GenomeNet

Database: UniProt
Entry: CADH2_ARATH
LinkDB: CADH2_ARATH
Original site: 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   24-JAN-2024, entry version 149.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-coniferol + NADP(+) = (E)-coniferaldehyde + H(+) + NADPH;
CC         Xref=Rhea:RHEA:22444, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547,
CC         ChEBI:CHEBI:17745, 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:22446;
CC         Evidence={ECO:0000269|PubMed:14745009};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-sinapyl alcohol + NADP(+) = (E)-sinapaldehyde + H(+) +
CC         NADPH; Xref=Rhea:RHEA:45704, ChEBI:CHEBI:15378, ChEBI:CHEBI:27949,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64557;
CC         EC=1.1.1.195; Evidence={ECO:0000269|PubMed:14745009};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45706;
CC         Evidence={ECO:0000269|PubMed:14745009};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-coumaroyl alcohol + NADP(+) = (E)-4-coumaraldehyde +
CC         H(+) + NADPH; Xref=Rhea:RHEA:45724, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28353, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:64555; EC=1.1.1.195;
CC         Evidence={ECO:0000269|PubMed:14745009};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45726;
CC         Evidence={ECO:0000269|PubMed:14745009};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-caffeyl alcohol + NADP(+) = (E)-caffeyl aldehyde + H(+) +
CC         NADPH; Xref=Rhea:RHEA:45728, ChEBI:CHEBI:15378, ChEBI:CHEBI:28323,
CC         ChEBI:CHEBI:31334, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000269|PubMed:14745009};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45730;
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}.
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; 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.Q9SJ25; -.
DR   PaxDb; 3702-AT2G21730-1; -.
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; AT2G21730; CAD2.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_026673_20_2_1; -.
DR   InParanoid; Q9SJ25; -.
DR   OMA; RNKAFGW; -.
DR   OrthoDB; 1550at2759; -.
DR   PhylomeDB; Q9SJ25; -.
DR   BioCyc; ARA:AT2G21730-MONOMER; -.
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:0050268; F:coniferyl-alcohol dehydrogenase activity; IEA:RHEA.
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   CDD; cd05283; CAD1; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF44; CINNAMYL ALCOHOL DEHYDROGENASE 2-RELATED; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//
DBGET integrated database retrieval system