2F41

Crystal structure of FapR- a global regulator of fatty acid biosynthesis in B. subtilis

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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)
A	d2f41a1	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	PaaI/YdiI-like	Transcription factor FapR, C-terminal domain	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
B	d2f41b_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	PaaI/YdiI-like	Transcription factor FapR, C-terminal domain	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
D	d2f41d_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	PaaI/YdiI-like	Transcription factor FapR, C-terminal domain	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
C	d2f41c_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	PaaI/YdiI-like	Transcription factor FapR, C-terminal domain	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	PaaI/YdiI-like	8028166	4000624	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8040545	3000149	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8040545	3000149	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8040545	3000149	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8040545	3000149	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	4HBT	e2f41A1	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: 4HBT	ECOD (1.6)
B	4HBT	e2f41B1	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: 4HBT	ECOD (1.6)
D	4HBT	e2f41D1	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: 4HBT	ECOD (1.6)
C	4HBT	e2f41C1	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: 4HBT	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
B	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
D	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
C	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF03061	Thioesterase superfamily (4HBT)	Thioesterase superfamily	This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyses the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas ...	This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyses the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyse the hydrolysis of other long chain fatty acyl-CoA thioesters.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Transcription factor fapR	DNA binding binding organic cyclic compound binding nucleic acid binding transcription regulator activity DNA-binding transcription factor activity	regulation of cellular process negative regulation of biological process RNA metabolic process regulation of primary metabolic process negative regulation of RNA biosynthetic process RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription nucleic acid biosynthetic process regulation of RNA metabolic process negative regulation of cellular process negative regulation of nucleobase-containing compound metabolic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of cellular process negative regulation of biological process RNA metabolic process regulation of primary metabolic process negative regulation of RNA biosynthetic process RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription nucleic acid biosynthetic process regulation of RNA metabolic process negative regulation of cellular process negative regulation of nucleobase-containing compound metabolic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process negative regulation of macromolecule metabolic process regulation of biosynthetic process negative regulation of DNA-templated transcription regulation of biological process negative regulation of metabolic process biological regulation primary metabolic process regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process regulation of gene expression biosynthetic process negative regulation of biosynthetic process negative regulation of macromolecule biosynthetic process metabolic process cellular process regulation of macromolecule biosynthetic process macromolecule metabolic process regulation of DNA-templated transcription regulation of metabolic process negative regulation of RNA metabolic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process lipid biosynthetic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process small molecule metabolic process monocarboxylic acid metabolic process lipid metabolic process negative regulation of small molecule metabolic process ketone metabolic process regulation of lipid metabolic process negative regulation of lipid biosynthetic process regulation of small molecule metabolic process negative regulation of fatty acid biosynthetic process negative regulation of fatty acid metabolic process regulation of ketone metabolic process regulation of fatty acid metabolic process regulation of fatty acid biosynthetic process regulation of lipid biosynthetic process negative regulation of lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR036388	Winged helix-like DNA-binding domain superfamily	Homologous Superfamily
A, B, C, D	IPR029069	HotDog domain superfamily	Homologous Superfamily
A, B, C, D	IPR006683	Thioesterase domain	Domain
A, B, C, D	IPR017275	Transcription factor FapR	Family

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.