ID CADH_EUCBO Reviewed; 355 AA. AC P50746; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 03-AUG-2022, entry version 94. DE RecName: Full=Probable cinnamyl alcohol dehydrogenase; DE Short=CAD; DE EC=1.1.1.195; GN Name=CAD1; OS Eucalyptus botryoides (Southern mahogany) (Eucalyptus saligna subsp. OS botryoides). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus. OX NCBI_TaxID=33130; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Callus; RX PubMed=7906894; DOI=10.1104/pp.104.1.305; RA Hibino T., Chen J.-Q., Shibata D., Higuchi T.; RT "Nucleotide sequence of a Eucalyptus botryoides gene encoding cinnamyl RT alcohol dehydrogenase."; RL Plant Physiol. 104:305-306(1994). 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}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA04046.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D16624; BAA04046.1; ALT_SEQ; Genomic_DNA. DR AlphaFoldDB; P50746; -. DR SMR; P50746; -. 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 3: Inferred from homology; KW Lignin biosynthesis; Metal-binding; NADP; Oxidoreductase; Zinc. FT CHAIN 1..355 FT /note="Probable cinnamyl alcohol dehydrogenase" FT /id="PRO_0000160792" 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 162 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 166 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O49482" FT BINDING 187..192 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O49482" FT BINDING 210..215 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O49482" FT BINDING 250 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O49482" FT BINDING 274 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O49482" FT BINDING 297..299 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O49482" SQ SEQUENCE 355 AA; 38679 MW; 8F1D067A409D629A CRC64; MGSLEKERTT TGWAARDPSG VLSPYTYSLR NTGPEDLYIK VLSCGICHSD IHQIKNDLGM SHYPMVPGHE VVGEVLEVGS EVTKYRVGDR VGTGIVVGCC RSCGPCNSDQ EQYCNKKIWN YNDVYTDGKP TQGGFAGEIV VGQRFVVKIP DGLESEQDAV MCAGVTVYSP LVRFGLKQSG LRGGILGLGG VGHMGVKIAK AMGHHVTVIS SSDKKRTEAL EHLGADAYLV SSDENGMKEA TDSLDYIFDT IPVVHPLEPY LALLKLDGKL ILTGVINAPL QFISPMVMLG RKSITGSFIG SMKETEEMLE FCKEKGLTSQ IEVIKMDYVN TALERLEKND VRYRFVVDVA GSKLD //