamilyThiolase-like8037437 3000122 SCOP2B (2022-06-29)
Q [auth G]SCOP2B SuperfamilySDR-like8057092 3000038 SCOP2B (2022-06-29)
R [auth H]SCOP2B SuperfamilySDR-like8057092 3000038 SCOP2B (2022-06-29)
S [auth I]SCOP2B SuperfamilySDR-like8057092 3000038 SCOP2B (2022-06-29)
T [auth J]SCOP2B SuperfamilySDR-like8057092 3000038 SCOP2B (2022-06-29)
U [auth K]SCOP2B SuperfamilySDR-like8057092 3000038 SCOP2B (2022-06-29)
V [auth L]SCOP2B SuperfamilySDR-like8057092 3000038 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth 0]IMPDH_1st_1e2cdh01 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: IMPDH_1st_1ECOD (1.6)
B [auth 1]IMPDH_1st_1e2cdh11 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: IMPDH_1st_1ECOD (1.6)
C [auth 2]IMPDH_1st_1e2cdh21 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: IMPDH_1st_1ECOD (1.6)
D [auth 3]IMPDH_1st_1e2cdh31 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: IMPDH_1st_1ECOD (1.6)
IA [auth Y]IMPDH_1st_1e2cdhY1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: IMPDH_1st_1ECOD (1.6)
JA [auth Z]IMPDH_1st_1e2cdhZ1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: IMPDH_1st_1ECOD (1.6)
AA [auth Q]FabD_1ste2cdhQ1 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: FabD_1stECOD (1.6)
AA [auth Q]Acyl_transf_1_1ste2cdhQ2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
BA [auth R]FabD_1ste2cdhR1 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: FabD_1stECOD (1.6)
BA [auth R]Acyl_transf_1_1ste2cdhR2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
E [auth 4]FabD_1ste2cdh41 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: FabD_1stECOD (1.6)
E [auth 4]Acyl_transf_1_1ste2cdh42 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
F [auth 5]FabD_1ste2cdh51 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: FabD_1stECOD (1.6)
F [auth 5]Acyl_transf_1_1ste2cdh52 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
G [auth 6]FabD_1ste2cdh61 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: FabD_1stECOD (1.6)
G [auth 6]Acyl_transf_1_1ste2cdh62 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
H [auth 7]FabD_1ste2cdh71 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: FabD_1stECOD (1.6)
H [auth 7]Acyl_transf_1_1ste2cdh72 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
I [auth 8]FabD_1ste2cdh81 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: FabD_1stECOD (1.6)
I [auth 8]Acyl_transf_1_1ste2cdh82 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
J [auth 9]FabD_1ste2cdh91 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: FabD_1stECOD (1.6)
J [auth 9]Acyl_transf_1_1ste2cdh92 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
W [auth M]FabD_1ste2cdhM1 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: FabD_1stECOD (1.6)
W [auth M]Acyl_transf_1_1ste2cdhM2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
X [auth N]FabD_1ste2cdhN1 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: FabD_1stECOD (1.6)
X [auth N]Acyl_transf_1_1ste2cdhN2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
Y [auth O]FabD_1ste2cdhO1 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: FabD_1stECOD (1.6)
Y [auth O]Acyl_transf_1_1ste2cdhO2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
Z [auth P]FabD_1ste2cdhP1 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: FabD_1stECOD (1.6)
Z [auth P]Acyl_transf_1_1ste2cdhP2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
K [auth A]ketoacyl-synte2cdhA1 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: ketoacyl-syntECOD (1.6)
K [auth A]Ketoacyl-synt_Ce2cdhA2 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: Ketoacyl-synt_CECOD (1.6)
L [auth B]ketoacyl-synte2cdhB1 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: ketoacyl-syntECOD (1.6)
L [auth B]Ketoacyl-synt_Ce2cdhB2 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: Ketoacyl-synt_CECOD (1.6)
M [auth C]ketoacyl-synte2cdhC1 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: ketoacyl-syntECOD (1.6)
