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Database: UniProt
Entry: Q9CAI3
LinkDB: Q9CAI3
Original site: Q9CAI3 
ID   CADH1_ARATH             Reviewed;         355 AA.
AC   Q9CAI3;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JAN-2019, entry version 130.
DE   RecName: Full=Probable cinnamyl alcohol dehydrogenase 1;
DE            Short=AtCAD1;
DE            EC=1.1.1.195;
GN   Name=CAD1; Synonyms=CADG; OrderedLocusNames=At1g72680;
GN   ORFNames=F28P22.13;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
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
RT   dehydrogenase 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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
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
RT   of Arabidopsis thaliana.";
RL   Planta 225:23-39(2006).
RN   [6]
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.,
RA   Lewis N.G.;
RT   "Expression of cinnamyl alcohol dehydrogenases and their putative
RT   homologues during Arabidopsis thaliana growth and development: lessons
RT   for database annotations?";
RL   Phytochemistry 68:1957-1974(2007).
CC   -!- FUNCTION: Involved in lignin biosynthesis. Catalyzes the final
CC       step specific for the production of lignin monomers. Catalyzes the
CC       NADPH-dependent reduction of coniferaldehyde, 5-
CC       hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and
CC       caffeyl aldehyde to their respective alcohols.
CC       {ECO:0000250|UniProtKB:O49482}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde +
CC         H(+) + NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16731, ChEBI:CHEBI:33227, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.195;
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.
CC       {ECO:0000250|UniProtKB:O49482};
CC   -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid
CC       biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O49482}.
CC   -!- TISSUE SPECIFICITY: Expressed in the vasculature of the primary
CC       root and elongation regions. Expressed in the hypocotyl, cotyledon
CC       veins, vasculature of the first rosette leaves, hydathodes and at
CC       the base of the trichomes. In stems, expressed in the vascular
CC       cambium, interfascicular cambium developing xylem and cortex
CC       region. Expressed in the style, the vascular strands of the sepals
CC       pollen and anthers in flowers, in the abscission and stigmatic
CC       regions of siliques and seed funicule and testa.
CC       {ECO:0000269|PubMed:16832689, ECO:0000269|PubMed:17467016}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
DR   EMBL; AY288079; AAP40269.1; -; mRNA.
DR   EMBL; AC010926; AAG51850.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35360.1; -; Genomic_DNA.
DR   EMBL; BT002440; AAO00800.1; -; mRNA.
DR   EMBL; BT008840; AAP68279.1; -; mRNA.
DR   PIR; E96751; E96751.
DR   RefSeq; NP_177412.1; NM_105927.4.
DR   UniGene; At.35070; -.
DR   ProteinModelPortal; Q9CAI3; -.
DR   SMR; Q9CAI3; -.
DR   BioGrid; 28819; 1.
DR   STRING; 3702.AT1G72680.1; -.
DR   iPTMnet; Q9CAI3; -.
DR   PaxDb; Q9CAI3; -.
DR   PRIDE; Q9CAI3; -.
DR   EnsemblPlants; AT1G72680.1; AT1G72680.1; AT1G72680.
DR   GeneID; 843600; -.
DR   Gramene; AT1G72680.1; AT1G72680.1; AT1G72680.
DR   KEGG; ath:AT1G72680; -.
DR   Araport; AT1G72680; -.
DR   TAIR; locus:2030210; AT1G72680.
DR   eggNOG; KOG0023; Eukaryota.
DR   eggNOG; COG1064; LUCA.
DR   HOGENOM; HOG000294667; -.
DR   KO; K00083; -.
DR   OMA; EHDSCGH; -.
DR   OrthoDB; 625659at2759; -.
DR   PhylomeDB; Q9CAI3; -.
DR   BioCyc; ARA:AT1G72680-MONOMER; -.
DR   UniPathway; UPA00711; -.
DR   PRO; PR:Q9CAI3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9CAI3; baseline and differential.
DR   Genevisible; Q9CAI3; AT.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
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; IEP:UniProtKB.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
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   2: Evidence at transcript level;
KW   Complete proteome; Lignin biosynthesis; Metal-binding; NADP;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN         1    355       Probable cinnamyl alcohol dehydrogenase
FT                                1.
FT                                /FTId=PRO_0000382636.
FT   NP_BIND     189    194       NADP. {ECO:0000250|UniProtKB:O49482}.
FT   NP_BIND     212    217       NADP. {ECO:0000250|UniProtKB:O49482}.
FT   NP_BIND     298    300       NADP. {ECO:0000250|UniProtKB:O49482}.
FT   METAL        48     48       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:O49482}.
FT   METAL        70     70       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:O49482}.
FT   METAL        71     71       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:O49482}.
FT   METAL       101    101       Zinc 2. {ECO:0000250|UniProtKB:O49482}.
FT   METAL       104    104       Zinc 2. {ECO:0000250|UniProtKB:O49482}.
FT   METAL       107    107       Zinc 2. {ECO:0000250|UniProtKB:O49482}.
FT   METAL       115    115       Zinc 2. {ECO:0000250|UniProtKB:O49482}.
FT   METAL       164    164       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:O49482}.
FT   BINDING     168    168       NADP. {ECO:0000250|UniProtKB:O49482}.
FT   BINDING     252    252       NADP. {ECO:0000250|UniProtKB:O49482}.
FT   BINDING     276    276       NADP; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:O49482}.
SQ   SEQUENCE   355 AA;  38671 MW;  64AFBDB42F004E9F CRC64;
     MSSSESVENE CMCWAARDPS GLLSPHTITR RSVTTDDVSL TITHCGVCYA DVIWSRNQHG
     DSKYPLVPGH EIAGIVTKVG PNVQRFKVGD HVGVGTYVNS CRECEYCNEG QEVNCAKGVF
     TFNGIDHDGS VTKGGYSSHI VVHERYCYKI PVDYPLESAA PLLCAGITVY APMMRHNMNQ
     PGKSLGVIGL GGLGHMAVKF GKAFGLSVTV FSTSISKKEE ALNLLGAENF VISSDHDQMK
     ALEKSLDFLV DTASGDHAFD PYMSLLKIAG TYVLVGFPSE IKISPANLNL GMRMLAGSVT
     GGTKITQQML DFCAAHKIYP NIEVIPIQKI NEALERVVKK DIKYRFVIDI KNSLK
//
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