CCR1_ORYSJ
ID CCR1_ORYSJ Reviewed; 338 AA.
AC Q6K9A2;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cinnamoyl-CoA reductase 1 {ECO:0000305};
DE Short=OsCCR1 {ECO:0000303|PubMed:16380417};
DE EC=1.2.1.44 {ECO:0000269|PubMed:16380417};
GN Name=CCR1 {ECO:0000303|PubMed:16380417};
GN OrderedLocusNames=Os02g0808800 {ECO:0000312|EMBL:BAF10374.1},
GN LOC_Os02g56460 {ECO:0000305};
GN ORFNames=OJ1112_G06.14 {ECO:0000312|EMBL:BAD19133.1},
GN OJ1520_C09.26 {ECO:0000312|EMBL:BAD19248.1},
GN OsJ_08807 {ECO:0000312|EMBL:EAZ25022.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH RAC1,
RP SUBCELLULAR LOCATION, AND INDUCTION BY SPHINGOLIPID ELICITOR.
RX PubMed=16380417; DOI=10.1073/pnas.0509875103;
RA Kawasaki T., Koita H., Nakatsubo T., Hasegawa K., Wakabayashi K.,
RA Takahashi H., Umemura K., Umezawa T., Shimamoto K.;
RT "Cinnamoyl-CoA reductase, a key enzyme in lignin biosynthesis, is an
RT effector of small GTPase Rac in defense signaling in rice.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:230-235(2006).
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 cinnamaldehydes.
CC Probably involved in the formation of lignin in defense responses.
CC {ECO:0000269|PubMed:16380417}.
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:16380417};
CC -!- ACTIVITY REGULATION: Activated by the small GTPase RAC1.
CC {ECO:0000269|PubMed:16380417}.
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Interacts with RAC1 in a GTP-dependent manner.
CC {ECO:0000269|PubMed:16380417}.
CC -!- INTERACTION:
CC Q6K9A2; Q9SSX0: RAC1; NbExp=3; IntAct=EBI-15561872, EBI-15561891;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16380417}.
CC -!- INDUCTION: By sphingolipid elicitor (SE).
CC {ECO:0000269|PubMed:16380417}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; AP003996; BAD19133.1; -; Genomic_DNA.
DR EMBL; AP004064; BAD19248.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF10374.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS81500.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ25022.1; -; Genomic_DNA.
DR EMBL; AK064401; BAG89093.1; -; mRNA.
DR RefSeq; XP_015622902.1; XM_015767416.1.
DR AlphaFoldDB; Q6K9A2; -.
DR SMR; Q6K9A2; -.
DR DIP; DIP-61087N; -.
DR IntAct; Q6K9A2; 1.
DR STRING; 4530.OS02T0808800-01; -.
DR PaxDb; Q6K9A2; -.
DR PRIDE; Q6K9A2; -.
DR EnsemblPlants; Os02t0808800-01; Os02t0808800-01; Os02g0808800.
DR GeneID; 4331085; -.
DR Gramene; Os02t0808800-01; Os02t0808800-01; Os02g0808800.
DR KEGG; osa:4331085; -.
DR eggNOG; KOG1502; Eukaryota.
DR HOGENOM; CLU_007383_9_0_1; -.
DR InParanoid; Q6K9A2; -.
DR OMA; ADCKNAH; -.
DR OrthoDB; 848823at2759; -.
DR UniPathway; UPA00711; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016621; F:cinnamoyl-CoA reductase activity; IDA: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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009809; P:lignin biosynthetic process; IDA:UniProtKB.
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 Cytoplasm; Disulfide bond; Lignin biosynthesis; NADP; Oxidoreductase;
KW Plant defense; Reference proteome.
FT CHAIN 1..338
FT /note="Cinnamoyl-CoA reductase 1"
FT /id="PRO_0000437027"
FT ACT_SITE 169
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 22..28
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 73..74
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 93..95
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 169
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 192..195
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 207
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT DISULFID 158..166
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
SQ SEQUENCE 338 AA; 37390 MW; B1C9611FE897BFD0 CRC64;
MSSNFEANNN NNGEKQLVCV TGAGGFIGSW VVKELLIRGY HVRGTARDPA DSKNAHLLEL
EGADERLSLC RADVLDAASL RAAFSGCHGV FHVASPVSND PDLVPVAVEG TRNVINAAAD
MGVRRVVFTS SYGAVHMNPN RSPDAVLDET CWSDYEFCKQ TDNLYCCAKM MAEMTATEEA
AKRGLELAVV VPSMTMGPML QQTLNFSTNH VARYLMGTKK SYPNAVAAYV DVRDVARAHV
LVYERPEARG RYLCIGTVLH RAELLRMLRE LFPRYPATAK CEDDGKPMAK PYKFSNQRLK
DLGLEFTPLR KSLNEAVLCM QQKGHLPLIY PVPKRAYL
