AFS1_MALDO
ID AFS1_MALDO Reviewed; 576 AA.
AC Q84LB2; Q2VU74; Q2VU78; Q2VU82; Q2VU83; Q32WH6; Q32WH8; Q32WI0; Q32WI2;
AC Q6Q2J2; Q6QWJ1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=(E,E)-alpha-farnesene synthase;
DE Short=MdASF1;
DE EC=4.2.3.46;
DE AltName: Full=Prenyltransferase;
DE EC=2.5.1.-;
GN Name=AFS1; Synonyms=AFAR;
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND INDUCTION BY 1-MCP.
RC STRAIN=cv. Law Rome; TISSUE=Peelings;
RX PubMed=14740213; DOI=10.1007/s00425-003-1191-4;
RA Pechous S.W., Whitaker B.D.;
RT "Cloning and functional expression of an (E, E)-alpha-farnesene synthase
RT cDNA from peel tissue of apple fruit.";
RL Planta 219:84-94(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Idared; TISSUE=Peelings;
RA Pechous S.W., Watkins C.B., Whitaker B.D.;
RT "Expression of a-farnesene synthase gene AFS1 in relation to levels of a-
RT farnesene and conjugated trienols in peel tissue of scald-susceptible 'Law
RT Rome' and scald-resistant 'Idared' apple fruit.";
RL Postharvest Biol. Technol. 35:125-132(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF ASP-326 AND
RP ASP-330.
RC STRAIN=cv. Aotea, cv. Pinkie, and cv. Royal Gala;
RX PubMed=17140613; DOI=10.1016/j.phytochem.2006.10.017;
RA Green S., Friel E.N., Matich A., Beuning L.L., Cooney J.M., Rowan D.D.,
RA MacRae E.;
RT "Unusual features of a recombinant apple alpha-farnesene synthase.";
RL Phytochemistry 68:176-188(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Ralls; TISSUE=Leaf;
RA Yuan K.J., Liu Q.Z., Li B., Zhang L.S.;
RT "Genomic structure and sequence polymorphism of E,E-alpha-farnesene
RT synthase gene in apples (Malus domestica Borkh.).";
RL Yuan Yi Xue Bao 34:1003-1006(2007).
RN [5]
RP POTASSIUM-BINDING, AND MUTAGENESIS OF ASP-484; SER-485; SER-487 AND
RP SER-488.
RX PubMed=19181671; DOI=10.1074/jbc.m807140200;
RA Green S., Squire C.J., Nieuwenhuizen N.J., Baker E.N., Laing W.;
RT "Defining the potassium binding region in an apple terpene synthase.";
RL J. Biol. Chem. 284:8661-8669(2009).
CC -!- FUNCTION: Sesquiterpene synthase catalyzing the production of (E,E)-
CC alpha-farnesene, the predominant terpene produced during storage of
CC fruits. Produces all six isomers (E,E)-alpha-farnesene, (Z,E)-alpha-
CC farnesene, (E,Z)-alpha-farnesene, (Z,Z)-alpha-farnesene, (E)-beta-
CC farnesene and (Z)-beta-farnesene from a mix of isomeric forms of the
CC farnesyl diphosphate precursor. Able to convert geranyl diphosphate to
CC the monoterpenes (E)-beta-ocimene, linalool and beta-myrcene. Has also
CC a prenyltransferase activity producing alpha-farnesene directly from
CC geranyl diphosphate and isoprenyl diphosphate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-farnesene +
CC diphosphate; Xref=Rhea:RHEA:27421, ChEBI:CHEBI:10280,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.46;
CC Evidence={ECO:0000269|PubMed:14740213, ECO:0000269|PubMed:17140613};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17140613};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17140613};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:17140613};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for farnesyl diphosphate {ECO:0000269|PubMed:17140613};
CC Note=activity enhanced 5-fold on addition of 30-50 mM potassium.;
CC pH dependence:
CC Optimum pH is 7.0-8.5. {ECO:0000269|PubMed:17140613};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17140613}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by ethylene. Inhibited by 1-methylcyclopropene
CC (1-MCP). {ECO:0000269|PubMed:14740213}.
CC -!- MISCELLANEOUS: The activity enhancement by potassium is associated only
CC with sesquiterpene synthase activity and not monoterpene or
CC prenyltransferase activities.
CC -!- MISCELLANEOUS: Oxidation products of (E,E)-alpha-farnesene are the
CC causal agents of superficial scald.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; AY182241; AAO22848.2; -; mRNA.
DR EMBL; AY523409; AAS01424.1; -; mRNA.
DR EMBL; AY563622; AAS68019.1; -; mRNA.
DR EMBL; AY787633; AAX19772.1; -; mRNA.
DR EMBL; AY787634; AAX19773.1; -; mRNA.
DR EMBL; AY787635; AAX19774.1; -; mRNA.
DR EMBL; AY787636; AAX19775.1; -; mRNA.
DR EMBL; AY787638; AAX19777.1; -; mRNA.
DR EMBL; AY787639; AAX19778.1; -; mRNA.
DR EMBL; AY787640; AAX19779.1; -; mRNA.
DR EMBL; AY787641; AAX19780.1; -; mRNA.
DR EMBL; AY805408; AAX21241.1; -; Genomic_DNA.
DR EMBL; AY805409; AAX21242.1; -; Genomic_DNA.
DR EMBL; AY805410; AAX21243.1; -; Genomic_DNA.
DR EMBL; AY805413; AAX21246.1; -; Genomic_DNA.
DR EMBL; AY805414; AAX21247.1; -; Genomic_DNA.
DR EMBL; AY805415; AAX21248.1; -; Genomic_DNA.
DR EMBL; AY805416; AAX21249.1; -; Genomic_DNA.
