T3R_CATRO
ID T3R_CATRO Reviewed; 356 AA.
AC A0A161CAI1; A0A0H3WJF8;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=16-methoxy-2,3-dihydro-3-hydroxytabersonine synthase {ECO:0000303|Ref.1};
DE EC=1.1.99.41 {ECO:0000269|PubMed:25918424};
DE AltName: Full=3-hydroxy-1,2-didehydro-2,3-dihydrotabersonine reductase {ECO:0000305};
DE AltName: Full=Alcohol dehydrogenase-like protein 1 {ECO:0000303|PubMed:25918424};
DE Short=ADHL1 {ECO:0000303|PubMed:25918424};
DE AltName: Full=Tabersonine 3-reductase {ECO:0000303|PubMed:25918424};
GN Name=T3R {ECO:0000303|PubMed:25918424};
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058 {ECO:0000312|EMBL:AKV60044.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Foureau E., Kellner F., Duge de Bernonville T., Brown S., Clastre M.,
RA Lanoue A., Papon N., O'Connor S., Courdavault V.;
RT "Characterization of 16-methoxy-2,3-dihydro-3-hydroxytabersonine
RT synthase.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-356, FUNCTION, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RX PubMed=25918424; DOI=10.1073/pnas.1501821112;
RA Qu Y., Easson M.L., Froese J., Simionescu R., Hudlicky T., De Luca V.;
RT "Completion of the seven-step pathway from tabersonine to the anticancer
RT drug precursor vindoline and its assembly in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:6224-6229(2015).
RN [3]
RP INDUCTION BY HERBIVORY.
RX PubMed=28094274; DOI=10.1038/srep40453;
RA Duge de Bernonville T., Carqueijeiro I., Lanoue A., Lafontaine F.,
RA Sanchez Bel P., Liesecke F., Musset K., Oudin A., Glevarec G., Pichon O.,
RA Besseau S., Clastre M., St-Pierre B., Flors V., Maury S., Huguet E.,
RA O'Connor S.E., Courdavault V.;
RT "Folivory elicits a strong defense reaction in Catharanthus roseus:
RT metabolomic and transcriptomic analyses reveal distinct local and systemic
RT responses.";
RL Sci. Rep. 7:40453-40453(2017).
CC -!- FUNCTION: Converts the unstable imine alcohols produced by
CC CYP71D1V2/T3O into 3-hydroxy-16-methoxy-2,3-dihydrotabersonine or 3-
CC hydroxy-2,3-dihydrotabersonine. {ECO:0000269|PubMed:25918424}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + A = (3R)-
CC 1,2-didehydro-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + AH2;
CC Xref=Rhea:RHEA:52484, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:58485, ChEBI:CHEBI:136640; EC=1.1.99.41;
CC Evidence={ECO:0000269|PubMed:25918424};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxy-2,3-dihydrotabersonine + A = (3R)-1,2-
CC didehydro-3-hydroxy-2,3-dihydrotabersonine + AH2;
CC Xref=Rhea:RHEA:55388, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:138461, ChEBI:CHEBI:138462; EC=1.1.99.41;
CC Evidence={ECO:0000269|PubMed:25918424};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P06525};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P06525};
CC -!- PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis.
CC -!- TISSUE SPECIFICITY: Expressed in leaf epidermis.
CC {ECO:0000269|PubMed:25918424}.
CC -!- INDUCTION: Up-regulated by herbivory. {ECO:0000269|PubMed:28094274}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AKM12281.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KR063270; AKV60044.1; -; mRNA.
DR EMBL; KP122966; AKM12281.1; ALT_INIT; mRNA.
DR AlphaFoldDB; A0A161CAI1; -.
DR SMR; A0A161CAI1; -.
DR KEGG; ag:AKM12281; -.
DR BRENDA; 1.1.99.41; 1211.
DR UniPathway; UPA00365; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009820; P:alkaloid metabolic 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; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; Metal-binding; NAD; Nucleotide-binding;
KW Oxidoreductase; Zinc.
FT CHAIN 1..356
FT /note="16-methoxy-2,3-dihydro-3-hydroxytabersonine
FT synthase"
FT /id="PRO_0000439950"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 187..192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT CONFLICT 13
FT /note="F -> L (in Ref. 2; AKM12281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 38566 MW; 6D5E0CD69AA3EA38 CRC64;
MSSEMAAKSV KAFGLALKDS SGLFSPFNFS RRATGEHDVQ LKVLYCGVCN FDNLMRRNKY
GRTKFPYVFG HEIVGVVTEV GSNVKKFKIG NKVGVSFIVD TCRECERCKI GQQIACKKAV
SSDGFFETPG YGGCSNIFVA DENYVILWPE NLPMDSGAPL LCIGITCYNP LRRFGLDKPG
VRVGIVGLGA VGHLAIKFAK AFGARVTLIS SSPGKKDEAF QKFGVDSFLV SSNAEEMQAA
AETLDGILDT VPVVHPLEPL FALLKPLGKL IIIGEPHKPF EVSAMSLMEG GKIISASTGG
SIKDTQEIVD FAAEHNVVAD VEVIPVDYVN TAMERLDKAD VKYRFVIDIG NTFKSP
