CADH4_ARATH
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 03-AUG-2022, entry version 145.
DE RecName: Full=Cinnamyl alcohol dehydrogenase 4 {ECO:0000303|PubMed:14745009};
DE Short=AtCAD4 {ECO:0000303|PubMed:14745009};
DE EC=1.1.1.195 {ECO:0000269|PubMed:14745009};
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, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, 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 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; Evidence={ECO:0000269|PubMed:14745009};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10394;
CC Evidence={ECO:0000269|PubMed:14745009};
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 {ECO:0000269|PubMed:14745009}.
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}.
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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 AlphaFoldDB; P48523; -.
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; LPWIQKR; -.
DR OrthoDB; 625659at2759; -.
DR PhylomeDB; P48523; -.
DR BioCyc; MetaCyc:AT3G19450-MON; -.
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 InterPro; IPR013149; ADH-like_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 BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 189..194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 212..217
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 252
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 276
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 299..301
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
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
