ID CADH4_ARATH Reviewed; 365 AA. AC P48523; B1GUX6; Q53ZN1; Q8L9U1; Q94B56; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 29-SEP-2021, entry version 142. DE RecName: Full=Cinnamyl alcohol dehydrogenase 4; DE Short=AtCAD4; DE EC=1.1.1.195; DE AltName: Full=Cinnamyl alcohol dehydrogenase C; GN Name=CAD4; Synonyms=CAD, CAD-C, CAD2, LCAD-C; OrderedLocusNames=At3g19450; GN ORFNames=MLD14.19; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX 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 a RT cinnamyl alcohol dehydrogenase."; RL Plant Physiol. 107:285-286(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, GENE RP FAMILY, AND NOMENCLATURE. RX PubMed=14745009; DOI=10.1073/pnas.0307987100; RA Kim S.-J., Kim M.-R., Bedgar D.L., Moinuddin S.G.A., Cardenas C.L., RA Davin L.B., Kang C., Lewis N.G.; RT "Functional reclassification of the putative cinnamyl alcohol dehydrogenase RT multigene family in Arabidopsis."; RL Proc. Natl. Acad. Sci. U.S.A. 101:1455-1460(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Can-0, cv. Cha-0, cv. Col-2, cv. Cvi-0, cv. Gr-5, cv. Ita-0, RC cv. Kas-1, cv. Kon, cv. La-0, cv. Me-0, cv. Mh-0, cv. Mr-0, cv. Nc-1, RC cv. Per-1, cv. Ri-0, cv. Rsch-0, cv. Rub-1, cv. Tul-0, cv. Wassilewskija, RC and cv. Yo-0; RX PubMed=18221273; DOI=10.1111/j.1365-294x.2007.03633.x; RA Ramos-Onsins S.E., Puerma E., Balana-Alcaide D., Salguero D., Aguade M.; RT "Multilocus analysis of variation using a large empirical data set: RT phenylpropanoid pathway genes in Arabidopsis thaliana."; RL Mol. Ecol. 17:1211-1223(2008). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10819329; DOI=10.1093/dnares/7.2.131; 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 [5] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=12805615; DOI=10.1104/pp.103.021048; RA Sibout R., Eudes A., Pollet B., Goujon T., Mila I., Granier F., Seguin A., RA Lapierre C., Jouanin L.; RT "Expression pattern of two paralogs encoding cinnamyl alcohol RT dehydrogenases in Arabidopsis. Isolation and characterization of the RT corresponding mutants."; RL Plant Physiol. 132:848-860(2003). RN [9] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=15937231; DOI=10.1105/tpc.105.030767; RA Sibout R., Eudes A., Mouille G., Pollet B., Lapierre C., Jouanin L., RA Seguin A.; RT "CINNAMYL ALCOHOL DEHYDROGENASE-C and -D are the primary genes involved in RT lignin biosynthesis in the floral stem of Arabidopsis."; RL Plant Cell 17:2059-2076(2005). RN [10] RP TISSUE SPECIFICITY. RX PubMed=17467016; DOI=10.1016/j.phytochem.2007.02.032; RA Kim S.-J., Kim K.-W., Cho M.-H., Franceschi V.R., Davin L.B., Lewis N.G.; RT "Expression of cinnamyl alcohol dehydrogenases and their putative RT homologues during Arabidopsis thaliana growth and development: lessons for RT database annotations?"; RL Phytochemistry 68:1957-1974(2007). CC -!- FUNCTION: Involved in lignin biosynthesis in the floral stem. Catalyzes CC the final step specific for the production of lignin monomers. CC Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5- CC hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl CC aldehyde to their respective alcohols. {ECO:0000269|PubMed:12805615, CC ECO:0000269|PubMed:14745009, ECO:0000269|PubMed:15937231}. 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=47 uM for 4-coumaraldehyde (at pH 6.25-6.5 and 35 degrees Celsius) CC {ECO:0000269|PubMed:14745009}; CC KM=87 uM for caffeyl aldehyde (at pH 6.25 and 30 degrees Celsius) CC {ECO:0000269|PubMed:14745009}; CC KM=65 uM for coniferaldehyde (at pH 6.25-6.5 and 35 degrees Celsius) CC {ECO:0000269|PubMed:14745009}; CC KM=85 uM for 5-hydroxyconiferaldehyde (at pH 6.25-6.5 and 30 degrees CC Celsius) {ECO:0000269|PubMed:14745009}; CC KM=274 uM for sinapaldehyde (at pH 6.25-6.5 and 30 degrees Celsius) CC {ECO:0000269|PubMed:14745009}; CC Vmax=44.0 pmol/sec/ug enzyme with 4-coumaraldehyde as substrate (at CC pH 6.25-6.5 and 35 degrees Celsius) {ECO:0000269|PubMed:14745009}; CC Vmax=17.1 pmol/sec/ug enzyme with caffeyl aldehyde as substrate (at CC pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009}; CC Vmax=26.8 pmol/sec/ug enzyme with coniferaldehyde as substrate (at pH CC 6.25-6.5 and 35 degrees Celsius) {ECO:0000269|PubMed:14745009}; CC Vmax=32.3 pmol/sec/ug enzyme with 5-hydroxyconiferaldehyde as CC substrate (at pH 6.25-6.5 and 30 degrees Celsius) CC {ECO:0000269|PubMed:14745009}; CC Vmax=9.2 pmol/sec/ug enzyme with sinapaldehyde as substrate (at pH CC 6.25-6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009}; CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O49482}. CC -!