ID CADH2_TOBAC Reviewed; 357 AA.
AC P30360;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Probable cinnamyl alcohol dehydrogenase 2;
DE Short=CAD 2;
DE EC=1.1.1.195 {ECO:0000250|UniProtKB:O49482};
GN Name=CAD19;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Samsun; TISSUE=Stem;
RX PubMed=1643282; DOI=10.1007/bf00027075;
RA Knight M.E., Halpin C., Schuch W.;
RT "Identification and characterisation of cDNA clones encoding cinnamyl
RT alcohol dehydrogenase from tobacco.";
RL Plant Mol. Biol. 19:793-801(1992).
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; 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 -!- INDUCTION: By fungal elicitor.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X62344; CAA44217.1; -; mRNA.
DR PIR; S23526; S23526.
DR RefSeq; NP_001312913.1; NM_001325984.1.
DR AlphaFoldDB; P30360; -.
DR SMR; P30360; -.
DR STRING; 4097.P30360; -.
DR PaxDb; 4097-P30360; -.
DR GeneID; 107816761; -.
DR KEGG; nta:107816761; -.
DR OrthoDB; 1550at2759; -.
DR UniPathway; UPA00711; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 Direct protein sequencing; Lignin biosynthesis; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..357
FT /note="Probable cinnamyl alcohol dehydrogenase 2"
FT /id="PRO_0000160806"
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"
SQ SEQUENCE 357 AA; 38761 MW; D481B10B4DCB8F4E CRC64;
MGSLDVEKSA IGWAARDPSG LLSPYTYTLR NTGPEDVQVK VLYCGLCHSD LHQVKNDLGM
SNYPLVPGHE VVGKVVEVGA DVSKFKVGDT VGVGLLVGSC RNCGPCKREI EQYCNKKIWN
CNDVYTDGKP TQGGFANSMV VDQNFVVKIP EGMAPEQAAP LLCAGITVYS PFNHFGFNQS
GFRGGILGLG GVGHMGVKIA KAMGHHVTVI SSSNKKRQEA LEHLGADDYL VSSDTDKMQE
AADSLDYIID TVPVGHPLEL YLSLLKIDGK LILIGVINTP LQFISPMVML GRKSITGSFI
GSMKETEEML DFCKEKGVTS QIEIVKMDYI NTAMERLEKN DVSYRFVVDV AGSKLDQ
//
