CYADH_CATRO
ID CYADH_CATRO Reviewed; 376 AA.
AC A0A0C5DM37;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=CYP enzymes assisting alcohol dehydrogenase {ECO:0000305|PubMed:25675512};
DE Short=CrCYPADH {ECO:0000303|PubMed:25675512};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:P06525};
DE AltName: Full=Alcohol dehydrogenase 2 {ECO:0000303|PubMed:25675512};
GN Name=CYPADH {ECO:0000303|PubMed:25675512};
GN Synonyms=ADH2 {ECO:0000303|PubMed:25675512};
GN ORFNames=Caros007480 {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, PATHWAY, AND BIOTECHNOLOGY.
RX PubMed=25675512; DOI=10.1073/pnas.1423555112;
RA Brown S., Clastre M., Courdavault V., O'Connor S.E.;
RT "De novo production of the plant-derived alkaloid strictosidine in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:3205-3210(2015).
CC -!- FUNCTION: May be a positive catalyzer of strictosidine production by
CC assisting secologanin biosynthesis, thus being involved in monoterpene
CC indole alkaloids accumulation. {ECO:0000269|PubMed:25675512}.
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:25675512}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06525}.
CC -!- BIOTECHNOLOGY: Promotes strictosidine production by assisting
CC secologanin biosynthesis when expressed in a S.cerevisiae host
CC optimized for the biosynthesis of monoterpene indole alkaloids.
CC {ECO:0000269|PubMed:25675512}.
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; KP411012; AJO70764.1; -; mRNA.
DR AlphaFoldDB; A0A0C5DM37; -.
DR SMR; A0A0C5DM37; -.
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; IDA: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 Alkaloid metabolism; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..376
FT /note="CYP enzymes assisting alcohol dehydrogenase"
FT /id="PRO_0000446417"
FT BINDING 43
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 45
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 45
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 64
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 64
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 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 173
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 199..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 294..296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 371
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
SQ SEQUENCE 376 AA; 40654 MW; B2D576722F141DCD CRC64;
MQIITCKAVV CWAAGEPPVV EEILVEPPRS GEVRIKILFA SLCHTDVLAC KGFPTPMFPR
VLGHEGVGVV ECVGEGVSEL REGDVVIPTY LGECGECENC ESGRTNLCRT YPLQAFTGLM
PDGSSRMSSA KGGEMLYQFL SCSTWSEYTV IDANYAVKID SRIPLPHASF LSCGFTTGFG
ATWKEAKLQE GSSTVAVLGL GAVGLGAVEG ARVQGVTQII GIDINDNKRE KGEAFGMTHF
INPKKDNNKS ISELVKELTK GQGVDVCFEC TGVPDLVNEA LESTKIGTGN MIMLGAGTQK
SMTINFVSLL GCRTFKYSVF GGVKVQSDLP LIIQKCLNKE IQKIEQLLTH QVQLEDINRA
FELLKEPDCV KVLITL
