Thioesterase_acyl-transferase

Relationship

Family: Thioesterase_acyl-transferase

Block: X

Parent Family: No family

Comment

This bacterial family of Acyl transferases (ACT or myristoyl-acp-specific thioesterases) catalyses the first step in the bioluminescent fatty acid reductase system, which is required for aldehyde biosynthesis. This enzyme belongs to the LuxD family. Together with acyl-protein synthetase (LuxE) and reductase (LuxC), it belongs to a multienzyme complex. This complex channels activated fatty acids into the aldehyde substrate for the luciferase-catalyzed bacterial bioluminescence reaction. The C-terminal region of LuxD interacts with LuxE to causes a conformational change. LuxD has a calculated M(r) of 34,384 and comprises 305 aa residues. Induction of luminescence only occurs at high cell density. Some bacteria have N-acylhomoserine lactone autoinducers for luminescence. Warning: the serine 77 in GXSXG motif is not the active site serine 114 as determined by X ray structure AASLS in Vibrio harveyi see Lawson et al., 2003. Family TE19 in ThYme database

Database

Interpro : IPR003157 Acyl transferase, LuxD

PIRSF : PIRSF009416 lux-specific fatty acid reductase, acyl-ACP thioesterase subunit

Pdoc : No Pdoc

Pfam : PF02273 Acyl_transf_2

Prints : No Print

EC Number : No EC Number

Sequences

Peptide in Fasta
Nucleotide in Fasta
Alignment with Multalin Text only
Seed alignment with MAFFT No colour
Alignment with MAFFT No colour
Dendrogram The dnd file

Structures (1)

Genes Proteins in Thioesterase_acyl-transferase family (17)

No fragment of genes

Structures in Thioesterase_acyl-transferase family (1)

Substrates in Thioesterase_acyl-transferase family (1)

No Inhibitor

References (5)

Title : Thioesterase enzyme families: Functions, structures, and mechanisms - Caswell_2021_Protein.Sci__
Author(s) : Caswell BT , de Carvalho CC , Nguyen H , Roy M , Nguyen T , Cantu DC
Ref : Protein Science , : , 2021
PubMedID: 34921469

Title : ThYme: a database for thioester-active enzymes - Cantu_2011_Nucleic.Acids.Res_39_D342
Author(s) : Cantu DC , Chen Y , Lemons ML , Reilly PJ
Ref : Nucleic Acids Research , 39 :D342 , 2011
PubMedID: 21045059

Title : Thioesterases: a new perspective based on their primary and tertiary structures. - Cantu_2010_Protein.Sci_19_1281
Author(s) : Cantu DC , Chen Y , Reilly PJ
Ref : Protein Science , 19 :1281 , 2010
PubMedID: 20506386

Title : Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi - Lawson_1994_Biochemistry_33_9382
Author(s) : Lawson DM , Derewenda U , Serre L , Ferri S , Szittner R , Wei Y , Meighen EA , Derewenda ZS
Ref : Biochemistry , 33 :9382 , 1994
PubMedID: 8068614
Gene_locus related to this paper: pholu-lxd1 , phopo-luxd , vibha-1luxd

Title : Sequence of the luxD gene encoding acyltransferase of the lux operon from Photobacterium leiognathi - Chao_1993_Gene_126_155
Author(s) : Chao YF , Weng SF , Lin JW
Ref : Gene , 126 :155 , 1993
PubMedID: 8472957
Gene_locus related to this paper: phole-lxd2