REDX2_CATRO
ID REDX2_CATRO Reviewed; 323 AA.
AC A0A2P1GIY9;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Protein REDOX 2 {ECO:0000303|PubMed:29511102};
DE EC=1.7.1.- {ECO:0000269|PubMed:29511102};
GN Name=Redox2 {ECO:0000303|PubMed:29511102};
GN ORFNames=Caros002920 {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 second 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 -!- CATALYTIC ACTIVITY:
CC Reaction=15alpha-stemmadenine + NADP(+) = 15alpha-stemmadenine
CC intermediate II + 2 H(+) + NADPH; Xref=Rhea:RHEA:58564,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:142667, ChEBI:CHEBI:142674;
CC Evidence={ECO:0000269|PubMed:29511102};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58566;
CC Evidence={ECO:0000269|PubMed:29511102};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29511102}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P46336}.
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 16S- and 16R-
CC deshydroxymethylstemmadenine (16S/16R-DHS) and, to some extent, of
CC akuammicine. {ECO:0000269|PubMed:29511102}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=ORCAE database;
CC URL="https://bioinformatics.psb.ugent.be/orcae/overview/Catro";
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DR EMBL; MF770510; AVM85918.1; -; mRNA.
DR AlphaFoldDB; A0A2P1GIY9; -.
DR SMR; A0A2P1GIY9; -.
DR BioCyc; MetaCyc:MON-20647; -.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd19124; AKR_AKR4A_4B; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044497; AKR4A/B.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; NADP; Oxidoreductase.
FT CHAIN 1..323
FT /note="Protein REDOX 2"
FT /id="PRO_0000446426"
FT REGION 302..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 58
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 167..168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 215..220
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P46336"
FT BINDING 289..297
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT SITE 88
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:P46336"
SQ SEQUENCE 323 AA; 36501 MW; 084818C5625D74F7 CRC64;
MEKQVEIPEV ELNSGHKMPI VGYGTCVPEP MPPLEELTAI FLDAIKVGYR HFDTASSYGT
EEALGKAIAE AINSGLVKSR EEFFISCKLW IEDADHDLIL PALNQSLQIL GVDYLDLYMI
HMPVRVRKGA PMFNYSKEDF LPFDIQGTWK AMEECSKQGL AKSIGVSNYS VEKLTKLLET
STIPPAVNQV EMNVAWQQRK LLPFCKEKNI HITSWSPLLS YGVAWGSNAV MENPVLQQIA
ASKGKTVAQV ALRWIYEQGA SLITRTSNKD RMFENVQIFD WELSKEELDQ IHEIPQRRGT
LGEEFMHPEG PIKSPEELWD GDL
