ID CAD4_ARATH STANDARD; PRT; 365 AA. AC P48523; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE CINNAMYL-ALCOHOL DEHYDROGENASE 2 (EC 1.1.1.195) (CAD). GN CAD. OS ARABIDOPSIS THALIANA (MOUSE-EAR CRESS). OC EUKARYOTA; VIRIDIPLANTAE; STREPTOPHYTA; EMBRYOPHYTA; TRACHEOPHYTA; OC EUPHYLLOPHYTES; SPERMATOPHYTA; MAGNOLIOPHYTA; EUDICOTYLEDONS; ROSIDAE; OC CAPPARALES; BRASSICACEAE; ARABIDOPSIS. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 95175612. RA BAUCHER M., VAN DOORSSELAERE J., GIELEN J., INZE D., RA VAN MONTAGU M., BOERJAN W.; RT "Genomic nucleotide sequence of an Arabidopsis thaliana gene encoding RT a cinnamyl alcohol dehydrogenase."; RL PLANT PHYSIOL. 107:285-286(1995). 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. COULD PLAY A ROLE IN PLANT DEFENSE. 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; Z31715; G757535; -. DR PROSITE; PS00059; ADH_ZINC; 1. DR PFAM; PF00107; adh_zinc; 1. DR HSSP; P01308; 1MHI. KW OXIDOREDUCTASE; NADP; ZINC; LIGNIN BIOSYNTHESIS; MULTIGENE FAMILY. FT METAL 48 48 ZINC (CATALYTIC) (BY SIMILARITY). FT METAL 70 70 ZINC (CATALYTIC) (BY SIMILARITY). FT METAL 101 101 ZINC (SECOND ATOM) (BY SIMILARITY). FT METAL 104 104 ZINC (SECOND ATOM) (BY SIMILARITY). FT METAL 107 107 ZINC (SECOND ATOM) (BY SIMILARITY). FT METAL 115 115 ZINC (SECOND ATOM) (BY SIMILARITY). FT METAL 164 164 ZINC (CATALYTIC) (BY SIMILARITY). SQ SEQUENCE 365 AA; 39098 MW; 6C644F2F CRC32; MGSVEAGEKK ALGWAARDPS GVLSPYSYTL RSTGADDVYI KVICCGICHT DIHQIKNDLG MSNYPMVPGH EVVGEVLEVG SDVSKFTVGD VVGVGVVVGC CGSCKPCSSE LEQYCNKRIW SYNDVYTDGK PTQGGFADTM IVNQKFVVKI PEGMAVEQAA PLLCAGVTVY SPLSHFGLMA SGLKGGILGL GGVGHMGVKI AKAMGHHVTV ISSSDKKKEE AIEHLGADDY VVSSDPAEMQ RLADSLDYII DTVPVFHPLD PYLACLKLDG KLILMGVINT PLQFVTPLVI LGRKVISGSF IGSIKETEEV LAFCKEKGLT STIETVKIDE LNIAFERLRK NDVRYRFVVD VAGSNLVEEA ATTTN //