ID CCR1_ARATH Reviewed; 344 AA. AC Q9S9N9; Q9FPM0; DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 15-FEB-2017, entry version 112. DE RecName: Full=Cinnamoyl-CoA reductase 1; DE Short=AtCCR1; DE EC=1.2.1.44; DE AltName: Full=Protein IRREGULAR XYLEM 4; GN Name=CCR1; Synonyms=IRX4; OrderedLocusNames=At1g15950; GN ORFNames=T24D18.5; 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], FUNCTION, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC TISSUE=Seedling; RX PubMed=11430991; DOI=10.1016/S0031-9422(01)00053-X; RA Lauvergeat V., Lacomme C., Lacombe E., Lasserre E., Roby D., RA Grima-Pettenati J.; RT "Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are RT differentially expressed during development and in response to RT infection with pathogenic bacteria."; RL Phytochemistry 57:1187-1195(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, RP AND DISRUPTION PHENOTYPE. RC STRAIN=cv. Columbia; RX PubMed=16153410; DOI=10.1016/j.phytochem.2004.12.016; RA Patten A.M., Cardenas C.L., Cochrane F.C., Laskar D.D., Bedgar D.L., RA Davin L.B., Lewis N.G.; RT "Reassessment of effects on lignification and vascular development in RT the irx4 Arabidopsis mutant."; RL Phytochemistry 66:2092-2107(2005). RN [3] 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 [4] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., RA Hayashizaki Y., Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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, AND DISRUPTION PHENOTYPE. RC STRAIN=cv. Landsberg erecta; RX PubMed=11389761; DOI=10.1046/j.1365-313x.2001.01021.x; RA Jones L., Ennos A.R., Turner S.R.; RT "Cloning and characterization of irregular xylem4 (irx4): a severely RT lignin-deficient mutant of Arabidopsis."; RL Plant J. 26:205-216(2001). RN [9] RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16122934; DOI=10.1016/j.plaphy.2005.06.003; RA Baltas M., Lapeyre C., Bedos-Belval F., Maturano M., Saint-Aguet P., RA Roussel L., Duran H., Grima-Pettenati J.; RT "Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from RT Arabidopsis thaliana."; RL Plant Physiol. Biochem. 43:746-753(2005). RN [10] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=cv. Columbia; RX PubMed=18046574; DOI=10.1007/s00425-007-0669-x; RA Mir Derikvand M., Sierra J.B., Ruel K., Pollet B., Do C.T., RA Thevenin J., Buffard D., Jouanin L., Lapierre C.; RT "Redirection of the phenylpropanoid pathway to feruloyl malate in RT Arabidopsis mutants deficient for cinnamoyl-CoA reductase 1."; RL Planta 227:943-956(2008). RN [11] RP FUNCTION. RX PubMed=19674336; DOI=10.1111/j.1469-8137.2009.02951.x; RA Ruel K., Berrio-Sierra J., Derikvand M.M., Pollet B., Thevenin J., RA Lapierre C., Jouanin L., Joseleau J.P.; RT "Impact of CCR1 silencing on the assembly of lignified secondary walls RT in Arabidopsis thaliana."; RL New Phytol. 184:99-113(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19376835; DOI=10.1104/pp.109.138677; RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., RA Grossmann J., Gruissem W., Baginsky S.; RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel RT chloroplast kinase substrates and phosphorylation networks."; RL Plant Physiol. 150:889-903(2009). RN [13] RP FUNCTION. RX PubMed=20829305; DOI=10.1093/mp/ssq045; RA Thevenin J., Pollet B., Letarnec B., Saulnier L., Gissot L., RA Maia-Grondard A., Lapierre C., Jouanin L.; RT "The simultaneous repression of CCR and CAD, two enzymes of the lignin RT biosynthetic pathway, results in sterility and dwarfism in Arabidopsis RT thaliana."; RL Mol. Plant 4:70-82(2011). CC -!- FUNCTION: Involved in the latter stages of lignin biosynthesis. CC Catalyzes one of the last steps of monolignol biosynthesis, the CC conversion of cinnamoyl-CoAs into their corresponding CC cinnamaldehydes. {ECO:0000269|PubMed:11389761, CC ECO:0000269|PubMed:11430991, ECO:0000269|PubMed:16122934, CC ECO:0000269|PubMed:16153410, ECO:0000269|PubMed:18046574, CC ECO:0000269|PubMed:19674336, ECO:0000269|PubMed:20829305}. CC -!