GS_CATRO
ID GS_CATRO Reviewed; 364 AA.
AC W8JWW7;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Geissoschizine synthase {ECO:0000303|PubMed:29147812, ECO:0000303|PubMed:29511102};
DE Short=CrGS {ECO:0000303|PubMed:29147812, ECO:0000303|PubMed:29511102};
DE EC=1.3.1.36 {ECO:0000269|PubMed:29147812, ECO:0000269|PubMed:30256480};
DE AltName: Full=Alcohol dehydrogenase 14 {ECO:0000303|PubMed:24710322};
DE Short=CrADH14 {ECO:0000303|PubMed:24710322};
GN Name=GS {ECO:0000303|PubMed:29147812, ECO:0000303|PubMed:29511102};
GN Synonyms=ADH14 {ECO:0000303|PubMed:24710322};
GN ORFNames=Caros006689 {ECO:0000303|PubMed:24710322};
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Little Bright Eyes;
RX PubMed=24710322; DOI=10.1038/ncomms4606;
RA Miettinen K., Dong L., Navrot N., Schneider T., Burlat V., Pollier J.,
RA Woittiez L., van der Krol S., Lugan R., Ilc T., Verpoorte R.,
RA Oksman-Caldentey K.M., Martinoia E., Bouwmeester H., Goossens A.,
RA Memelink J., Werck-Reichhart D.;
RT "The seco-iridoid pathway from Catharanthus roseus.";
RL Nat. Commun. 5:3606-3606(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP PATHWAY.
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).
RN [4]
RP INDUCTION BY SILVER NITRATE AND METHYL JASMONATE.
RX PubMed=30340174; DOI=10.1016/j.plaphy.2018.10.015;
RA Paeizi M., Karimi F., Razavi K.;
RT "Changes in medicinal alkaloids production and expression of related
RT regulatory and biosynthetic genes in response to silver nitrate combined
RT with methyl jasmonate in Catharanthus roseus in vitro propagated shoots.";
RL Plant Physiol. Biochem. 132:623-632(2018).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=29147812; DOI=10.1007/s00425-017-2812-7;
RA Qu Y., Thamm A.M.K., Czerwinski M., Masada S., Kim K.H., Jones G.,
RA Liang P., De Luca V.;
RT "Geissoschizine synthase controls flux in the formation of monoterpenoid
RT indole alkaloids in a Catharanthus roseus mutant.";
RL Planta 247:625-634(2018).
CC -!- FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid
CC indole alkaloids (MIAs, e.g. catharanthine, tabersonine,
CC vincadifformine, vindoline, vincristine, quinine and strychnine)
CC biosynthesis pathway. Catalyzes iminium reduction on 4,21-
CC dehydrogeissoschizine to produce 19E-geissoschizine, precursor of
CC catharanthine and tabersonine derivatives (PubMed:29147812,
CC PubMed:30256480). May also catalyze the production of reactive
CC intermediate used by the HL1, HL2, HL3 and HL4 to form catharanthine,
CC vincadifformine and tabersonine (PubMed:30256480).
CC {ECO:0000269|PubMed:29147812, ECO:0000269|PubMed:30256480}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(19S)-geissoschizine + NADP(+) = 4,21-dehydrogeissoschizine +
CC NADPH; Xref=Rhea:RHEA:11376, ChEBI:CHEBI:17037, ChEBI:CHEBI:17294,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.36;
CC Evidence={ECO:0000269|PubMed:29147812, ECO:0000269|PubMed:30256480};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11378;
CC Evidence={ECO:0000269|PubMed:29147812, ECO:0000269|PubMed:30256480};
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. {ECO:0000269|PubMed:29147812,
CC ECO:0000269|PubMed:30256480}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06525}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf epidermis.
CC {ECO:0000269|PubMed:24710322, ECO:0000269|PubMed:30256480}.
CC -!- INDUCTION: Induced by methyl jasmonate (MeJA, MJ) and silver nitrate
CC (AgNO(3)). {ECO:0000269|PubMed:30340174}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of ajmalicine at the expense of
CC catharanthine and vindoline production (PubMed:29147812,
CC PubMed:30256480). Lower tabersonine-forming activity (PubMed:30256480).
CC {ECO:0000269|PubMed:29147812, ECO:0000269|PubMed:30256480}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=ORCAE database;
CC URL="https://bioinformatics.psb.ugent.be/orcae/overview/Catro";
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DR EMBL; KF302079; AHK60846.1; -; mRNA.
DR EMBL; MF770507; AVM85915.1; -; mRNA.
DR AlphaFoldDB; W8JWW7; -.
DR SMR; W8JWW7; -.
DR KEGG; ag:AHK60846; -.
DR BioCyc; MetaCyc:MON-12392; -.
DR GO; GO:0047920; F:geissoschizine dehydrogenase activity; IMP:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035834; P:indole alkaloid metabolic process; IDA:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0010272; P:response to silver ion; IEP: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 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 Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..364
FT /note="Geissoschizine synthase"
FT /id="PRO_0000446403"
FT BINDING 51
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 73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 73
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 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 168
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 193..198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 280..282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00327"
SQ SEQUENCE 364 AA; 39517 MW; F28063FB64D619A6 CRC64;
MAGETTKLDL SVKAVGWGAA DASGVLQPIK FYRRVPGERD VKIRVLYSGV CNFDMEMVRN
KWGFTRYPYV FGHETAGEVV EVGSKVEKFK VGDKVAVGCM VGSCGQCYNC QSGMENYCPE
PNMADGSVYR EQGERSYGGC SNVMVVDEKF VLRWPENLPQ DKGVALLCAG VVVYSPMKHL
GLDKPGKHIG VFGLGGLGSV AVKFIKAFGG KATVISTSRR KEKEAIEEHG ADAFVVNTDS
EQLKALAGTM DGVVDTTPGG RTPMSLMLNL LKFDGAVMLV GAPESLFELP AAPLIMGRKK
IIGSSTGGLK EYQEMLDFAA KHNIVCDTEV IGIDYLSTAM ERIKNLDVKY RFAIDIGNTL
KFEE
