ID CADH_EUCBO STANDARD; PRT; 355 AA. AC P50746; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE CINNAMYL ALCOHOL DEHYDROGENASE (EC 1.1.1.195) (CAD). GN CAD1. OS Eucalyptus botryoides. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC euphyllophytes; Spermatophyta; Magnoliophyta; eudicotyledons; OC core eudicots; Rosidae; eurosids II; Myrtales; Myrtaceae; Eucalyptus. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=CALLUS; RX MEDLINE; 94159802. RA HIBINO T., CHEN J.-Q., SHIBATA D., HIGUCHI T.; RT "Nucleotide sequence of a Eucalyptus botryoides gene encoding RT cinnamyl alcohol dehydrogenase."; RL Plant Physiol. 104:305-306(1994). CC -!- FUNCTION: THIS PROTEIN CATALYZES THE FINAL STEP IN A BRANCH OF CC PHENYLPROPANOID SYNTHESIS SPECIFIC FOR PRODUCTION OF LIGNIN CC MONOMERS. IT ACTS ON CONIFERYL-, SINAPYL-, 4-COUMARYL- AND CC CINNAMYL-ALCOHOL. CC -!- CATALYTIC ACTIVITY: CINNAMYL ALCOHOL + NADP(+) = CINNAMALDEHYDE CC + NADPH. CC -!- PATHWAY: LIGNIN SYNTHESIS. CC -!- SIMILARITY: BELONGS TO THE ZINC-CONTAINING ALCOHOL DEHYDROGENASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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. DR PFAM; PF00107; adh_zinc; 1. DR PROSITE; PS00059; ADH_ZINC; 1. KW Oxidoreductase; NADP; Zinc; Lignin biosynthesis. FT METAL 47 47 ZINC (CATALYTIC) (BY SIMILARITY). FT METAL 69 69 ZINC (CATALYTIC) (BY SIMILARITY). FT METAL 100 100 ZINC (SECOND ATOM) (BY SIMILARITY). FT METAL 103 103 ZINC (SECOND ATOM) (BY SIMILARITY). FT METAL 106 106 ZINC (SECOND ATOM) (BY SIMILARITY). FT METAL 114 114 ZINC (SECOND ATOM) (BY SIMILARITY). FT METAL 162 162 ZINC (CATALYTIC) (BY SIMILARITY). SQ SEQUENCE 355 AA; 38679 MW; 521A8030 CRC32; 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 //