CCR1_PETHY
ID CCR1_PETHY Reviewed; 333 AA.
AC A0A059TC02;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Cinnamoyl-CoA reductase 1 {ECO:0000303|PubMed:24985707, ECO:0000303|PubMed:25217505};
DE Short=PhCCR1 {ECO:0000303|PubMed:24985707, ECO:0000303|PubMed:25217505};
DE EC=1.2.1.44 {ECO:0000250|UniProtKB:Q9S9N9};
DE AltName: Full=Coniferylaldehyde synthase {ECO:0000305};
DE EC=1.2.1.- {ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505};
GN Name=CCR1 {ECO:0000303|PubMed:24985707, ECO:0000303|PubMed:25217505};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN
RP COMPLEX WITH NADP, FUNCTION, MUTAGENESIS OF CYS-150 AND CYS-158, DISULFIDE
RP BONDS, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND PATHWAY.
RX PubMed=25217505; DOI=10.1105/tpc.114.127399;
RA Pan H., Zhou R., Louie G.V., Muhlemann J.K., Bomati E.K., Bowman M.E.,
RA Dudareva N., Dixon R.A., Noel J.P., Wang X.;
RT "Structural studies of cinnamoyl-CoA reductase and cinnamyl-alcohol
RT dehydrogenase, key enzymes of monolignol biosynthesis.";
RL Plant Cell 26:3709-3727(2014).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INDUCTION, AND PATHWAY.
RC STRAIN=cv. Mitchell;
RX PubMed=24985707; DOI=10.1111/nph.12913;
RA Muhlemann J.K., Woodworth B.D., Morgan J.A., Dudareva N.;
RT "The monolignol pathway contributes to the biosynthesis of volatile
RT phenylpropenes in flowers.";
RL New Phytol. 204:661-670(2014).
CC -!- FUNCTION: Involved in the latter stages of lignin biosynthesis
CC (PubMed:24985707). Catalyzes one of the last steps of monolignol
CC biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding
CC cinnamaldehydes (PubMed:25217505, PubMed:24985707). Mediates the
CC conversion of feruloyl CoA to coniferylaldehyde (PubMed:25217505,
CC PubMed:24985707). Also active toward p-coumaroyl-CoA and sinapoyl-CoA
CC (PubMed:25217505, PubMed:24985707). Involved in the production of
CC floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g.
CC cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with
CC the anthocyanin biosynthesis pathway involved in flower pigmentation
CC (PubMed:24985707). {ECO:0000269|PubMed:24985707,
CC ECO:0000269|PubMed:25217505}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-coniferaldehyde + CoA + NADP(+) = (E)-feruloyl-CoA + H(+)
CC + NADPH; Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:87305; EC=1.2.1.44;
CC Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64650;
CC Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumaraldehyde + CoA + NADP(+) = (E)-4-coumaroyl-CoA +
CC H(+) + NADPH; Xref=Rhea:RHEA:64652, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28353, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:85008; EC=1.2.1.44;
CC Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64654;
CC Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-sinapaldehyde + CoA + NADP(+) = (E)-sinapoyl-CoA + H(+) +
CC NADPH; Xref=Rhea:RHEA:64656, ChEBI:CHEBI:15378, ChEBI:CHEBI:27949,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57393, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.44;
CC Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64658;
CC Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505};
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:0000250|UniProtKB:Q9S9N9};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10622;
CC Evidence={ECO:0000250|UniProtKB:Q9S9N9};
CC -!- ACTIVITY REGULATION: Inhibited by sodium iodide-mediated oxidation.
CC {ECO:0000269|PubMed:25217505}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=208.6 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:25217505};
CC KM=307.6 uM for feruloyl-CoA {ECO:0000269|PubMed:25217505};
CC KM=270.3 uM for sinapoyl-CoA {ECO:0000269|PubMed:25217505};
CC Vmax=1235.7 nmol/sec/mg enzyme with p-coumaroyl-CoA as substrate
CC {ECO:0000269|PubMed:25217505};
CC Vmax=5713 nmol/sec/mg enzyme with feruloyl-CoA as substrate
CC {ECO:0000269|PubMed:25217505};
CC Vmax=3384.7 nmol/sec/mg enzyme with sinapoyl-CoA as substrate
CC {ECO:0000269|PubMed:25217505};
CC Note=kcat is 1.2 sec(-1) with p-coumaroyl-CoA as substrate
CC (PubMed:25217505). kcat is 5.8 sec(-1) with feruloyl-CoA as substrate
CC (PubMed:25217505). kcat is 3.4 sec(-1) with sinapoyl-CoA as substrate
CC (PubMed:25217505). {ECO:0000269|PubMed:25217505};
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:25217505};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24985707}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, leaves and stems.
