LUXD1_PHOLU
ID LUXD1_PHOLU Reviewed; 307 AA.
AC P19197; Q48732; Q56818;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Acyl transferase {ECO:0000255|HAMAP-Rule:MF_00774};
DE Short=ACT {ECO:0000255|HAMAP-Rule:MF_00774};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_00774};
DE AltName: Full=C14ACP-TE {ECO:0000255|HAMAP-Rule:MF_00774};
DE AltName: Full=Myristoyl-ACP-specific thioesterase {ECO:0000255|HAMAP-Rule:MF_00774};
GN Name=luxD {ECO:0000255|HAMAP-Rule:MF_00774};
OS Photorhabdus luminescens (Xenorhabdus luminescens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=29488;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hm;
RX PubMed=2216747; DOI=10.1093/nar/18.18.5570;
RA Cochrum L., Hruska K.S., Rucker E.B., Johnston T.C.;
RT "The nucleotide sequence of the luxD gene of Xenorhabdus luminescens Hm.";
RL Nucleic Acids Res. 18:5570-5570(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29999 / DSM 3368 / BCRC 14801 / CIP 106429 / NCIMB 12670 / Hb;
RX PubMed=1644764; DOI=10.1128/jb.174.16.5371-5381.1992;
RA Meighen E.A., Szittner R.B.;
RT "Multiple repetitive elements and organization of the lux operons of
RT luminescent terrestrial bacteria.";
RL J. Bacteriol. 174:5371-5381(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 232-307.
RC STRAIN=ATCC 29999 / DSM 3368 / BCRC 14801 / CIP 106429 / NCIMB 12670 / Hb;
RX PubMed=2204626; DOI=10.1016/s0021-9258(17)46262-4;
RA Szittner R., Meighen E.;
RT "Nucleotide sequence, expression, and properties of luciferase coded by lux
RT genes from a terrestrial bacterium.";
RL J. Biol. Chem. 265:16581-16587(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 262-307.
RX PubMed=2383248; DOI=10.1016/0006-291x(90)92106-a;
RA Johnston T.C., Rucker E.B., Cochrum L., Hruska K.S., Vandegrift V.;
RT "The nucleotide sequence of the luxA and luxB genes of Xenorhabdus
RT luminescens HM and a comparison of the amino acid sequences of luciferases
RT from four species of bioluminescent bacteria.";
RL Biochem. Biophys. Res. Commun. 170:407-415(1990).
RN [5]
RP MUTAGENESIS OF SER-79.
RX PubMed=2071574; DOI=10.1016/s0021-9258(18)98772-7;
RA Ferri S.R., Meighen E.A.;
RT "A lux-specific myristoyl transferase in luminescent bacteria related to
RT eukaryotic serine esterases.";
RL J. Biol. Chem. 266:12852-12857(1991).
CC -!- FUNCTION: Acyl transferase is part of the fatty acid reductase system
CC required for aldehyde biosynthesis; it produces fatty acids for the
CC luminescent reaction.
CC -!- PATHWAY: Lipid metabolism; fatty acid reduction for biolumincescence.
CC {ECO:0000255|HAMAP-Rule:MF_00774}.
CC -!- SIMILARITY: Belongs to the LuxD family. {ECO:0000255|HAMAP-
CC Rule:MF_00774}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X53783; CAA37799.1; -; Genomic_DNA.
DR EMBL; M90093; AAA27618.1; -; Genomic_DNA.
DR EMBL; M57416; AAA27622.1; -; Genomic_DNA.
DR EMBL; M55977; AAA27625.1; -; Genomic_DNA.
DR PIR; S11686; S11686.
DR AlphaFoldDB; P19197; -.
DR SMR; P19197; -.
DR STRING; 29488.KS18_21615; -.
DR ESTHER; pholu-lxd1; Thioesterase_acyl-transferase.
DR UniPathway; UPA00569; -.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProtKB-UniRule.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-UniRule.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00774; LuxD; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003157; LuxD.
DR Pfam; PF02273; Acyl_transf_2; 1.
DR PIRSF; PIRSF009416; LuxD; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Luminescence; Transferase.
FT CHAIN 1..307
FT /note="Acyl transferase"
FT /id="PRO_0000220190"
FT ACT_SITE 116
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00774"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00774"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00774"
FT MUTAGEN 79
FT /note="S->T,A,G: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2071574"
FT CONFLICT 140
FT /note="F -> V (in Ref. 2; AAA27618)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="N -> D (in Ref. 2; AAA27618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 34700 MW; 99D904AAB1DEDC3F CRC64;
MENESKYKTI DHVICVEGNK KIHVWETLPE ENSPKRKNAI IIASGFARRM DHFAGLAEYL
SRNGFHVIRY DSLHHVGLSS GTIDEFTMSI GKQSLLAVVD WLTTRKINNF GMLASSLSAR
IAYASLSEIN ASFLITAVGF VNLRYSLERA LGFDYLSLPI NELPNNLDFE GHKLGAEVFA
RDCLDFGWED LASTINNMMY LDIPFIAFTA NNDNWVKQDE VITLLSNIRS NRCKIYSLLG
SSHDLSENLV VLRNFYQSVT KAAIAMDNDH LDIDVDITEP SFEHLTIATV NERRMRIEIE
NQAISLS