LUXD_ALIF1
ID LUXD_ALIF1 Reviewed; 307 AA.
AC Q5DZ04;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
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}; OrderedLocusNames=VF_A0922;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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. {ECO:0000255|HAMAP-Rule:MF_00774}.
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}.
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DR EMBL; CP000021; AAW87992.1; -; Genomic_DNA.
DR RefSeq; WP_011263742.1; NC_006841.2.
DR RefSeq; YP_206880.1; NC_006841.2.
DR AlphaFoldDB; Q5DZ04; -.
DR SMR; Q5DZ04; -.
DR STRING; 312309.VF_A0922; -.
DR ESTHER; vibf1-q5dz04; Thioesterase_acyl-transferase.
DR EnsemblBacteria; AAW87992; AAW87992; VF_A0922.
DR KEGG; vfi:VF_A0922; -.
DR PATRIC; fig|312309.11.peg.3524; -.
DR eggNOG; COG1073; Bacteria.
DR HOGENOM; CLU_882365_0_0_6; -.
DR OMA; FARRMDH; -.
DR OrthoDB; 631878at2; -.
DR UniPathway; UPA00569; -.
DR Proteomes; UP000000537; Chromosome II.
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 3: Inferred from homology;
KW Acyltransferase; Luminescence; Reference proteome; Transferase.
FT CHAIN 1..307
FT /note="Acyl transferase"
FT /id="PRO_1000046810"
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"
SQ SEQUENCE 307 AA; 34198 MW; 0CDBC0A1B6F7E6B0 CRC64;
MKDESSFFTI DHIIELENGQ SIRVWETPPK SDTHKKNSTI VIAAGFARRM DHFAGLAEYL
SSNGFRVIRY DSLHHVGLSS GQIDEFSMSI GKHSLLIVVG WLRAKGIQNL GIIAASLSAR
IAYEVINDID ASFLITAVGV VNLQDTLEKA LKYDYLRLPI DELPDDLDFE GHNLGSKVFV
TDCLKNEWDT LGSTFKAVQG LNIPFIAFTA NGDSWVNQSD VEKMIDNIDT TQCKLYSLIG
SSHDLGENLV VLRNFYESVT RAAVALDKGS LDLDIEIVEP GFEDLTSTTV KERRLRNKIE
NELLELA