DR EMBL; AY805417; AAX21250.1; -; Genomic_DNA.
DR EMBL; AY805418; AAX21251.1; -; Genomic_DNA.
DR EMBL; AY805419; AAX21252.1; -; Genomic_DNA.
DR EMBL; DQ901739; ABJ90485.1; -; Genomic_DNA.
DR RefSeq; NP_001280822.1; NM_001293893.1.
DR AlphaFoldDB; Q84LB2; -.
DR SMR; Q84LB2; -.
DR STRING; 3750.XP_008383949.1; -.
DR GeneID; 103446592; -.
DR KEGG; mdm:103446592; -.
DR OrthoDB; 401091at2759; -.
DR BioCyc; MetaCyc:MON-13546; -.
DR BRENDA; 4.2.3.46; 3164.
DR SABIO-RK; Q84LB2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052578; F:alpha-farnesene synthase activity; IEA:RHEA.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Potassium;
KW Transferase.
FT CHAIN 1..576
FT /note="(E,E)-alpha-farnesene synthase"
FT /id="PRO_0000401483"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81192"
FT BINDING 484
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000305"
FT BINDING 487
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT VARIANT 105
FT /note="E -> K (in strain: cv. Idared)"
FT VARIANT 113
FT /note="I -> V (in strain: cv. Aotea)"
FT VARIANT 129
FT /note="G -> A (in strain: cv. Aotea)"
FT VARIANT 130
FT /note="T -> A (in strain: cv. Idared)"
FT VARIANT 237
FT /note="N -> D (in strain: cv. Aotea)"
FT VARIANT 281
FT /note="I -> F (in strain: cv. Idared, cv. Pinkie, cv. Ralls
FT and cv. Royal Gala)"
FT VARIANT 291
FT /note="R -> G (in strain: cv. Idared)"
FT VARIANT 297
FT /note="A -> S (in strain: cv. cv. Idared, cv. Pinkie, cv.
FT Ralls and cv. Royal Gala)"
FT VARIANT 381
FT /note="E -> Q (in strain: cv. Aotea)"
FT VARIANT 451
FT /note="D -> G (in strain: cv. Ralls)"
FT VARIANT 505
FT /note="K -> E (in strain: cv. Aotea)"
FT VARIANT 530
FT /note="F -> S (in strain: cv. Aotea)"
FT VARIANT 565
FT /note="H -> Q (in strain: cv. Aotea)"
FT MUTAGEN 326
FT /note="D->A: Loss of monoterpene synthase, sesquiterpene
FT synthase and prenyltransferase activities. Loss of
FT monoterpene synthase, sesquiterpene synthase and
FT prenyltransferase activities; when associated with A-330."
FT /evidence="ECO:0000269|PubMed:17140613"
FT MUTAGEN 330
FT /note="D->A: Loss of monoterpene synthase, sesquiterpene
FT synthase and prenyltransferase activities; when associated
FT with A-326."
FT /evidence="ECO:0000269|PubMed:17140613"
FT MUTAGEN 484
FT /note="D->A: No effect on sesquiterpene synthase activity,
FT but loss of activity enhancement by potassium."
FT /evidence="ECO:0000269|PubMed:19181671"
FT MUTAGEN 485
FT /note="S->A: No effect on sesquiterpene synthase activity
FT and on activity enhancement by potassium, but 2-fold
FT increase in monoterpene synthase activity."
FT /evidence="ECO:0000269|PubMed:19181671"
FT MUTAGEN 487
FT /note="S->A: Loss of sesquiterpene synthase activity."
FT /evidence="ECO:0000269|PubMed:19181671"
FT MUTAGEN 487
FT /note="S->K: 4-fold higher sesquiterpene synthase activity
FT in absence of potassium, and loss of activity enhancement
FT by potassium."
FT /evidence="ECO:0000269|PubMed:19181671"
FT MUTAGEN 488
FT /note="S->A: Decreased mono- and sesquiterpene synthase
FT activity, but no effect on activity enhancement by
FT potassium."
FT /evidence="ECO:0000269|PubMed:19181671"
FT CONFLICT 150
FT /note="G -> S (in Ref. 3; AAX21242)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="F -> L (in Ref. 3; AAX21251)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="N -> S (in Ref. 3; AAX21251)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 66183 MW; 4FABCBE4B43B3465 CRC64;
MEFRVHLQAD NEQKIFQNQM KPEPEASYLI NQRRSANYKP NIWKNDFLDQ SLISKYDGDE
YRKLSEKLIE EVKIYISAET MDLVAKLELI DSVRKLGLAN LFEKEIKEAL DSIAAIESDN
LGTRDDLYGT ALHFKILRQH GYKVSQDIFG RFMDEKGTLE NHHFAHLKGM LELFEASNLG
FEGEDILDEA KASLTLALRD SGHICYPDSN LSRDVVHSLE LPSHRRVQWF DVKWQINAYE
KDICRVNATL LELAKLNFNV VQAQLQKNLR EASRWWANLG IADNLKFARD RLVECFACAV
GVAFEPEHSS FRICLTKVIN LVLIIDDVYD IYGSEEELKH FTNAVDRWDS RETEQLPECM
KMCFQVLYNT TCEIAREIEE ENGWNQVLPQ LTKVWADFCK ALLVEAEWYN KSHIPTLEEY
LRNGCISSSV SVLLVHSFFS ITHEGTKEMA DFLHKNEDLL YNISLIVRLN NDLGTSAAEQ
ERGDSPSSIV CYMREVNASE ETARKNIKGM IDNAWKKVNG KCFTTNQVPF LSSFMNNATN
MARVAHSLYK DGDGFGDQEK GPRTHILSLL FQPLVN
