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Database: UniProt
Entry: G8CUP5_CATRO
LinkDB: G8CUP5_CATRO
Original site: G8CUP5_CATRO 
ID   G8CUP5_CATRO            Unreviewed;       361 AA.
AC   G8CUP5;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=CAD2 protein {ECO:0000313|EMBL:AYE56097.1};
DE   SubName: Full=Cr2141 {ECO:0000313|EMBL:AEO99200.1};
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 {ECO:0000313|EMBL:AEO99200.1};
RN   [1] {ECO:0000313|EMBL:AEO99200.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Usera A.R., Yerkes N.M., Liscombe D.K., Nims N.E., O'Connor S.E.;
RT   "Chemoenzymatic Synthesis of a Photo-Affinity Probe for Enzyme
RT   Identification in Plants.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AYE56097.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30256480;
RA   Qu Y., Safonova O., 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; HQ380174; AEO99200.1; -; mRNA.
DR   EMBL; MH194346; AYE56097.1; -; mRNA.
DR   AlphaFoldDB; G8CUP5; -.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   CDD; cd05283; CAD1; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF65; CINNAMYL ALCOHOL DEHYDROGENASE 8; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          24..352
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   361 AA;  38411 MW;  67FEBBA810A2F72E CRC64;
     MAGKSPEEEH PVKTYGLAAH DSSGVLSPFK FSRRATLEDD VRFKVLYCGI CHTDLHFAKN
     EWGISTYPLV PGHEIVGEVT EVGGKVTKVK VGDKVGVGCL VGSCRTCDNC RADLENYCPK
     MVLTYASPNV DGTITYGGYS NEMVCNEHFI VRFPENLPLD GGAPLLCAGI TVYSPMKYYG
     FAKPGSHIAV NGLGGLGHVA VKFAKAMGAK VTVISTSEGK KDDALNRLGA DAFLLSSNPE
     ALQAATGTFD GILNTISAKH AIIPLLGLLK SHGKLVLLGA PPEPLDLHSA PLLMGRKMVA
     GSSIGGLKET QEMLDFAGKH NITADIELIS ADNINTALER LAKGDVRYRF VLDVAKTLKA
     P
//
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