ID E9M774_HEVBR Unreviewed; 357 AA.
AC E9M774;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=cinnamyl-alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013171};
DE EC=1.1.1.195 {ECO:0000256|ARBA:ARBA00013171};
GN Name=CAD {ECO:0000313|EMBL:ADU64756.1};
OS Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC Hevea.
OX NCBI_TaxID=3981 {ECO:0000313|EMBL:ADU64756.1};
RN [1] {ECO:0000313|EMBL:ADU64757.1}
RP NUCLEOTIDE SEQUENCE.
RA Saha T., Ravindran M.;
RT "Molecular cloning and characterisation of a gene encoding cinnamyl alcohol
RT dehydrogenase (CAD) in rubber (Hevea brasiliensis).";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU64756.1}
RP NUCLEOTIDE SEQUENCE.
RA Saha T., Ravindran M., Thomas K.U.;
RT "Molecular cloning and characterisation of lignin biosynthesis genes in
RT rubber (Hevea brasiliensis).";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumaroyl alcohol + NADP(+) = (E)-4-coumaraldehyde +
CC H(+) + NADPH; Xref=Rhea:RHEA:45724, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28353, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:64555; EC=1.1.1.195;
CC Evidence={ECO:0000256|ARBA:ARBA00036200};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45726;
CC Evidence={ECO:0000256|ARBA:ARBA00036200};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) +
CC NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731,
CC ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.195; Evidence={ECO:0000256|ARBA:ARBA00036166};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10394;
CC Evidence={ECO:0000256|ARBA:ARBA00036166};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-coniferol + NADP(+) = (E)-coniferaldehyde + H(+) + NADPH;
CC Xref=Rhea:RHEA:22444, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547,
CC ChEBI:CHEBI:17745, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.195; Evidence={ECO:0000256|ARBA:ARBA00036509};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22446;
CC Evidence={ECO:0000256|ARBA:ARBA00036509};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-sinapyl alcohol + NADP(+) = (E)-sinapaldehyde + H(+) +
CC NADPH; Xref=Rhea:RHEA:45704, ChEBI:CHEBI:15378, ChEBI:CHEBI:27949,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64557;
CC EC=1.1.1.195; Evidence={ECO:0000256|ARBA:ARBA00035824};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45706;
CC Evidence={ECO:0000256|ARBA:ARBA00035824};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004928}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; HQ229952; ADU64756.1; -; mRNA.
DR EMBL; HQ229953; ADU64757.1; -; Genomic_DNA.
DR AlphaFoldDB; E9M774; -.
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 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:SF1; CINNAMYL ALCOHOL DEHYDROGENASE 5; 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 20..348
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 357 AA; 38871 MW; D0B39D57E7506F19 CRC64;
MGGLETERVV VGWAARDPSG ILSPYTYTLR NTGPEDVLLK VLSCGICHTD IHQVKNELGM
SRYPMVPGHE VVGEVVEVGS EVTNFRVGDV VGVGVIVGCC RNCNPCKSDV EQYCNKKIWS
YNDVYTDGKT TQGGFAQSMI VDQKFVVKIP DGMSAEQAAP LLCAGLTVYS PLSHFGLNKS
GQRGGILGLG GVGHMGVKIA KAMGHHVTVI SSSDKKRAEA MEHLGADEYL VSSDATRMQE
FADTLDYIID TVPAVHALEP YLSLLKLDGR LILMGVINAP LQFLTPLVML GRKSITGSFI
GSMKETEEML EFCKEKGITS MIEVVKMDYV NEALERLEKN DVRYRFVVDV AGSKLEP
//