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 11-DEC-2019, entry version 92. 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 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_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 NP_BIND 187..192 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:O49482" FT NP_BIND 210..215 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:O49482" FT NP_BIND 297..299 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 47 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 69 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 70 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 100 FT /note="Zinc 2" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 103 FT /note="Zinc 2" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 106 FT /note="Zinc 2" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 114 FT /note="Zinc 2" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 162 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000250|UniProtKB:O49482" FT BINDING 49 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:O49482" FT BINDING 166 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:O49482" FT BINDING 250 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:O49482" FT BINDING 274 FT /note="NADP; via carbonyl oxygen" 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 //