Family: Thioesterase_acyl-transferase

Block: X

Parent Family: No family


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


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


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

Structure Name Proteins
1THT Vibrio harveyi Myristoyl-ACP-specific thioesterase vibha-1luxd

Gene_locus Name Species
9bact-d8pbw6 Candidatus Nitrospira defluvii Putative uncharacterized protein Candidatus Nitrospira defluvii
9bact-d8pdl3 Candidatus Nitrospira defluvii Putative uncharacterized protein Candidatus Nitrospira defluvii
9delt-a6g1j0 Plesiocystis pacifica SIR-1 LuxD. acyl transferase Plesiocystis pacifica SIR-1
9gamm-q4a538 Vibrio salmonicida Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238)) luxd Vibrio salmonicida
corad-d5ene2 Coraliomargarita akajimensis (strain DSM 45221 \/ IAM 15411 \/ JCM 2319 \/ KCTC 12865) Methyltransferase type 11 Coraliomargarita akajimensis
phole-lxd1 Photobacterium leiognathi subsp. leiognathi Photobacterium mondopomensis Photobacterium damselae thioesterase (c14acp-te) Photobacterium leiognathi
phole-lxd2 Photobacterium leiognathi Photobacterium mondopomensis thioesterase (c14acp-te) Photobacterium leiognathi
pholu-LUXD2 Photorhabdus luminescens (Xenorhabdus luminescens) and (subsp. laumondii) acyl transferase Photorhabdus luminescens
pholu-lxd1 Photorhabdus luminescens (Xenorhabdus luminescens) thioesterase Photorhabdus luminescens
pholu-lxd2 Photorhabdus luminescens (Xenorhabdus luminescens), Photorhabdus asymbiotica, thioesterase (c14acp-te) Photorhabdus luminescens
phopo-luxd Photobacterium phosphoreum Photobacterium kishitanii, thioesterase Photobacterium phosphoreum
sheha-LUXD Shewanella hanedai (Alteromonas hanedai) myristoryl-acp thioesterase (c14acp-te) Shewanella hanedai
shewm-luxd Shewanella woodyi (and strain ATCC 51908 \/ MS32) Myristoyl-ACP-specific thioesterase Shewanella woodyi
vibcl-q5ek34 Vibrio cholerae (strains bv. albensis\; VL426\; RC385) Vibrio sp. RC586 putative acyltransferase (fragment) luxD Vibrio cholerae
vibf1-q5dz04 Vibrio fischeri (strain ATCC 700601 \/ ES114) luxd. acyl transferase (EC 2.3.1.-) Vibrio fischeri
vibfi-LUXD Vibrio fischeri (and strain MJ11) acyl-transferase luxd (c14acp-te) Vibrio fischeri
vibha-1luxd Vibrio harveyi, Vibrio orientalis, Vibrio vulnificus, Vibrio chagasii myristoyl-ACP-specific thioesterase acyl transferase (luxD) gene Vibrio harveyi

Substrate Chemical Nomenclature Proteins
Myristoyl-ACP Myristoyl-Acyl-carrier protein

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
Abstract :
PubMedSearch : Caswell_2021_Protein.Sci__
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
Abstract :
PubMedSearch : Cantu_2011_Nucleic.Acids.Res_39_D342
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
Abstract :
PubMedSearch : Cantu_2010_Protein.Sci_19_1281
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
Abstract :
PubMedSearch : Lawson_1994_Biochemistry_33_9382
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
Abstract :
PubMedSearch : Chao_1993_Gene_126_155
PubMedID: 8472957
Gene_locus related to this paper: phole-lxd2