REDX1_CATRO
ID REDX1_CATRO Reviewed; 354 AA.
AC A0A2P1GIW4;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Protein REDOX 1 {ECO:0000303|PubMed:29511102};
DE EC=1.14.14.- {ECO:0000269|PubMed:29511102};
DE AltName: Full=Cinnamyl alcohol dehydrogenase 4;
GN Name=Redox1 {ECO:0000303|PubMed:29511102}; Synonyms=CAD4;
GN ORFNames=Caros018180 {ECO:0000305};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RX PubMed=29511102; DOI=10.1073/pnas.1719979115;
RA Qu Y., Easson M.E.A.M., Simionescu R., Hajicek J., Thamm A.M.K., Salim V.,
RA De Luca V.;
RT "Solution of the multistep pathway for assembly of corynanthean, strychnos,
RT iboga, and aspidosperma monoterpenoid indole alkaloids from 19E-
RT geissoschizine.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:3180-3185(2018).
RN [2]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Little Delicata;
RX PubMed=30256480; DOI=10.1111/tpj.14111;
RA Qu Y., Safonova O., De Luca V.;
RT "Completion of the canonical pathway for assembly of anticancer drugs
RT vincristine/vinblastine in Catharanthus roseus.";
RL Plant J. 97:257-266(2019).
CC -!- FUNCTION: Component of iboga and aspidosperma monoterpenoid indole
CC alkaloids (MIAs, e.g. tabersonine and catharanthine) biosynthesis
CC pathway from 19E-geissoschizine. Catalyzes the first oxidation step of
CC the unstable intermediate product resulting from the reaction triggered
CC by the geissoschizine oxidase (GO) in the stemmadenine biosynthesis
CC process from 19E-geissoschizine. {ECO:0000269|PubMed:29511102,
CC ECO:0000269|PubMed:30256480}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15alpha-stemmadenine intermediate I + H2O + NADPH = (16S)-
CC deshydroxymethyl-stemmadenine + formate + NADP(+);
CC Xref=Rhea:RHEA:58524, ChEBI:CHEBI:15377, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142668,
CC ChEBI:CHEBI:142671; Evidence={ECO:0000269|PubMed:29511102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58525;
CC Evidence={ECO:0000269|PubMed:29511102};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15alpha-stemmadenine intermediate I + H2O + NADPH = (16R)-
CC deshydroxymethyl-stemmadenine + formate + NADP(+);
CC Xref=Rhea:RHEA:58528, ChEBI:CHEBI:15377, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142668,
CC ChEBI:CHEBI:142670; Evidence={ECO:0000269|PubMed:29511102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58529;
CC Evidence={ECO:0000269|PubMed:29511102};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15alpha-stemmadenine intermediate II + NADP(+) = 15alpha-
CC stemmadenine intermediate I + NADPH; Xref=Rhea:RHEA:58560,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142667,
CC ChEBI:CHEBI:142668; Evidence={ECO:0000269|PubMed:29511102};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58562;
CC Evidence={ECO:0000269|PubMed:29511102};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P07327};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P07327};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29511102}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf epidermis.
CC {ECO:0000269|PubMed:30256480}.
CC -!- DISRUPTION PHENOTYPE: Reduced accumulation of catharanthine and
CC vindoline, but accumulation of akuammicine and short-lived MIA.
CC {ECO:0000269|PubMed:29511102}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=ORCAE database;
CC URL="https://bioinformatics.psb.ugent.be/orcae/overview/Catro";
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; MF770509; AVM85917.1; -; mRNA.
DR AlphaFoldDB; A0A2P1GIW4; -.
DR SMR; A0A2P1GIW4; -.
DR BioCyc; MetaCyc:MON-20646; -.
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; Oxidoreductase; Zinc.
FT CHAIN 1..354
FT /note="Protein REDOX 1"
FT /id="PRO_0000446420"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 45..49
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 185..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 271..273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 295..297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 340
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
SQ SEQUENCE 354 AA; 38236 MW; 5CCA92D3631BFBC1 CRC64;
MADRVKTVGW AAHDSSGFLS PFQFTRRATG EEDVRLKVLY CGVCHSDLHN IKNEMGFTSY
PCVPGHEVVG EVTEVGNKVK KFIIGDKVGV GLFVDSCGEC EQCVNDVETY CPKLKMAYLS
IDDDGTVIQG GYSKEMVIKE RYVFRWPENL PLPAGTPLLG AGSTVYSPMK YYGLDKSGQH
LGVVGLGGLG HLAVKFAKAF GLKVTVISTS PSKKDEAINH LGADAFLVST DQEQTQKAMS
TMDGIIDTVS APHALMPLFS LLKPNGKLIV VGAPNKPVEL DILFLVMGRK MLGTSAVGGV
KETQEMIDFA AKHGIVADVE VVEMENVNNA MERLAKGDVR YRFVLDIGNA TVAV
