LUXD_VIBHA
ID LUXD_VIBHA Reviewed; 305 AA.
AC P05521; P11002;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Acyl transferase;
DE Short=ACT;
DE EC=2.3.1.-;
DE AltName: Full=C14ACP-TE;
DE AltName: Full=Myristoyl-ACP-specific thioesterase;
GN Name=luxD;
OS Vibrio harveyi (Beneckea harveyi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=669;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3417663; DOI=10.1016/s0021-9258(18)37717-2;
RA Miyamoto C., Boylan M., Graham A.F., Meighen E.A.;
RT "Organization of the lux structural genes of Vibrio harveyi. Expression
RT under the T7 bacteriophage promoter, mRNA analysis, and nucleotide sequence
RT of the luxD gene.";
RL J. Biol. Chem. 263:13393-13399(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 83-305.
RX PubMed=3997817; DOI=10.1016/s0021-9258(18)88948-7;
RA Cohn D.H., Mileham A.J., Simon M.I., Nealson K.H., Rausch S.K., Bonam D.,
RA Baldwin T.O.;
RT "Nucleotide sequence of the luxA gene of Vibrio harveyi and the complete
RT amino acid sequence of the alpha subunit of bacterial luciferase.";
RL J. Biol. Chem. 260:6139-6146(1985).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=8068614; DOI=10.1021/bi00198a003;
RA Lawson D.M., Derewenda U., Serre L., Ferri S., Szittner R., Wei Y.,
RA Meighen E.A., Derewenda Z.S.;
RT "Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi.";
RL Biochemistry 33:9382-9388(1994).
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 -!- SIMILARITY: Belongs to the LuxD family. {ECO:0000305}.
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DR EMBL; J03950; AAA27535.1; -; Genomic_DNA.
DR EMBL; M10961; AAA88684.1; -; Genomic_DNA.
DR PIR; A28947; A28947.
DR RefSeq; WP_069687703.1; NZ_CP009468.1.
DR PDB; 1THT; X-ray; 2.10 A; A/B=1-305.
DR PDBsum; 1THT; -.
DR AlphaFoldDB; P05521; -.
DR SMR; P05521; -.
DR ESTHER; vibha-1luxd; Thioesterase_acyl-transferase.
DR PRIDE; P05521; -.
DR GeneID; 57823104; -.
DR PATRIC; fig|669.65.peg.3628; -.
DR UniPathway; UPA00569; -.
DR EvolutionaryTrace; P05521; -.
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 3D-structure; Acyltransferase; Luminescence; Transferase.
FT CHAIN 1..305
FT /note="Acyl transferase"
FT /id="PRO_0000220195"
FT ACT_SITE 114
FT /note="Charge relay system"
FT ACT_SITE 211
FT /note="Charge relay system"
FT ACT_SITE 241
FT /note="Charge relay system"
FT VARIANT 75
FT /note="G -> E (in mutant M17)"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:1THT"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1THT"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:1THT"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1THT"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:1THT"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:1THT"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1THT"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1THT"
FT HELIX 86..102
FT /evidence="ECO:0007829|PDB:1THT"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1THT"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:1THT"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1THT"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:1THT"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:1THT"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1THT"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1THT"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:1THT"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1THT"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:1THT"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:1THT"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:1THT"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:1THT"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:1THT"
FT HELIX 247..265
FT /evidence="ECO:0007829|PDB:1THT"
FT HELIX 280..296
FT /evidence="ECO:0007829|PDB:1THT"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1THT"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1THT"
SQ SEQUENCE 305 AA; 34207 MW; 316B694A0E864AD9 CRC64;
MNNQCKTIAH VLRVNNGQEL HVWETPPKEN VPFKNNTILI ASGFARRMDH FAGLAEYLSE
NGFHVFRYDS LHHVGLSSGS IDEFTMTTGK NSLCTVYHWL QTKGTQNIGL IAASLSARVA
YEVISDLELS FLITAVGVVN LRDTLEKALG FDYLSLPIDE LPNDLDFEGH KLGSEVFVRD
CFEHHWDTLD STLDKVANTS VPLIAFTANN DDWVKQEEVY DMLAHIRTGH CKLYSLLGSS
HDLGENLVVL RNFYQSVTKA AIAMDGGSLE IDVDFIEPDF EQLTIATVNE RRLKAEIESR
TPEMA
