ADH2_TANCI
ID ADH2_TANCI Reviewed; 379 AA.
AC A0A2I7G3B3;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Alcohol dehydrogenase 2 {ECO:0000303|PubMed:29122986};
DE Short=TcADH2 {ECO:0000303|PubMed:29122986};
DE EC=1.1.1.144 {ECO:0000269|PubMed:29122986};
DE EC=1.1.1.347 {ECO:0000269|PubMed:29122986};
DE AltName: Full=Trans-chrysanthemal synthase {ECO:0000305};
DE EC=1.1.1.- {ECO:0000269|PubMed:29122986};
GN Name=ADH2 {ECO:0000303|PubMed:29122986};
OS Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum
OS cinerariifolium).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Anthemidinae; Tanacetum.
OX NCBI_TaxID=118510;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=29122986; DOI=10.1104/pp.17.01330;
RA Xu H., Moghe G.D., Wiegert-Rininger K., Schilmiller A.L., Barry C.S.,
RA Last R.L., Pichersky E.;
RT "Coexpression analysis identifies two oxidoreductases involved in the
RT biosynthesis of the monoterpene acid moiety of natural pyrethrin
RT insecticides in Tanacetum cinerariifolium.";
RL Plant Physiol. 176:524-537(2018).
RN [2]
RP REVIEW.
RX PubMed=15964038; DOI=10.1016/j.phytochem.2005.05.005;
RA Matsuda K., Kikuta Y., Haba A., Nakayama K., Katsuda Y., Hatanaka A.,
RA Komai K.;
RT "Biosynthesis of pyrethrin I in seedlings of Chrysanthemum
RT cinerariaefolium.";
RL Phytochemistry 66:1529-1535(2005).
RN [3]
RP REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Component of the monoterpenoid pyrethrins biosynthesis;
CC pyrethrins are widely used plant-derived pesticide (PubMed:30468448).
CC Mediates the conversion of trans-chrysanthemol into trans-chrysanthemal
CC (PubMed:29122986). {ECO:0000269|PubMed:29122986,
CC ECO:0000303|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R,R)-chrysanthemol + NAD(+) = (1R,3R)-chrysanthemal + H(+) +
CC NADH; Xref=Rhea:RHEA:60668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:143898, ChEBI:CHEBI:143899;
CC Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60669;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + nerol = H(+) + NADH + neral; Xref=Rhea:RHEA:60672,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29020, ChEBI:CHEBI:29452,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60673;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-(-)-citronellol + NAD(+) = (S)-(-)-citronellal + H(+) +
CC NADH; Xref=Rhea:RHEA:60676, ChEBI:CHEBI:88, ChEBI:CHEBI:368,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60677;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + perillyl alcohol = H(+) + NADH + perillyl aldehyde;
CC Xref=Rhea:RHEA:10664, ChEBI:CHEBI:15378, ChEBI:CHEBI:15420,
CC ChEBI:CHEBI:15421, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.144; Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10665;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6E)-8-hydroxygeraniol + NAD(+) = (6E)-8-hydroxygeranial +
CC H(+) + NADH; Xref=Rhea:RHEA:58848, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64235,
CC ChEBI:CHEBI:64238; Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58849;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geraniol + NAD(+) = (2E)-geranial + H(+) + NADH;
CC Xref=Rhea:RHEA:34347, ChEBI:CHEBI:15378, ChEBI:CHEBI:16980,
CC ChEBI:CHEBI:17447, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.347; Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34348;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P40394};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P40394};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=236 uM for trans-chrysanthemol {ECO:0000269|PubMed:29122986};
CC KM=193 uM for NAD(+) {ECO:0000269|PubMed:29122986};
CC Note=kcat is 0.75 sec(-1) with trans-chrysanthemol as substrate (in
CC the presence of NAD(+)) (PubMed:29122986). kcat is 0.64 sec(-1) with
CC NAD(+) as substrate (in the presence of trans-chrysanthemol)
CC (PubMed:29122986). {ECO:0000269|PubMed:29122986};
CC -!- PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:29122986}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P40394}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and disk florets.
CC {ECO:0000269|PubMed:29122986}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-IV subfamily. {ECO:0000305}.
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DR EMBL; MF497444; AUQ44118.1; -; mRNA.
DR AlphaFoldDB; A0A2I7G3B3; -.
DR SMR; A0A2I7G3B3; -.
DR BioCyc; MetaCyc:MON-20952; -.
DR GO; GO:0018457; F:perillyl-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Isoprene biosynthesis; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..379
FT /note="Alcohol dehydrogenase 2"
FT /id="PRO_0000447847"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 49..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 203..208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 275..277
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 298..300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 321..323
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
SQ SEQUENCE 379 AA; 41397 MW; 9AC6589BB4227E9E CRC64;
MSLNTPDVII CKAAVVRELG RSVMVEEIKV DPPKATEVRI KMLFASICHT DMLCFDGFPT
PLFPRIPGHE GVGMVESVGE DIKTKLKPGD IVMPLFMGEC GQCLNCKSKR TNLCHAYPLT
LSGLLLDGTS RMSIAKTEET IYHHLSCSTW SEYMVIDINY VLKIDPKMHL PYASFLSCGF
TTGFGAPWKE TQITKGSIVA VFGLGAVGLG AIKGAQMQGA SIIIGVDINE NKAAKGKAFG
MTHFINPKDH PNQLVSDMVR DITDGLGVDY CFECTGIASL LKEIIEASKI GFGTTILIGA
APDNVPISSL SLINGRTLKG TTFGGVRTRS DLPIILQKCM NEEIELDELM SHEIRLENIH
EIFEILKKPD CVKILINFD