- TISSUE SPECIFICITY: Expressed at the lateral root initiation sites, in CC the vascular tissues of the primary lateral root and the root caps. CC Expressed in the hypocotyl, cotyledon and leaf veins, apical meristem CC region, hydathodes, at the base of the trichomes and cauline leaves. In CC stems, expressed in the cells associated with the vascular cambium, CC interfascicular cambium and the developing xylem. Expressed in the CC vascular strand of petals and sepals, anthers, stamen filaments, stigma CC with papillary cells in flowers, and abscission, style and stigmatic CC regions of siliques. {ECO:0000269|PubMed:12805615, CC ECO:0000269|PubMed:17467016}. CC -!- DISRUPTION PHENOTYPE: Reduced lignin content and rigidity of the floral CC stems. {ECO:0000269|PubMed:15937231}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {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; Z31715; CAA83508.1; -; Genomic_DNA. DR EMBL; AY302081; AAP59434.1; -; mRNA. DR EMBL; AM887553; CAP09010.1; -; Genomic_DNA. DR EMBL; AM887554; CAP09011.1; -; Genomic_DNA. DR EMBL; AM887555; CAP09012.1; -; Genomic_DNA. DR EMBL; AM887556; CAP09013.1; -; Genomic_DNA. DR EMBL; AM887557; CAP09014.1; -; Genomic_DNA. DR EMBL; AM887558; CAP09015.1; -; Genomic_DNA. DR EMBL; AM887559; CAP09016.1; -; Genomic_DNA. DR EMBL; AM887560; CAP09017.1; -; Genomic_DNA. DR EMBL; AM887561; CAP09018.1; -; Genomic_DNA. DR EMBL; AM887562; CAP09019.1; -; Genomic_DNA. DR EMBL; AM887563; CAP09020.1; -; Genomic_DNA. DR EMBL; AM887564; CAP09021.1; -; Genomic_DNA. DR EMBL; AM887565; CAP09022.1; -; Genomic_DNA. DR EMBL; AM887566; CAP09023.1; -; Genomic_DNA. DR EMBL; AM887567; CAP09024.1; -; Genomic_DNA. DR EMBL; AM887568; CAP09025.1; -; Genomic_DNA. DR EMBL; AM887569; CAP09026.1; -; Genomic_DNA. DR EMBL; AM887570; CAP09027.1; -; Genomic_DNA. DR EMBL; AM887571; CAP09028.1; -; Genomic_DNA. DR EMBL; AM887572; CAP09029.1; -; Genomic_DNA. DR EMBL; AB025624; BAB02470.1; -; Genomic_DNA. DR EMBL; CP002686; AEE76241.1; -; Genomic_DNA. DR EMBL; AF370261; AAK44076.1; -; mRNA. DR EMBL; AY042841; AAK68781.1; -; mRNA. DR EMBL; AY063076; AAL34250.1; -; mRNA. DR EMBL; AY088220; AAM65761.1; -; mRNA. DR PIR; S45094; S45094. DR RefSeq; NP_188576.1; NM_112832.4. DR SMR; P48523; -. DR BioGRID; 6812; 1. DR STRING; 3702.AT3G19450.1; -. DR MetOSite; P48523; -. DR PaxDb; P48523; -. DR PRIDE; P48523; -. DR ProteomicsDB; 239123; -. DR EnsemblPlants; AT3G19450.1; AT3G19450.1; AT3G19450. DR GeneID; 821479; -. DR Gramene; AT3G19450.1; AT3G19450.1; AT3G19450. DR KEGG; ath:AT3G19450; -. DR Araport; AT3G19450; -. DR TAIR; locus:2090704; AT3G19450. DR eggNOG; KOG0023; Eukaryota. DR HOGENOM; CLU_026673_20_2_1; -. DR InParanoid; P48523; -. DR OMA; FARNEHK; -. DR OrthoDB; 625659at2759; -. DR PhylomeDB; P48523; -. DR BioCyc; MetaCyc:AT3G19450-MONOMER; -. DR BRENDA; 1.1.1.195; 399. DR SABIO-RK; P48523; -. DR UniPathway; UPA00711; -. DR PRO; PR:P48523; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; P48523; baseline and differential. DR Genevisible; P48523; AT. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IDA:TAIR. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central. 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; IGI:TAIR. DR GO; GO:0080167; P:response to karrikin; IEP:TAIR. 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 1: Evidence at protein level; KW Lignin biosynthesis; Metal-binding; NADP; Oxidoreductase; KW Reference proteome; Zinc. FT CHAIN 1..365 FT /note="Cinnamyl alcohol dehydrogenase 4" FT /id="PRO_0000160790" FT NP_BIND 189..194 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:O49482" FT NP_BIND 212..217 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:O49482" FT NP_BIND 299..301 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 48 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 71 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 101 FT /note="Zinc 2" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 104 FT /note="Zinc 2" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 107 FT /note="Zinc 2" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 115 FT /note="Zinc 2" FT /evidence="ECO:0000250|UniProtKB:O49482" FT METAL 164 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000250|UniProtKB:O49482" FT BINDING 50 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:O49482" FT BINDING 168 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:O49482" FT BINDING 252 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:O49482" FT BINDING 276 FT /note="NADP; via carbonyl oxygen" FT /evidence="ECO:0000250|UniProtKB:O49482" FT CONFLICT 139 FT /note="T -> A (in Ref. 3; CAP09015)" FT /evidence="ECO:0000305" FT CONFLICT 234 FT /note="S -> T (in Ref. 3; CAP09015)" FT /evidence="ECO:0000305" 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 //