M [auth C]Ketoacyl-synt_Ce2cdhC2 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: Ketoacyl-synt_CECOD (1.6)
N [auth D]ketoacyl-synte2cdhD1 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: ketoacyl-syntECOD (1.6)
N [auth D]Ketoacyl-synt_Ce2cdhD2 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: Ketoacyl-synt_CECOD (1.6)
O [auth E]ketoacyl-synte2cdhE1 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: ketoacyl-syntECOD (1.6)
O [auth E]Ketoacyl-synt_Ce2cdhE2 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: Ketoacyl-synt_CECOD (1.6)
P [auth F]ketoacyl-synte2cdhF1 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: ketoacyl-syntECOD (1.6)
P [auth F]Ketoacyl-synt_Ce2cdhF2 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: Ketoacyl-synt_CECOD (1.6)
Q [auth G]adh_short_C2_1e2cdhG1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
R [auth H]adh_short_C2_1e2cdhH1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
S [auth I]adh_short_C2_1e2cdhI1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
T [auth J]adh_short_C2_1e2cdhJ1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
U [auth K]adh_short_C2_1e2cdhK1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
V [auth L]adh_short_C2_1e2cdhL1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
CA [auth S]MaoC_dehydratase2cdhS1 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: MaoC_dehydratasECOD (1.6)
CA [auth S]MaoC_dehydrat_Ne2cdhS2 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: MaoC_dehydrat_NECOD (1.6)
DA [auth T]MaoC_dehydratase2cdhT1 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: MaoC_dehydratasECOD (1.6)
DA [auth T]MaoC_dehydrat_Ne2cdhT2 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: MaoC_dehydrat_NECOD (1.6)
EA [auth U]MaoC_dehydratase2cdhU1 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: MaoC_dehydratasECOD (1.6)
EA [auth U]MaoC_dehydrat_Ne2cdhU2 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: MaoC_dehydrat_NECOD (1.6)
FA [auth V]MaoC_dehydratase2cdhV1 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: MaoC_dehydratasECOD (1.6)
FA [auth V]MaoC_dehydrat_Ne2cdhV2 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: MaoC_dehydrat_NECOD (1.6)
GA [auth W]MaoC_dehydratase2cdhW1 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: MaoC_dehydratasECOD (1.6)
GA [auth W]MaoC_dehydrat_Ne2cdhW2 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: MaoC_dehydrat_NECOD (1.6)
HA [auth X]MaoC_dehydratase2cdhX1 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: MaoC_dehydratasECOD (1.6)
HA [auth X]MaoC_dehydrat_Ne2cdhX2 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: MaoC_dehydrat_NECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF02801Beta-ketoacyl synthase, C-terminal domain (Ketoacyl-synt_C)Beta-ketoacyl synthase, C-terminal domainThe 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
PF00109Beta-ketoacyl synthase, N-terminal domain (ketoacyl-synt)Beta-ketoacyl synthase, N-terminal domainThe 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
PF00106short chain dehydrogenase (adh_short)short chain dehydrogenaseThis family contains a wide variety of dehydrogenases.Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
ENOYL REDUCTASE---
MALONYL/PALMITOYL TRANSFERASE---
KETOACYL SYNTHASE
KETOACYL REDUCTASE
DEHYDRATASE---

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
IPR016039Thiolase-likeHomologous Superfamily
IPR014031Beta-ketoacyl synthase, C-terminalDomain
IPR000794Beta-ketoacyl synthaseFamily
IPR018201Beta-ketoacyl synthase, active siteActive Site
IPR020841Polyketide synthase, beta-ketoacyl synthase domainDomain
IPR014030Beta-ketoacyl synthase, N-terminalDomain
IPR0112843-oxoacyl-(acyl-carrier-protein) reductaseFamily
IPR036291NAD(P)-binding domain superfamilyHomologous Superfamily
IPR002347Short-chain dehydrogenase/reductase SDRFamily
IPR020904Short-chain dehydrogenase/reductase, conserved siteConserved Site