ID CADH_MEDSA Reviewed; 358 AA.
AC P31656;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Probable cinnamyl alcohol dehydrogenase;
DE Short=CAD;
DE EC=1.1.1.195 {ECO:0000250|UniProtKB:O49482};
GN Name=CAD2;
OS Medicago sativa (Alfalfa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Apollo;
RA van Doorsselaere J., Baucher M., Feuillet C., Boudet A.M., van Montagu M.,
RA Inze D.;
RT "Isolation of cinnamyl alcohol dehydrogenase cDNAs from two important
RT economic species: alfalfa and poplar. Demonstration of a high homology of
RT the gene within angiosperms.";
RL Plant Physiol. Biochem. 33:105-109(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=cv. Siriver; TISSUE=Stem;
RX PubMed=10579494; DOI=10.1023/a:1006381630494;
RA Brill E.M., Abrahams S., Hayes C.M., Jenkins C.L., Watson J.M.;
RT "Molecular characterization and expression of a wound-inducible cDNA
RT encoding a novel cinnamyl-alcohol dehydrogenase enzyme in lucerne (Medicago
RT sativa L.).";
RL Plant Mol. Biol. 41:279-291(1999).
CC -!- FUNCTION: This protein catalyzes the final step in a branch of
CC phenylpropanoid synthesis specific for production of lignin monomers.
CC It acts on coniferyl-, sinapyl-, 4-coumaryl- and cinnamyl-alcohol.
CC {ECO:0000305|PubMed:10579494}.
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:0000250|UniProtKB:O49482};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10394;
CC Evidence={ECO:0000250|UniProtKB:O49482};
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:0000250|UniProtKB:O49482};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22446;
CC Evidence={ECO:0000250|UniProtKB:O49482};
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:0000250|UniProtKB:O49482};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45706;
CC Evidence={ECO:0000250|UniProtKB:O49482};
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:0000250|UniProtKB:O49482};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45726;
CC Evidence={ECO:0000250|UniProtKB:O49482};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-caffeyl alcohol + NADP(+) = (E)-caffeyl aldehyde + H(+) +
CC NADPH; Xref=Rhea:RHEA:45728, ChEBI:CHEBI:15378, ChEBI:CHEBI:28323,
CC ChEBI:CHEBI:31334, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:O49482};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45730;
CC Evidence={ECO:0000250|UniProtKB:O49482};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O49482};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O49482};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000250|UniProtKB:O49482}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O49482}.
CC -!- TISSUE SPECIFICITY: Most actively expressed in stem, hypocotyl and root
CC tissue.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; Z19573; CAA79625.1; -; mRNA.
DR EMBL; AF083332; AAC35845.1; -; mRNA.
DR PIR; S31572; S31572.
DR AlphaFoldDB; P31656; -.
DR SMR; P31656; -.
DR UniPathway; UPA00711; -.
DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050268; F:coniferyl-alcohol dehydrogenase activity; IEA:RHEA.
DR GO; GO:0052747; F:sinapyl alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
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 4; 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 1: Evidence at protein level;
KW Lignin biosynthesis; Metal-binding; NADP; Oxidoreductase; Zinc.
FT CHAIN 1..358
FT /note="Probable cinnamyl alcohol dehydrogenase"
FT /id="PRO_0000160798"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 189..194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 212..217
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 252
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 276
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 299..301
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
SQ SEQUENCE 358 AA; 38948 MW; FBA609408D01BF56 CRC64;
MGSIEAAERT TVGLAAKDPS GILTPYTYTL RNTGPDDVYI KIHYCGVCHS DLHQIKNDLG
MSNYPMVPGH EVVGEVLEVG SNVTRFKVGE IVGVGLLVGC CKSCRACDSE IEQYCNKKIW
SYNDVYTDGK ITQGGFAEST VVEQKFVVKI PEGLAPEQVA PLLCAGVTVY SPLSHFGLKT
PGLRGGILGL GGVGHMGVKV AKALGHHVTV ISSSDKKKKE ALEDLGADNY LVSSDTVGMQ
EAADSLDYII DTVPVGHPLE PYLSLLKIDG KLILMGVINT PLQFVTPMVM LGRKSITGSF
VGSVKETEEM LEFWKEKGLT SMIEIVTMDY INKAFERLEK NDVRYRFVVD VKGSKFEE
//
