CADH3_ARATH
ID CADH3_ARATH Reviewed; 375 AA.
AC Q9SJ10;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cinnamyl alcohol dehydrogenase 3 {ECO:0000303|PubMed:14745009};
DE Short=AtCAD3 {ECO:0000303|PubMed:14745009};
DE EC=1.1.1.195 {ECO:0000269|PubMed:14745009};
GN Name=CAD3 {ECO:0000303|PubMed:14745009};
GN Synonyms=CAD8 {ECO:0000303|PubMed:16832689},
GN CADF {ECO:0000303|PubMed:16832689}, LCAD-F {ECO:0000303|PubMed:16832689};
GN OrderedLocusNames=At2g21890 {ECO:0000312|Araport:AT2G21890};
GN ORFNames=F7D8.21 {ECO:0000312|EMBL:AAD20406.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=16832689; DOI=10.1007/s00425-006-0326-9;
RA Eudes A., Pollet B., Sibout R., Do C.-T., Seguin A., Lapierre C.,
RA Jouanin L.;
RT "Evidence for a role of AtCAD 1 in lignification of elongating stems of
RT Arabidopsis thaliana.";
RL Planta 225:23-39(2006).
RN [5]
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. Catalyzes the final step
CC specific for the production of lignin monomers. Catalyzes the NADPH-
CC dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde,
CC sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their
CC respective alcohols. {ECO:0000269|PubMed:14745009}.
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=292 uM for 4-coumaraldehyde (at pH 6.25 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC KM=581 uM for caffeyl aldehyde (at pH 6.25 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC KM=362 uM for coniferaldehyde (at pH 6.25 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC KM=534 uM for 5-hydroxyconiferaldehyde (at pH 6.25 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:14745009};
CC KM=629 uM for sinapaldehyde (at pH 6.25 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC Vmax=20.1 pmol/sec/ug enzyme with 4-coumaraldehyde as substrate (at
CC pH 6.25 and 40 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC Vmax=9.7 pmol/sec/ug enzyme with caffeyl aldehyde as substrate (at pH
CC 6.25 and 40 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC Vmax=4.8 pmol/sec/ug enzyme with coniferaldehyde as substrate (at pH
CC 6.25 and 40 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC Vmax=17.9 pmol/sec/ug enzyme with 5-hydroxyconiferaldehyde as
CC substrate (at pH 6.25 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC Vmax=9.1 pmol/sec/ug enzyme with sinapaldehyde as substrate (at pH
CC 6.25 and 40 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O49482}.
CC -!- TISSUE SPECIFICITY: Expressed in the root tips. Expressed in the apical
CC meristematic regions, leaf veins and at the base of the trichomes.
CC Expressed at the base of the stems. Expressed in the abscission zones
CC of newly formed siliques. {ECO:0000269|PubMed:16832689,
CC ECO:0000269|PubMed:17467016}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AY302078; AAP59431.1; -; mRNA.
DR EMBL; AC007019; AAD20406.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07235.1; -; Genomic_DNA.
DR PIR; D84606; D84606.
DR RefSeq; NP_179780.1; NM_127758.3.
DR AlphaFoldDB; Q9SJ10; -.
DR SMR; Q9SJ10; -.
DR STRING; 3702.AT2G21890.1; -.
DR PaxDb; Q9SJ10; -.
DR PRIDE; Q9SJ10; -.
DR ProteomicsDB; 240272; -.
DR EnsemblPlants; AT2G21890.1; AT2G21890.1; AT2G21890.
DR GeneID; 816725; -.
DR Gramene; AT2G21890.1; AT2G21890.1; AT2G21890.
DR KEGG; ath:AT2G21890; -.
DR Araport; AT2G21890; -.
DR TAIR; locus:2052494; AT2G21890.
DR eggNOG; KOG0023; Eukaryota.
DR HOGENOM; CLU_026673_20_2_1; -.
DR InParanoid; Q9SJ10; -.
DR OMA; CNIAANI; -.
DR OrthoDB; 625659at2759; -.
DR PhylomeDB; Q9SJ10; -.
DR BioCyc; ARA:AT2G21890-MON; -.
DR SABIO-RK; Q9SJ10; -.
DR UniPathway; UPA00711; -.
DR PRO; PR:Q9SJ10; -.
DR Proteomes; UP000006548; Chromosome 2.
DR Genevisible; Q9SJ10; AT.
DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IDA:UniProtKB.
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; IC:UniProtKB.
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..375
FT /note="Cinnamyl alcohol dehydrogenase 3"
FT /id="PRO_0000382638"
FT BINDING 44
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 46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 66
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 67
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 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 160
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 164
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 186..191
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 209..214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 249
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 296..298
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
SQ SEQUENCE 375 AA; 40886 MW; ADC1FFCABEA2D113 CRC64;
MVDQNRAFGW AANDESGVLS PFHFSRRENG ENDVTVKILF CGVCHSDLHT IKNHWGFSRY
PIIPGHEIVG IATKVGKNVT KFKEGDRVGV GVIIGSCQSC ESCNQDLENY CPKVVFTYNS
RSSDGTRNQG GYSDVIVVDH RFVLSIPDGL PSDSGAPLLC AGITVYSPMK YYGMTKESGK
RLGVNGLGGL GHIAVKIGKA FGLRVTVISR SSEKEREAID RLGADSFLVT TDSQKMKEAV
GTMDFIIDTV SAEHALLPLF SLLKVSGKLV ALGLLEKPLD LPIFPLVLGR KMVGGSQIGG
MKETQEMLEF CAKHKIVSDI ELIKMSDINS AMDRLVKSDV RYRFVIDVAN SLLPESSAEI
LTEHVDHGVS ITSRF
