CADH_PINRA
ID CADH_PINRA Reviewed; 357 AA.
AC Q40976; O81222;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Probable cinnamyl alcohol dehydrogenase;
DE Short=CAD;
DE EC=1.1.1.195;
GN Name=CAD;
OS Pinus radiata (Monterey pine) (Pinus insignis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3347;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Male cone;
RA Wagner A., Walden A., Walter C.;
RT "A cDNA encoding a cinnamyl alcohol dehydrogenase from Pinus radiata.";
RL (er) Plant Gene Register PGR96-097(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Moyle R., Wagner A., Walter C.;
RT "Nucleotide sequence of a cinnamyl alcohol dehydrogenase (CAD) gene from
RT Pinus radiata.";
RL (er) Plant Gene Register PGR98-118(1998).
CC -!- FUNCTION: Involved in lignin biosynthesis. Catalyzes the final step
CC specific for the production of lignin monomers. Catalyzes the NADPH-
CC dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde,
CC sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their
CC respective alcohols. {ECO:0000250|UniProtKB:O49482}.
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;
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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O49482}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; U62394; AAB38774.1; -; mRNA.
DR EMBL; AF060491; AAC31166.1; -; Genomic_DNA.
DR AlphaFoldDB; Q40976; -.
DR SMR; Q40976; -.
DR UniPathway; UPA00711; -.
DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
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 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 2: Evidence at transcript level;
KW Lignin biosynthesis; Metal-binding; NADP; Oxidoreductase; Zinc.
FT CHAIN 1..357
FT /note="Probable cinnamyl alcohol dehydrogenase"
FT /id="PRO_0000160801"
FT BINDING 47
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 49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 69
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 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 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 163
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 167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 188..193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 211..216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 251
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 275
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 298..300
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT CONFLICT 179
FT /note="E -> G (in Ref. 2; AAC31166)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 38924 MW; CFDB18429392D42D CRC64;
MGSLETEKTV TGYAARDSSG HLSPYTYNLR KKGPEDVIVK VIYCGICHSD LVQMRNEMGM
SHYPMVPGHE VVGIVTEIGS EVKKFKVGEH VGVGCIVGSC RSCGNCNQSM EQYCSKRIWT
YNDVNHDGTP TQGGFASSMV VDQMFVVRIP ENLPLEQAAP LLCAGVTVFS PMKHFAMTEP
GKKCGILGLG GVGHMGVKIA KAFGLHVTVI SSSDKKKEEA MEVLGADAYL VSKDTEKMME
AAESLDYIMD TIPVAHPLEP YLALLKTNGK LVMLGVVPEP LHFVTPLLIL GRRSIAGSFI
GSMEETQETL DFCAEKKVSS MIEVVGLDYI NTAMERLEKN DVRYRFVVDV AGSKLDN
