DPAS_CATRO
ID DPAS_CATRO Reviewed; 365 AA.
AC A0A1B1FHP3;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Dehydroprecondylocarpine acetate synthase {ECO:0000303|PubMed:29724909};
DE EC=1.1.1.- {ECO:0000269|PubMed:29724909};
GN Name=DPAS {ECO:0000303|PubMed:29724909};
GN ORFNames=Caros004542 {ECO:0000305}, Cr033537 {ECO:0000312|EMBL:ANQ45231.1};
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].
RC STRAIN=cv. Little Bright Eyes;
RA Stavrinides A.K., O'Connor S.E., Tatsis E.C., Caputi L., Foureau E.,
RA Stevenson C.E.M., Lawson D.M., Courdavault V.;
RT "The structural basis of ajmalicine biosynthesis: Active site elements that
RT control stereoselectivity in alkaloids.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR
RP LOCATION, HOMODIMERIZATION, AND INTERACTION WITH CS AND TS.
RC STRAIN=cv. Little Bright Eyes;
RX PubMed=29724909; DOI=10.1126/science.aat4100;
RA Caputi L., Franke J., Farrow S.C., Chung K., Payne R.M.E., Nguyen T.-D.,
RA Dang T.-T.T., Soares Teto Carqueijeiro I., Koudounas K.,
RA Duge de Bernonville T., Ameyaw B., Jones D.M., Vieira I.J.C.,
RA Courdavault V., O'Connor S.E.;
RT "Missing enzymes in the biosynthesis of the anticancer drug vinblastine in
RT Madagascar periwinkle.";
RL Science 360:1235-1239(2018).
CC -!- FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid
CC indole alkaloids (MIAs, e.g. vinblastine, catharanthine, tabersonine,
CC vincadifformine, vindoline, vincristine, quinine and strychnine)
CC biosynthesis pathway. Converts precondylocarpine acetate to
CC dihydroprecondylocarpine acetate. {ECO:0000269|PubMed:29724909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroprecondylocarpine acetate + NADP(+) = H(+) + NADPH +
CC precondylocarpine acetate; Xref=Rhea:RHEA:58576, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142769,
CC ChEBI:CHEBI:142770; Evidence={ECO:0000269|PubMed:29724909};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58578;
CC Evidence={ECO:0000269|PubMed:29724909};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00327};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P00327};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29724909}.
CC -!- SUBUNIT: Homodimer. Interaction with catharanthine synthase (CS) and
CC tabersonine synthase (TS). {ECO:0000269|PubMed:29724909}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29724909}.
CC -!- DISRUPTION PHENOTYPE: Strong accumulation of precondylocarpine acetate.
CC {ECO:0000269|PubMed:29724909}.
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";
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DR EMBL; KU865331; ANQ45231.1; -; mRNA.
DR AlphaFoldDB; A0A1B1FHP3; -.
DR SMR; A0A1B1FHP3; -.
DR BioCyc; MetaCyc:MON-20638; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0009821; P:alkaloid biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
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.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; Cytoplasm; Glycoprotein; Metal-binding; NAD;
KW Oxidoreductase; Zinc.
FT CHAIN 1..365
FT /note="Dehydroprecondylocarpine acetate synthase"
FT /id="PRO_0000446421"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 54
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 54
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 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 193..198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 279..281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 365 AA; 38948 MW; A41E5F11E0626BB5 CRC64;
MAGKSAEEEH PIKAYGWAVK DRTTGILSPF KFSRRATGDD DVRIKILYCG ICHTDLASIK
NEYEFLSYPL VPGMEIVGIA TEVGKDVTKV KVGEKVALSA YLGCCGKCYS CVNELENYCP
EVIIGYGTPY HDGTICYGGL SNETVANQSF VLRFPERLSP AGGAPLLSAG ITSFSAMRNS
GIDKPGLHVG VVGLGGLGHL AVKFAKAFGL KVTVISTTPS KKDDAINGLG ADGFLLSRDD
EQMKAAIGTL DAIIDTLAVV HPIAPLLDLL RSQGKFLLLG APSQSLELPP IPLLSGGKSI
IGSAAGNVKQ TQEMLDFAAE HDITANVEII PIEYINTAME RLDKGDVRYR FVVDIENTLT
PPSEL
