ADH1_TANCI
ID ADH1_TANCI Reviewed; 378 AA.
AC A0A2I7G3B2;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Alcohol dehydrogenase 1 {ECO:0000303|PubMed:29122986};
DE Short=TcADH1 {ECO:0000303|PubMed:29122986};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:A0A2I7G3B3};
GN Name=ADH1 {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], AND TISSUE SPECIFICITY.
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).
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 -!- PATHWAY: Isoprenoid biosynthesis. {ECO:0000250|UniProtKB:A0A2I7G3B3}.
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; MF497443; AUQ44117.1; -; mRNA.
DR AlphaFoldDB; A0A2I7G3B2; -.
DR SMR; A0A2I7G3B2; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
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 InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 2: Evidence at transcript level;
KW Isoprene biosynthesis; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..378
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000447848"
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 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 177
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 202..207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 231
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 274..276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 297..299
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 378 AA; 40383 MW; 888E5D24F3CF961D CRC64;
MAHKAPSVIT CKAAVVWELG GPVVLEEIKV DPPKASEVRI KMLCASICHT DVLCTKGFPI
PLFPRIPGHE GVGVIESVGI DAKGLKPGDI VMPLYLGECG QCLNCKTGKT NLCHVYPPPF
SGLMNDGTSR MTIARTGESI YHFTSCSTWT EYAVADCNYV LKIDPKISYP HASFLSCGFT
TGFGATWRET QVSKGSSVAV FGIGTVGLGV IKGAQLAGAS KIIGVDVNQY KAAKGKVFGM
TDFINPKDHP NKTVSELVKE ITHGLGVDYC FECTGVPSLL NEALEASKFG IGTVVPIGAG
GEASVAINSL ILFSGRTLKC TTFGGVRTQS DLPVIIDKCL NKEIQLDELL THEIQLENIQ
AAFEILKKPD CVKILINF
