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 10-MAY-2017, entry version 126. 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; GN OrderedLocusNames=At3g19450; ORFNames=MLD14.19; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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 RT a cinnamyl alcohol dehydrogenase."; RL Plant Physiol. 107:285-286(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, RP GENE 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 RT dehydrogenase 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, RC cv. Ita-0, cv. Kas-1, cv. Kon, cv. La-0, cv. Me-0, cv. Mh-0, cv. Mr-0, RC cv. Nc-1, cv. Per-1, cv. Ri-0, cv. Rsch-0, cv. Rub-1, cv. Tul-0, RC cv. Wassilewskija, 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., RA 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; RG The Arabidopsis Information Portal (Araport); RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. 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., 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). 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., RA Seguin A., 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 RT involved in 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., RA Lewis N.G.; RT "Expression of cinnamyl alcohol dehydrogenases and their putative RT homologues during Arabidopsis thaliana growth and development: lessons RT for database annotations?"; RL Phytochemistry 68:1957-1974(2007). CC -!- FUNCTION: Involved in lignin biosynthesis in the floral stem. CC Catalyzes the final step specific for the production of lignin CC monomers. Catalyzes the NADPH-dependent reduction of CC coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4- CC coumaraldehyde and caffeyl aldehyde to their respective alcohols. CC {ECO:0000269|PubMed:12805615, ECO:0000269|PubMed:14745009, CC ECO:0000269|PubMed:15937231}. CC -!- CATALYTIC ACTIVITY: Cinnamyl alcohol + NADP(+) = cinnamaldehyde + CC NADPH. 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=47 uM for 4-coumaraldehyde (at pH 6.25-6.5 and 35 degrees CC Celsius) {ECO:0000269|PubMed:14745009}; CC KM=87 uM for caffeyl aldehyde (at pH 6.25 and 30 degrees CC Celsius) {ECO:0000269|PubMed:14745009}; CC KM=65 uM for coniferaldehyde (at pH 6.25-6.5 and 35 degrees CC Celsius) {ECO:0000269|PubMed:14745009}; CC KM=85 uM for 5-hydroxyconiferaldehyde (at pH 6.25-6.5 and 30 CC degrees Celsius) {ECO:0000269|PubMed:14745009}; CC KM=274 uM for sinapaldehyde (at pH 6.25-6.5 and 30 degrees CC Celsius) {ECO:0000269|PubMed:14745009}; CC Vmax=44.0 pmol/sec/ug enzyme with 4-coumaraldehyde as substrate CC (at pH 6.25-6.5 and 35 degrees Celsius) CC {ECO:0000269|PubMed:14745009}; CC Vmax=17.1 pmol/sec/ug enzyme with caffeyl aldehyde as substrate CC (at pH 6.25 and 30 degrees Celsius) CC {ECO:0000269|PubMed:14745009}; CC Vmax=26.8 pmol/sec/ug enzyme with coniferaldehyde as substrate CC (at pH 6.25-6.5 and 35 degrees Celsius) CC {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 CC pH 6.25-6.5 and 30 degrees Celsius) CC {ECO:0000269|PubMed:14745009}; CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid CC biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O49482}. CC -!- TISSUE SPECIFICITY: Expressed at the lateral root initiation CC sites, in the vascular tissues of the primary lateral root and the CC root caps. Expressed in the hypocotyl, cotyledon and leaf veins, CC apical meristem region, hydathodes, at the base of the trichomes CC and cauline leaves. In stems, expressed in the cells associated CC with the vascular cambium, interfascicular cambium and the CC developing xylem. Expressed in the vascular strand of petals and CC sepals, anthers, stamen filaments, stigma with papillary cells in CC flowers, and abscission, style and stigmatic regions of siliques. CC {ECO:0000269|PubMed:12805615, ECO:0000269|PubMed:17467016}. CC -!- DISRUPTION PHENOTYPE: Reduced lignin content and rigidity of the CC floral 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 UniGene; At.24340; -. DR ProteinModelPortal; P48523; -. DR SMR; P48523; -. DR BioGrid; 6812; 1. DR STRING; 3702.AT3G19450.1; -. DR PaxDb; P48523; -. DR PRIDE; P48523; -. 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 eggNOG; COG1064; LUCA. DR HOGENOM; HOG000294667; -. DR InParanoid; P48523; -. DR KO; K00083; -. DR OMA; NEFANMS; -. DR OrthoDB; EOG09360FXB; -. 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:0045551; F:cinnamyl-alcohol dehydrogenase activity; IDA:TAIR. 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. DR InterPro; IPR016040; NAD(P)-bd_dom. 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 Complete proteome; Lignin biosynthesis; Metal-binding; NADP; KW Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1 365 Cinnamyl alcohol dehydrogenase 4. FT /FTId=PRO_0000160790. FT NP_BIND 189 194 NADP. {ECO:0000250|UniProtKB:O49482}. FT NP_BIND 212 217 NADP. {ECO:0000250|UniProtKB:O49482}. FT NP_BIND 299 301 NADP. {ECO:0000250|UniProtKB:O49482}. FT METAL 48 48 Zinc 1; catalytic. FT {ECO:0000250|UniProtKB:O49482}. FT METAL 70 70 Zinc 1; catalytic. FT {ECO:0000250|UniProtKB:O49482}. FT METAL 71 71 Zinc 1; catalytic. FT {ECO:0000250|UniProtKB:O49482}. FT METAL 101 101 Zinc 2. {ECO:0000250|UniProtKB:O49482}. FT METAL 104 104 Zinc 2. {ECO:0000250|UniProtKB:O49482}. FT METAL 107 107 Zinc 2. {ECO:0000250|UniProtKB:O49482}. FT METAL 115 115 Zinc 2. {ECO:0000250|UniProtKB:O49482}. FT METAL 164 164 Zinc 1; catalytic. FT {ECO:0000250|UniProtKB:O49482}. FT BINDING 50 50 NADP. {ECO:0000250|UniProtKB:O49482}. FT BINDING 168 168 NADP. {ECO:0000250|UniProtKB:O49482}. FT BINDING 252 252 NADP. {ECO:0000250|UniProtKB:O49482}. FT BINDING 276 276 NADP; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:O49482}. FT CONFLICT 139 139 T -> A (in Ref. 3; CAP09015). FT {ECO:0000305}. FT CONFLICT 234 234 S -> T (in Ref. 3; CAP09015). FT {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 //