1MLA

THE ESCHERICHIA COLI MALONYL-COA:ACYL CARRIER PROTEIN TRANSACYLASE AT 1.5-ANGSTROMS RESOLUTION. CRYSTAL STRUCTURE OF A FATTY ACID SYNTHASE COMPONENT

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	d1mlaa1	Alpha and beta proteins (a/b)	FabD/lysophospholipase-like	FabD/lysophospholipase-like	FabD-like	Catalytic domain of malonyl-CoA ACP transacylase FabD	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1mlaa2	Alpha and beta proteins (a+b)	Ferredoxin-like	Probable ACP-binding domain of malonyl-CoA ACP transacylase	Probable ACP-binding domain of malonyl-CoA ACP transacylase	Probable ACP-binding domain of malonyl-CoA ACP transacylase	(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	SCOP2 Family	Probable ACP-binding domain of malonyl-CoA ACP transacylase	8023159	4001289	SCOP2 (2022-06-29)
A	SCOP2 Family	FabD-like	8031640	4003614	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Probable ACP-binding domain of malonyl-CoA ACP transacylase	8035539	3001224	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	FabD/lysophospholipase-like	8044018	3001121	SCOP2 (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	F_UNCLASSIFIED	e1mlaA1	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)
A	PF00698	e1mlaA2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.70.250	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Malonyl-CoA ACP transacylase, ACP-binding	CATH (4.3.0)
A	3.40.366.10	Alpha Beta	3-Layer(aba) Sandwich	Malonyl-Coenzyme A Acyl Carrier Protein	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00698	Acyl transferase domain (Acyl_transf_1)	Acyl transferase domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	MALONYL-COENZYME A ACYL CARRIER PROTEIN TRANSACYLASE	malonyltransferase activity acyltransferase activity [acyl-carrier-protein] S-malonyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity S-acyltransferase activity catalytic activity S-malonyltransferase 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	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR016035	Acyl transferase/acyl hydrolase/lysophospholipase	Homologous Superfamily
A	IPR024925	Malonyl CoA-acyl carrier protein transacylase	Family
A	IPR001227	Acyl transferase domain superfamily	Homologous Superfamily
A	IPR016036	Malonyl-CoA ACP transacylase, ACP-binding	Homologous Superfamily
A	IPR014043	Acyl transferase	Domain
A	IPR004410	Malonyl CoA-acyl carrier protein transacylase, FabD-type	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
A	malonyl-CoA-acyl carrier protein transacylase M-CSA #291	In Escherichia coli Fatty acid synthesis, FAS II includes a specific malonyl-CoA:ACP transacylase (MCAT), which catalyses specifically the elongation step. The initiation of each elongation step in the fatty acid synthesis cycle requires the transfer of a malonyl moiety from the respective CoA thioester to the -SH group of the phosphopantetheine arm of the acyl carrier protein (ACP), the central component of any FAS. MCAT, along with Acyl-carrier-protein S-acetyltransferase (EC 2.3.1.38), is essential for the initiation of fatty-acid biosynthesis in bacteria. This enzyme also provides the malonyl groups for polyketide biosynthesis.	Defined by 6 residues: GLN:A-11SER:A-92LEU:A-93ARG:A-117HIS:A-201GLN:A-250 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif

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.