WAXS1_SIMCH
ID WAXS1_SIMCH Reviewed; 352 AA.
AC Q9XGY6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Long-chain-alcohol O-fatty-acyltransferase;
DE EC=2.3.1.75;
DE AltName: Full=Wax synthase;
OS Simmondsia chinensis (Jojoba) (Buxus chinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Simmondsiaceae; Simmondsia.
OX NCBI_TaxID=3999;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10712527; DOI=10.1104/pp.122.3.645;
RA Lardizabal K.D., Metz J.G., Sakamoto T., Hutton W.C., Pollard M.R.,
RA Lassner M.W.;
RT "Purification of a jojoba embryo wax synthase, cloning of its cDNA, and
RT production of high levels of wax in seeds of transgenic arabidopsis.";
RL Plant Physiol. 122:645-655(2000).
CC -!- FUNCTION: Catalyzes the final step in the synthesis of long-chain
CC linear esters (waxes). Has activity with both saturated and
CC monounsaturated acyl-CoA ranging from 14 to 24 carbons in length, but
CC C20:1 acyl-CoA is the preferred substrate.
CC {ECO:0000269|PubMed:10712527}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + a long chain fatty alcohol = a wax ester +
CC CoA; Xref=Rhea:RHEA:38443, ChEBI:CHEBI:10036, ChEBI:CHEBI:17135,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=2.3.1.75;
CC Evidence={ECO:0000269|PubMed:10712527};
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:10712527};
CC Multi-pass membrane protein {ECO:0000269|PubMed:10712527}.
CC -!- SIMILARITY: Belongs to the wax synthase family. {ECO:0000305}.
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DR EMBL; AF149919; AAD38041.1; -; mRNA.
DR PIR; T48903; T48903.
DR AlphaFoldDB; Q9XGY6; -.
DR BioCyc; MetaCyc:MON-13890; -.
DR BRENDA; 2.3.1.75; 5733.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102966; F:arachidoyl-CoA:1-dodecanol O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047196; F:long-chain-alcohol O-fatty-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR044851; Wax_synthase.
DR InterPro; IPR032805; Wax_synthase_dom.
DR InterPro; IPR017088; Wax_synthase_Magnoliopsida.
DR PANTHER; PTHR31595; PTHR31595; 1.
DR Pfam; PF13813; MBOAT_2; 1.
DR PIRSF; PIRSF037006; Wax_synthase; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Microsome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..352
FT /note="Long-chain-alcohol O-fatty-acyltransferase"
FT /id="PRO_0000380676"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 352 AA; 40157 MW; F91D6BD896003629 CRC64;
MEVEKELKTF SEVWISAIAA ACYCRFVPAV APHGGALRLL LLLPVVLLFI FLPLRLSSFH
LGGPTALYLV WLANFKLLLF AFHLGPLSNP SLSLLHFIST TLLPIKFRDD PSNDHEKNKR
TLSFEWRKVV LFVAKLVFFA GILKIYEFRK DLPHFVISVL YCFHFYLGTE ITLAASAVIA
RATLGLDLYP QFNEPYLATS LQDFWGRRWN LMVSDILGLT TYQPVRRVLS RWVRLRWEVA
GAMLVAFTVS GLMHEVFFFY LTRARPSWEV TGFFVLHGVC TAVEMVVKKA VSGKVRLRRE
VSGALTVGFV MVTGGWLFLP QLVRHGVDLK TIDEYPVMFN YTQKKLMGLL GW
