ID CADH1_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-FEB-2005 (Rel. 46, Last annotation update) DE Cinnamyl-alcohol dehydrogenase (EC 1.1.1.195) (CAD). GN Name=CAD; OrderedLocusNames=At3g19450; ORFNames=MLD14.19; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=95175612; PubMed=7870825; DOI=10.1104/pp.107.1.285; RA Baucher M., van Doorsselaere J., Gielen J., Inze D., van Montagu M., RA Boerjan W.; RT "Genomic nucleotide sequence of an Arabidopsis thaliana gene encoding RT a cinnamyl alcohol dehydrogenase."; RL Plant Physiol. 107:285-286(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20277480; PubMed=10819329; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). 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 -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity). CC -!- PATHWAY: Lignin biosynthesis. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. 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; CAA83508.1; -. DR EMBL; AB025624; BAB02470.1; -. DR EMBL; AF370261; AAK44076.1; -. DR EMBL; AY063076; AAL34250.1; -. DR InterPro; IPR002328; ADH_zinc. DR InterPro; IPR002085; Adh_zn_family. DR InterPro; IPR011032; GroES_like. DR Pfam; PF00107; ADH_zinc_N; 1. DR PROSITE; PS00059; ADH_ZINC; 1. KW Lignin biosynthesis; Metal-binding; Multigene family; NADP; KW Oxidoreductase; Zinc. FT METAL 48 48 Zinc 1 (catalytic) (By similarity). FT METAL 70 70 Zinc 1 (catalytic) (By similarity). FT METAL 101 101 Zinc 2 (By similarity). FT METAL 104 104 Zinc 2 (By similarity). FT METAL 107 107 Zinc 2 (By similarity). FT METAL 115 115 Zinc 2 (By similarity). FT METAL 164 164 Zinc 1 (catalytic) (By similarity). SQ SEQUENCE 365 AA; 39098 MW; 10675455727DC689 CRC64; 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 //