CADH2_ARATH
ID CADH2_ARATH Reviewed; 376 AA.
AC Q9SJ25;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Cinnamyl alcohol dehydrogenase 2 {ECO:0000303|PubMed:14745009};
DE Short=AtCAD2 {ECO:0000303|PubMed:14745009};
DE EC=1.1.1.195 {ECO:0000269|PubMed:14745009};
GN Name=CAD2 {ECO:0000303|PubMed:14745009};
GN Synonyms=CAD7 {ECO:0000305}, CADE {ECO:0000303|PubMed:16832689},
GN LCAD-E {ECO:0000305};
GN OrderedLocusNames=At2g21730 {ECO:0000312|Araport:AT2G21730};
GN ORFNames=F7D8.5 {ECO:0000312|EMBL:AAD20393.1};
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=114 uM for 4-coumaraldehyde (at pH 6.5 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC KM=161 uM for caffeyl aldehyde (at pH 6.25-6.5 and 40 degrees
CC Celsius) {ECO:0000269|PubMed:14745009};
CC KM=452 uM for coniferaldehyde (at pH 6.5 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC KM=336 uM for 5-hydroxyconiferaldehyde (at pH 6.5 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:14745009};
CC KM=2161 uM for sinapaldehyde (at pH 6.5 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC Vmax=3.3 pmol/sec/ug enzyme with 4-coumaraldehyde as substrate (at pH
CC 6.5 and 40 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC Vmax=22.2 pmol/sec/ug enzyme with caffeyl aldehyde as substrate (at
CC pH 6.25-6.5 and 40 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC Vmax=8.0 pmol/sec/ug enzyme with coniferaldehyde as substrate (at pH
CC 6.5 and 40 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC Vmax=16.4 pmol/sec/ug enzyme with 5-hydroxyconiferaldehyde as
CC substrate (at pH 6.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC Vmax=48.1 pmol/sec/ug enzyme with sinapaldehyde as substrate (at pH
CC 6.5 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 at the base of the stems.
CC {ECO:0000269|PubMed:16832689, ECO:0000269|PubMed:17467016}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AY302077; AAP59430.1; -; mRNA.
DR EMBL; AC007019; AAD20393.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07217.1; -; Genomic_DNA.
DR PIR; E84604; E84604.
DR RefSeq; NP_179765.1; NM_127743.4.
DR AlphaFoldDB; Q9SJ25; -.
DR SMR; Q9SJ25; -.
DR STRING; 3702.AT2G21730.1; -.
DR PaxDb; Q9SJ25; -.
DR PRIDE; Q9SJ25; -.
DR ProteomicsDB; 223863; -.
DR EnsemblPlants; AT2G21730.1; AT2G21730.1; AT2G21730.
DR GeneID; 816710; -.
DR Gramene; AT2G21730.1; AT2G21730.1; AT2G21730.
DR KEGG; ath:AT2G21730; -.
DR Araport; AT2G21730; -.
DR TAIR; locus:2052516; AT2G21730.
DR eggNOG; KOG0023; Eukaryota.
DR HOGENOM; CLU_026673_20_2_1; -.
DR InParanoid; Q9SJ25; -.
DR OMA; FILPGHR; -.
DR OrthoDB; 625659at2759; -.
DR PhylomeDB; Q9SJ25; -.
DR BioCyc; ARA:AT2G21730-MON; -.
DR SABIO-RK; Q9SJ25; -.
DR UniPathway; UPA00711; -.
DR PRO; PR:Q9SJ25; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJ25; baseline and differential.
DR Genevisible; Q9SJ25; 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..376
FT /note="Cinnamyl alcohol dehydrogenase 2"
FT /id="PRO_0000382637"
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 161
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 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 187..192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 210..215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 250
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 274
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 297..299
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
SQ SEQUENCE 376 AA; 40909 MW; E85BBD9FD9F1EA94 CRC64;
MVDQNKAFGW AANDESGVLS PFHFSRRENG ENDVTVKILF CGVCHSDLHT IKNHWGFSRY
PIIPGHEIVG IATKVGKNVT KFKEGDRVGV GVIIGSCQSC ESCNQDLENY CPKVVFTYNS
RSSDGTSRNQ GGYSDVIVVD HRFVLSIPDG LPSDSGAPLL CAGITVYSPM KYYGMTKESG
KRLGVNGLGG LGHIAVKIGK AFGLRVTVIS RSSEKEREAI DRLGADSFLV TTDSQKMKEA
VGTMDFIIDT VSAEHALLPL FSLLKVNGKL VALGLPEKPL DLPIFSLVLG RKMVGGSQIG
GMKETQEMLE FCAKHKIVSD IELIKMSDIN SAMDRLAKSD VRYRFVIDVA NSLLPESSAE
ILTEQVDHGV SITSRF
