CADH9_ARATH
ID CADH9_ARATH Reviewed; 360 AA.
AC P42734; B9DHS7; C0Z2D3; Q8LB84; Q94K02;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Probable cinnamyl alcohol dehydrogenase 9 {ECO:0000303|PubMed:14745009};
DE Short=AtCAD9 {ECO:0000303|PubMed:14745009};
DE EC=1.1.1.195 {ECO:0000250|UniProtKB:P48523, ECO:0000305|PubMed:16832689};
GN Name=CAD9; Synonyms=CAD1; OrderedLocusNames=At4g39330; ORFNames=T22F8.230;
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=7630954; DOI=10.1104/pp.108.3.1309;
RA Somers D.A., Nourse J.P., Manners J.M., Abrahams S.L., Watson J.M.;
RT "A gene encoding a cinnamyl alcohol dehydrogenase homolog in Arabidopsis
RT thaliana.";
RL Plant Physiol. 108:1309-1310(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], 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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
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 [9]
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. May catalyze the final step
CC specific for the production of lignin monomers, like coniferyl alcohol,
CC sinapyl alcohol and 4-coumaryl alcohol. {ECO:0000269|PubMed:16832689}.
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:0000250|UniProtKB:P48523,
CC ECO:0000305|PubMed:16832689};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10394;
CC Evidence={ECO:0000250|UniProtKB:P48523};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P42734-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42734-2; Sequence=VSP_037894, VSP_037895;
CC -!- TISSUE SPECIFICITY: Expressed in the vasculature of the primary root
CC and elongation regions. Expressed in the hypocotyl, cotyledon veins,
CC vasculature of the first rosette leaves, and hydathodes. In stems,
CC expressed in the vascular cambium, interfascicular cambium, developing
CC xylem, and phloem. Expressed in the entire floral organs at late
CC developing stage, and in the abscission, style and stigmatic regions of
CC siliques and seed funicules. {ECO:0000269|PubMed:16832689,
CC ECO:0000269|PubMed:17467016}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH56862.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L37883; AAA99511.1; -; Genomic_DNA.
DR EMBL; L37884; AAA74746.1; -; mRNA.
DR EMBL; AY302076; AAP59429.1; -; mRNA.
DR EMBL; AL050351; CAB43648.1; -; Genomic_DNA.
DR EMBL; AL161595; CAB80596.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87056.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87057.1; -; Genomic_DNA.
DR EMBL; AF370498; AAK43875.1; -; mRNA.
DR EMBL; AY064669; AAL47376.1; -; mRNA.
DR EMBL; AK317632; BAH20294.1; -; mRNA.
DR EMBL; AK318747; BAH56862.1; ALT_FRAME; mRNA.
DR EMBL; AY087363; AAM64913.1; -; mRNA.
DR PIR; S71179; S71179.
DR PIR; T08581; T08581.
DR RefSeq; NP_001031812.1; NM_001036735.2. [P42734-2]
DR RefSeq; NP_195643.1; NM_120093.5. [P42734-1]
DR AlphaFoldDB; P42734; -.
DR SMR; P42734; -.
DR BioGRID; 15368; 1.
DR IntAct; P42734; 1.
DR STRING; 3702.AT4G39330.1; -.
DR iPTMnet; P42734; -.
DR MetOSite; P42734; -.
DR PaxDb; P42734; -.
DR PRIDE; P42734; -.
DR ProteomicsDB; 240313; -. [P42734-1]
DR EnsemblPlants; AT4G39330.1; AT4G39330.1; AT4G39330. [P42734-1]
DR EnsemblPlants; AT4G39330.2; AT4G39330.2; AT4G39330. [P42734-2]
DR GeneID; 830088; -.
DR Gramene; AT4G39330.1; AT4G39330.1; AT4G39330. [P42734-1]
DR Gramene; AT4G39330.2; AT4G39330.2; AT4G39330. [P42734-2]
DR KEGG; ath:AT4G39330; -.
DR Araport; AT4G39330; -.
DR TAIR; locus:2136278; AT4G39330.
DR eggNOG; KOG0023; Eukaryota.
DR HOGENOM; CLU_026673_20_2_1; -.
DR InParanoid; P42734; -.
DR OMA; YCDGGYS; -.
DR PhylomeDB; P42734; -.
DR BioCyc; ARA:AT4G39330-MON; -.
DR UniPathway; UPA00711; -.
DR PRO; PR:P42734; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P42734; baseline and differential.
DR Genevisible; P42734; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IMP: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; IMP: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 Alternative splicing; Lignin biosynthesis; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..360
FT /note="Probable cinnamyl alcohol dehydrogenase 9"
FT /id="PRO_0000160810"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 191..196
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 214..219
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 301..303
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT VAR_SEQ 302..311
FT /note="DVGGMKETQE -> LLSLMLGTGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_037894"
FT VAR_SEQ 312..360
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_037895"
FT CONFLICT 202
FT /note="I -> S (in Ref. 1; AAA99511)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="D -> N (in Ref. 6; AAM64913)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 38934 MW; 0E4F3B0581785759 CRC64;
MAKSPETEHP NKVFGWGARD KSGVLSPFHF SRRDNGENDV TVKILFCGVC HTDLHTIKND
WGYSYYPVVP GHEIVGIATK VGKNVTKFKE GDRVGVGVIS GSCQSCESCD QDLENYCPQM
SFTYNAIGSD GTKNYGGYSE NIVVDQRFVL RFPENLPSDS GAPLLCAGIT VYSPMKYYGM
TEAGKHLGVA GLGGLGHVAV KIGKAFGLKV TVISSSSTKA EEAINHLGAD SFLVTTDPQK
MKAAIGTMDY IIDTISAVHA LYPLLGLLKV NGKLIALGLP EKPLELPMFP LVLGRKMVGG
SDVGGMKETQ EMLDFCAKHN ITADIELIKM DEINTAMERL AKSDVRYRFV IDVANSLSPP
