Annotations: 1THT

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1thta_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Thioesterases	Myristoyl-ACP-specific thioesterase	(Vibrio harveyi ) [TaxId: 669 ],	SCOPe (2.08)
B	d1thtb_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Thioesterases	Myristoyl-ACP-specific thioesterase	(Vibrio harveyi ) [TaxId: 669 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Thioesterases	8020176	4000718	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	alpha/beta-Hydrolases	8032556	3000102	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	alpha/beta-Hydrolases	8032556	3000102	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	PF02273	e1thtA1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF02273	ECOD (1.6)
B	PF02273	e1thtB1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF02273	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
B	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02273	Acyl transferase (Acyl_transf_2)	Acyl transferase	This bacterial family of Acyl transferases (or myristoyl-acp-specific thioesterases) catalyse the first step in the bioluminescent fatty acid reductase system.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	THIOESTERASE	acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity	bioluminescence cellular metabolic process metabolic process cellular process fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process organic acid metabolic process organic substance metabolic process cellular lipid metabolic process small molecule metabolic process monocarboxylic acid metabolic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR003157	Acyl transferase, LuxD	Family
A, B	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	myristoyl-ACP-specific thioesterase M-CSA #728	Myristoyl acyl carrier protein specific thioesterase (C14ACP-TE) is a lux-specific acyltransferase belonging to the alpha/beta hydrolase family. The acyl transferase is part of the fatty acid reductase system required for aldehyde biosynthesis. It produces fatty acids for the light-emitting reaction catalysed by luciferase in luminescent bacteria. In Vibrio harveyi, C14ACP-TE is responsible for catalysing the transfer or hydrolysis of acyl group from either myristoyl-ACP or myristoyl-CoA to form myristic acid, and for diverting the myristic acid to the bioluminescence pathway, where it undergoes NADPH-dependent reduction and subsequent FMNH2- and O2-dependent oxidation of the corresponding aldehyde, with accompanying emission of light.	Defined by 3 residues: SER:A-114ASP:A-211HIS:A-241 \| 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.