- CATALYTIC ACTIVITY: Cinnamaldehyde + CoA + NADP(+) = cinnamoyl-CoA CC + NADPH. {ECO:0000269|PubMed:11430991}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.96 uM for feruloyl-CoA {ECO:0000269|PubMed:11430991, CC ECO:0000269|PubMed:16122934, ECO:0000269|PubMed:16153410}; CC KM=2.27 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:11430991, CC ECO:0000269|PubMed:16122934, ECO:0000269|PubMed:16153410}; CC KM=6.32 uM for sinapoyl-CoA {ECO:0000269|PubMed:11430991, CC ECO:0000269|PubMed:16122934, ECO:0000269|PubMed:16153410}; CC KM=12.5 uM for caffeoyl-CoA {ECO:0000269|PubMed:11430991, CC ECO:0000269|PubMed:16122934, ECO:0000269|PubMed:16153410}; CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid CC biosynthesis. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=Q9S9N9-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers. CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype, delayed senescence, CC collapsed xylem and significant reduction of lignin content in CC ecotype Columbia (PubMed:19674336). Retarded growth, impaired CC upright growth, altered leaf morphology, dark green leaves, CC collapsed xylem and strong decrease in lignin content in ecotype CC Landsberg erecta (PubMed:11389761). {ECO:0000269|PubMed:11389761, CC ECO:0000269|PubMed:16153410, ECO:0000269|PubMed:18046574, CC ECO:0000269|PubMed:19674336}. CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. Dihydroflavonol-4-reductase subfamily. {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; AF320624; AAG46037.1; -; mRNA. DR EMBL; AY743921; AAU45042.1; -; mRNA. DR EMBL; AC010924; AAF18492.1; -; Genomic_DNA. DR EMBL; CP002684; AEE29388.1; -; Genomic_DNA. DR EMBL; AF332459; AAG48822.1; -; mRNA. DR EMBL; AF321114; AAL37194.1; -; mRNA. DR EMBL; AK228419; BAF00353.1; -; mRNA. DR EMBL; AY087316; AAM64866.1; -; mRNA. DR PIR; A86294; A86294. DR RefSeq; NP_001319013.1; NM_001332191.1. [Q9S9N9-1] DR RefSeq; NP_173047.1; NM_101463.4. [Q9S9N9-1] DR UniGene; At.23016; -. DR UniGene; At.72454; -. DR ProteinModelPortal; Q9S9N9; -. DR SMR; Q9S9N9; -. DR STRING; 3702.AT1G15950.1; -. DR iPTMnet; Q9S9N9; -. DR PaxDb; Q9S9N9; -. DR EnsemblPlants; AT1G15950.1; AT1G15950.1; AT1G15950. [Q9S9N9-1] DR EnsemblPlants; AT1G15950.3; AT1G15950.3; AT1G15950. [Q9S9N9-1] DR GeneID; 838165; -. DR Gramene; AT1G15950.1; AT1G15950.1; AT1G15950. DR Gramene; AT1G15950.3; AT1G15950.3; AT1G15950. DR KEGG; ath:AT1G15950; -. DR Araport; AT1G15950; -. DR TAIR; locus:2200427; AT1G15950. DR eggNOG; KOG1502; Eukaryota. DR eggNOG; COG0451; LUCA. DR HOGENOM; HOG000167998; -. DR KO; K09753; -. DR OMA; ITHILKY; -. DR OrthoDB; EOG09360DOS; -. DR PhylomeDB; Q9S9N9; -. DR BioCyc; MetaCyc:AT1G15950-MONOMER; -. DR BRENDA; 1.2.1.44; 399. DR SABIO-RK; Q9S9N9; -. DR UniPathway; UPA00711; -. DR PRO; PR:Q9S9N9; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9S9N9; baseline and differential. DR Genevisible; Q9S9N9; AT. DR GO; GO:0005829; C:cytosol; IDA:TAIR. DR GO; GO:0016621; F:cinnamoyl-CoA reductase activity; IDA:TAIR. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB. DR GO; GO:0009809; P:lignin biosynthetic process; IDA:TAIR. DR GO; GO:0009409; P:response to cold; IEP:TAIR. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR001509; Epimerase_deHydtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Lignin biosynthesis; NADP; KW Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1 344 Cinnamoyl-CoA reductase 1. FT /FTId=PRO_0000418212. FT NP_BIND 17 23 NADP. {ECO:0000250|UniProtKB:P51110}. FT NP_BIND 68 69 NADP. {ECO:0000250|UniProtKB:P51110}. FT NP_BIND 88 90 NADP. {ECO:0000250|UniProtKB:P51110}. FT NP_BIND 188 191 NADP. {ECO:0000250|UniProtKB:P51110}. FT ACT_SITE 165 165 Proton donor. FT {ECO:0000250|UniProtKB:Q12068}. FT BINDING 42 42 NADP. {ECO:0000250|UniProtKB:P51110}. FT BINDING 165 165 NADP. {ECO:0000250|UniProtKB:P51110}. FT BINDING 203 203 NADP. {ECO:0000250|UniProtKB:P51110}. FT MOD_RES 7 7 Phosphoserine. FT {ECO:0000244|PubMed:19376835}. FT CONFLICT 302 302 F -> L (in Ref. 1; AAG46037). FT {ECO:0000305}. FT CONFLICT 309 309 L -> F (in Ref. 1; AAG46037). FT {ECO:0000305}. SQ SEQUENCE 344 AA; 37489 MW; F6580F3D849B5A46 CRC64; MPVDVASPAG KTVCVTGAGG YIASWIVKIL LERGYTVKGT VRNPDDPKNT HLRELEGGKE RLILCKADLQ DYEALKAAID GCDGVFHTAS PVTDDPEQMV EPAVNGAKFV INAAAEAKVK RVVITSSIGA VYMDPNRDPE AVVDESCWSD LDFCKNTKNW YCYGKMVAEQ AAWETAKEKG VDLVVLNPVL VLGPPLQPTI NASLYHVLKY LTGSAKTYAN LTQAYVDVRD VALAHVLVYE APSASGRYLL AESARHRGEV VEILAKLFPE YPLPTKCKDE KNPRAKPYKF TNQKIKDLGL EFTSTKQSLY DTVKSLQEKG HLAPPPPPPS ASQESVENGI KIGS //