CC {ECO:0000269|PubMed:24985707}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the scent-producing corollas
CC and tubes of two days old flowers, reaching a maximum at day three
CC post-anthesis, and, to a lower extent, in other floral tissues (e.g.
CC ovary, pistil, sepals and stamen). {ECO:0000269|PubMed:24985707}.
CC -!- INDUCTION: Circadian-regulation with peak levels occurring in flowers
CC during the light period, in the afternoon.
CC {ECO:0000269|PubMed:24985707}.
CC -!- PTM: The formation of a reversible disulfide bond reduces activity by
CC perturbing the positioning of nearby catalytic residues.
CC {ECO:0000269|PubMed:25217505}.
CC -!- DISRUPTION PHENOTYPE: No visible effect on the emission and internal
CC pools of phenylpropene and benzenoid compounds, but increased
CC accumulation of feruloyl-CoA, p-coumaroyl-CoA and vanillin
CC (PubMed:24985707). Reduced lignin content (PubMed:24985707).
CC {ECO:0000269|PubMed:24985707}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; KF040494; AHX56186.1; -; mRNA.
DR PDB; 4R1S; X-ray; 1.60 A; A/B=1-333.
DR PDB; 4R1T; X-ray; 1.70 A; A=1-333.
DR PDBsum; 4R1S; -.
DR PDBsum; 4R1T; -.
DR AlphaFoldDB; A0A059TC02; -.
DR SMR; A0A059TC02; -.
DR BRENDA; 1.2.1.44; 4700.
DR UniPathway; UPA00711; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016621; F:cinnamoyl-CoA reductase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009809; P:lignin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009699; P:phenylpropanoid 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 3D-structure; Cytoplasm; Disulfide bond; Lignin biosynthesis; NADP;
KW Nucleotide-binding; Oxidoreductase; Phenylpropanoid metabolism.
FT CHAIN 1..333
FT /note="Cinnamoyl-CoA reductase 1"
FT /id="PRO_0000451497"
FT ACT_SITE 161
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 13..19
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:25217505,
FT ECO:0007744|PDB:4R1S"
FT BINDING 38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:25217505,
FT ECO:0007744|PDB:4R1S"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:25217505,
FT ECO:0007744|PDB:4R1S"
FT BINDING 64..65
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:25217505,
FT ECO:0007744|PDB:4R1S"
FT BINDING 84..86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:25217505,
FT ECO:0007744|PDB:4R1S"
FT BINDING 157
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:25217505,
FT ECO:0007744|PDB:4R1S"
FT BINDING 161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:25217505,
FT ECO:0007744|PDB:4R1S"
FT BINDING 184..187
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:25217505,
FT ECO:0007744|PDB:4R1S"
FT BINDING 199
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:25217505,
FT ECO:0007744|PDB:4R1S"
FT DISULFID 150..158
FT /evidence="ECO:0000269|PubMed:25217505,
FT ECO:0007744|PDB:4R1T"
FT MUTAGEN 150
FT /note="C->A,S: Increased activity."
FT /evidence="ECO:0000269|PubMed:25217505"
FT MUTAGEN 158
FT /note="C->A: Increased activity."
FT /evidence="ECO:0000269|PubMed:25217505"
FT MUTAGEN 158
FT /note="C->S: Reduced activity."
FT /evidence="ECO:0000269|PubMed:25217505"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:4R1T"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4R1S"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:4R1S"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:4R1S"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:4R1S"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 92..112
FT /evidence="ECO:0007829|PDB:4R1S"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4R1S"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 156..175
FT /evidence="ECO:0007829|PDB:4R1S"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4R1S"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:4R1S"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:4R1S"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4R1T"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 224..236
FT /evidence="ECO:0007829|PDB:4R1S"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4R1S"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 253..263
FT /evidence="ECO:0007829|PDB:4R1S"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:4R1S"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:4R1S"
SQ SEQUENCE 333 AA; 36886 MW; 3D30717DEFB5287A CRC64;
MRSVSGQVVC VTGAGGFIAS WLVKILLEKG YTVRGTVRNP DDPKNGHLRE LEGAKERLTL
CKADLLDYQS LREAINGCDG VFHTASPVTD DPEQMVEPAV IGTKNVINAA AEANVRRVVF
TSSIGAVYMD PNRDPETVVD ETCWSDPDFC KNTKNWYCYG KMVAEQAAWE EAKEKGVDLV
VINPVLVQGP LLQTTVNASV LHILKYLTGS AKTYANSVQA YVDVKDVALA HILLYETPEA
SGRYLCAESV LHRGDVVEIL SKFFPEYPIP TKCSDVTKPR VKPYKFSNQK LKDLGLEFTP
VKQCLYETVK SLQEKGHLPI PTQKDEPIIR IQP
