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 31-JUL-2019, entry version 91. 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; OC Pentapetalae; rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; OC 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 CC step specific for the production of lignin monomers. Catalyzes the CC NADPH-dependent reduction of coniferaldehyde, 5- CC hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and CC caffeyl aldehyde to their respective alcohols. CC {ECO:0000250|UniProtKB:O49482}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + CC H(+) + NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16731, ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; 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. CC {ECO:0000250|UniProtKB:O49482}; CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid CC 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 Probable cinnamyl alcohol dehydrogenase. FT /FTId=PRO_0000160792. FT NP_BIND 187 192 NADP. {ECO:0000250|UniProtKB:O49482}. FT NP_BIND 210 215 NADP. {ECO:0000250|UniProtKB:O49482}. FT NP_BIND 297 299 NADP. {ECO:0000250|UniProtKB:O49482}. FT METAL 47 47 Zinc 1; catalytic. FT {ECO:0000250|UniProtKB:O49482}. FT METAL 69 69 Zinc 1; catalytic. FT {ECO:0000250|UniProtKB:O49482}. FT METAL 70 70 Zinc 1; catalytic. FT {ECO:0000250|UniProtKB:O49482}. FT METAL 100 100 Zinc 2. {ECO:0000250|UniProtKB:O49482}. FT METAL 103 103 Zinc 2. {ECO:0000250|UniProtKB:O49482}. FT METAL 106 106 Zinc 2. {ECO:0000250|UniProtKB:O49482}. FT METAL 114 114 Zinc 2. {ECO:0000250|UniProtKB:O49482}. FT METAL 162 162 Zinc 1; catalytic. FT {ECO:0000250|UniProtKB:O49482}. FT BINDING 49 49 NADP. {ECO:0000250|UniProtKB:O49482}. FT BINDING 166 166 NADP. {ECO:0000250|UniProtKB:O49482}. FT BINDING 250 250 NADP. {ECO:0000250|UniProtKB:O49482}. FT BINDING 274 274 NADP; via carbonyl oxygen. FT {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 //