CCR2_ARATH
ID CCR2_ARATH Reviewed; 332 AA.
AC Q9SAH9; Q8LBL0; Q9C5Y1;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cinnamoyl-CoA reductase 2;
DE Short=AtCCR2;
DE EC=1.2.1.44;
GN Name=CCR2; OrderedLocusNames=At1g80820; ORFNames=F23A5.17;
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, TISSUE SPECIFICITY, AND INDUCTION.
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 infection
RT with pathogenic bacteria.";
RL Phytochemistry 57:1187-1195(2001).
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., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis 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 reference
RT 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., 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 [5]
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., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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.
CC -!- FUNCTION: Cinnamoyl-CoA reductase probably involved in the formation of
CC phenolic compounds associated with the hypersensitive response. Seems
CC not to be involved in lignin biosynthesis.
CC {ECO:0000269|PubMed:11430991}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamaldehyde + CoA + NADP(+) = (E)-cinnamoyl-CoA + H(+)
CC + NADPH; Xref=Rhea:RHEA:10620, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731,
CC ChEBI:CHEBI:57252, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.44;
CC Evidence={ECO:0000269|PubMed:11430991};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.7 uM for feruloyl-CoA {ECO:0000269|PubMed:11430991};
CC KM=30.7 uM for sinapoyl-CoA {ECO:0000269|PubMed:11430991};
CC KM=5.16 uM for caffeoyl-CoA {ECO:0000269|PubMed:11430991};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in leaves, stems and
CC flowers. {ECO:0000269|PubMed:11430991}.
CC -!- INDUCTION: By the bacterial pathogen X.campestris.
CC {ECO:0000269|PubMed:11430991}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; AF320623; AAG53687.1; -; mRNA.
DR EMBL; AC011713; AAF14669.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36454.1; -; Genomic_DNA.
DR EMBL; BT005826; AAO64761.1; -; mRNA.
DR EMBL; AK227576; BAE99569.1; -; mRNA.
DR EMBL; AY087148; AAM64706.1; -; mRNA.
DR PIR; G96840; G96840.
DR RefSeq; NP_178197.1; NM_106730.4.
DR AlphaFoldDB; Q9SAH9; -.
DR SMR; Q9SAH9; -.
DR STRING; 3702.AT1G80820.1; -.
DR PaxDb; Q9SAH9; -.
DR PRIDE; Q9SAH9; -.
DR ProteomicsDB; 222793; -.
DR DNASU; 844421; -.
DR EnsemblPlants; AT1G80820.1; AT1G80820.1; AT1G80820.
DR GeneID; 844421; -.
DR Gramene; AT1G80820.1; AT1G80820.1; AT1G80820.
DR KEGG; ath:AT1G80820; -.
DR Araport; AT1G80820; -.
DR TAIR; locus:2025832; AT1G80820.
DR eggNOG; KOG1502; Eukaryota.
DR HOGENOM; CLU_007383_9_0_1; -.
DR OrthoDB; 848823at2759; -.
DR PhylomeDB; Q9SAH9; -.
DR SABIO-RK; Q9SAH9; -.
DR UniPathway; UPA00711; -.
DR PRO; PR:Q9SAH9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SAH9; baseline and differential.
DR Genevisible; Q9SAH9; AT.
DR GO; GO:0016621; F:cinnamoyl-CoA reductase activity; IDA:TAIR.
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:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0042754; P:negative regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; NADP; Oxidoreductase; Plant defense; Reference proteome.
FT CHAIN 1..332
FT /note="Cinnamoyl-CoA reductase 2"
FT /id="PRO_0000418213"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 12..18
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 43
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 63..64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 83..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 156
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 160
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 183..186
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT DISULFID 149..157
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT CONFLICT 2
FT /note="L -> P (in Ref. 6; AAM64706)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="T -> A (in Ref. 6; AAM64706)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="L -> F (in Ref. 1; AAG53687)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="H -> D (in Ref. 1; AAG53687)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="S -> Y (in Ref. 6; AAM64706)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="S -> P (in Ref. 6; AAM64706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 36618 MW; 25D5160F54DAF5A7 CRC64;
MLVDGKLVCV TGAGGYIASW IVKLLLERGY TVRGTVRNPT DPKNNHLREL QGAKERLTLH
SADLLDYEAL CATIDGCDGV FHTASPMTDD PETMLEPAVN GAKFVIDAAA KAKVKRVVFT
SSIGAVYMNP NRDTQAIVDE NCWSDLDFCK NTKNWYCYGK MLAEQSAWET AKAKGVDLVV
LNPVLVLGPP LQSAINASLV HILKYLTGSA KTYANLTQVY VDVRDVALGH VLVYEAPSAS
GRYILAETAL HRGEVVEILA KFFPEYPLPT KCSDEKNPRA KPYKFTTQKI KDLGLEFKPI
KQSLYESVKS LQEKGHLPLP QDSNQNEVII ES
