1KAS

BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1kasa2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase II, C-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1kasa1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase II, N-terminal domain	(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	SCOP2B Superfamily	Thiolase-like	8041847	3000122	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Thiolase-like	8041846	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)
A	ketoacyl-synt	e1kasA1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ketoacyl-synt	ECOD (1.6)
A	Ketoacyl-synt_C_1	e1kasA2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Ketoacyl-synt_C_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	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
A	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
A	BETA-KETOACYL ACP SYNTHASE II	identical protein binding protein binding binding protein homodimerization activity protein dimerization activity 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 biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process fatty acid elongation, saturated fatty acid fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process cellular metabolic process oxoacid metabolic process cellular biosynthetic process lipid biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process fatty acid elongation, saturated fatty acid 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 fatty acid elongation biosynthetic process cellular lipid metabolic process metabolic process cellular process monocarboxylic acid metabolic process lipid metabolic process response to stimulus response to stress response to abiotic stimulus response to cold response to temperature stimulus monounsaturated fatty acid biosynthetic process monounsaturated fatty acid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR014031	Beta-ketoacyl synthase, C-terminal	Domain
A	IPR000794	Beta-ketoacyl synthase	Family
A	IPR014030	Beta-ketoacyl synthase, N-terminal	Domain
A	IPR016039	Thiolase-like	Homologous Superfamily
A	IPR018201	Beta-ketoacyl synthase, active site	Active Site
A	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain	Domain
A	IPR017568	3-oxoacyl-[acyl-carrier-protein] synthase 2	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
A	beta-ketoacyl-acyl-carrier-protein synthase II M-CSA #574	In the biosynthesis of fatty acids, the beta-ketoacyl-acyl carrier protein (ACP) synthases catalyse chain elongation by the addition of two-carbon units derived from malonyl-ACP to an acyl group bound to ACP. In Escherichia coli , the chain elongation step of fatty acid biosynthesis is carried out by at least three different enzymes, KAS I, II and III. Both KAS I and KAS II catalyse the condensation of a wide range of saturated acyl-ACPs. KAS I, however, may be responsible for a condensation reaction that cannot be catalysed by KAS II, namely elongation of C10:1, whereas KAS II is responsible for the elongation of palmoleitic acid C16:1 to cis -vaccenic acid C18:1. In E.coli, cis vaccenic acid synthesis increases upon a temperature downshift, and KAS II is believed to play a key role in this thermal regulation of fatty acid biosynthesis. KAS II is a homodimer and also known as FabF, name of gene coding for it. .	Defined by 6 residues: CYS:A-163HIS:A-303GLU:A-314LYS:A-335HIS:A-340PHE:A-400 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.3.1.41 (PDB Primary Data) Search M-CSA Motif + EC 2.3.1.41

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.