CNL_PETHY
ID CNL_PETHY Reviewed; 570 AA.
AC I3PB36; J9Q6B2;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Trans-cinnamate:CoA ligase, peroxisomal {ECO:0000305};
DE Short=Cinnamic acid:CoA ligase {ECO:0000303|PubMed:22649270};
DE Short=Ph-CNL {ECO:0000303|PubMed:22649270};
DE Short=PhCNL {ECO:0000303|PubMed:22649270};
DE EC=6.2.1.- {ECO:0000269|PubMed:22649270, ECO:0000269|PubMed:22771854};
DE AltName: Full=(E)-caffeate:CoA ligase CNL {ECO:0000305};
DE EC=6.2.1.- {ECO:0000269|PubMed:22649270};
DE AltName: Full=4-coumarate:CoA ligase CNL {ECO:0000303|PubMed:22649270};
DE EC=6.2.1.12 {ECO:0000269|PubMed:22649270, ECO:0000269|PubMed:22771854};
DE AltName: Full=Protein ACYL-ACTIVATING ENZYME {ECO:0000303|PubMed:22771854};
DE Short=PhAAE {ECO:0000303|PubMed:22771854};
GN Name=CNL {ECO:0000303|PubMed:22649270};
GN Synonyms=AAE {ECO:0000303|PubMed:22771854};
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] (ISOFORM 2), FUNCTION, DISRUPTION PHENOTYPE,
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, REPRESSION BY
RP ETHYLENE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Mitchell;
RX PubMed=22771854; DOI=10.1093/jxb/ers153;
RA Colquhoun T.A., Marciniak D.M., Wedde A.E., Kim J.Y., Schwieterman M.L.,
RA Levin L.A., Van Moerkercke A., Schuurink R.C., Clark D.G.;
RT "A peroxisomally localized acyl-activating enzyme is required for volatile
RT benzenoid formation in a Petuniaxhybrida cv. 'Mitchell Diploid' flower.";
RL J. Exp. Bot. 63:4821-4833(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE,
RP CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP INDUCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC STRAIN=cv. Mitchell;
RX PubMed=22649270; DOI=10.1105/tpc.112.097519;
RA Klempien A., Kaminaga Y., Qualley A., Nagegowda D.A., Widhalm J.R.,
RA Orlova I., Shasany A.K., Taguchi G., Kish C.M., Cooper B.R., D'Auria J.C.,
RA Rhodes D., Pichersky E., Dudareva N.;
RT "Contribution of CoA ligases to benzenoid biosynthesis in petunia
RT flowers.";
RL Plant Cell 24:2015-2030(2012).
CC -!- FUNCTION: Involved in the biosynthesis of floral volatile
CC benzenoid/phenylpropanoid (FVBP) scent (e.g. benzylbenzoate,
CC phenylethylbenzoate, and methylbenzoate) (PubMed:22771854,
CC PubMed:22649270). Catalyzes the formation of CoA esters of cinnamic
CC acid, and, with lower efficiency, of 4-coumaric acid and caffeic acid
CC (PubMed:22649270). {ECO:0000269|PubMed:22649270,
CC ECO:0000269|PubMed:22771854}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:19641, ChEBI:CHEBI:12876,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:85008, ChEBI:CHEBI:456215; EC=6.2.1.12;
CC Evidence={ECO:0000269|PubMed:22649270};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19642;
CC Evidence={ECO:0000269|PubMed:22649270};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-caffeate + ATP + CoA = (E)-caffeoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:36299, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57770,
CC ChEBI:CHEBI:87136, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:22649270};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36300;
CC Evidence={ECO:0000269|PubMed:22649270};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamate + ATP + CoA = (E)-cinnamoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:64788, ChEBI:CHEBI:15669,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57252,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:22649270};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64789;
CC Evidence={ECO:0000269|PubMed:22649270};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:22649270};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=285.7 uM for trans-cinnamic acid {ECO:0000269|PubMed:22649270};
CC KM=550.4 uM for 4-coumaric acid {ECO:0000269|PubMed:22649270};
CC KM=1024.4 uM for caffeic acid {ECO:0000269|PubMed:22649270};
CC KM=775.2 uM for CoA {ECO:0000269|PubMed:22649270};
CC Vmax=7401.7 pmol/sec/mg enzyme with trans-cinnamic acid as substrate
CC {ECO:0000269|PubMed:22649270};
CC Vmax=3890.7 pmol/sec/mg enzyme with 4-coumaric acid as substrate
CC {ECO:0000269|PubMed:22649270};
CC Vmax=3742.7 pmol/sec/mg enzyme with caffeic acid as substrate
CC {ECO:0000269|PubMed:22649270};
CC Vmax=7179.7 pmol/sec/mg enzyme with CoA acid as substrate
CC {ECO:0000269|PubMed:22649270};
CC Note=kcat is 0.472 sec(-1) with trans-cinnamic acid as substrate
CC (PubMed:22649270). kcat is 0.248 sec(-1) with 4-coumaric acid as
CC substrate (PubMed:22649270). kcat is 0.238 sec(-1) with caffeic acid
CC as substrate (PubMed:22649270). kcat is 0.458 sec(-1) with CoA as
CC substrate (PubMed:22649270). {ECO:0000269|PubMed:22649270};
CC pH dependence:
CC Optimum pH is 8 with cinnamic acid as a substrate.
CC {ECO:0000269|PubMed:22649270};
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis.
CC {ECO:0000269|PubMed:22649270}.
CC -!- PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene
CC biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step
CC 1/2. {ECO:0000269|PubMed:22649270}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22649270}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:22649270,
CC ECO:0000269|PubMed:22771854}. Note=Located in the peroxisomes of flower
CC petal limb cells. {ECO:0000269|PubMed:22771854}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=I3PB36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=I3PB36-2; Sequence=VSP_060792, VSP_060793;
CC -!- TISSUE SPECIFICITY: Mostly expressed in flower organs, with highest
CC levels in corollas and petal limbs, and, to a lesser extent, in petal
CC tubes, sepals, pistils, stamen, stigma, anthers and ovaries
CC (PubMed:22771854, PubMed:22649270). Also present at low levels in
CC leaves, stems and roots (PubMed:22771854, PubMed:22649270).
CC {ECO:0000269|PubMed:22649270, ECO:0000269|PubMed:22771854}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during flower development with highest
CC levels in open flowers, and fades out as flowers are senescing.
CC {ECO:0000269|PubMed:22771854}.
CC -!- INDUCTION: Circadian-regulation with peak levels occurring late
CC afternoon (e.g. 3 to 7 pm) (PubMed:22649270). Repressed by ethylene,
CC especially in senescing flowers (PubMed:22771854).
CC {ECO:0000269|PubMed:22649270, ECO:0000269|PubMed:22771854}.
CC -!- DISRUPTION PHENOTYPE: Disturbed benzenoid scent profile in flowers
CC characterized by a decreased emission of benzylbenzoate,
CC phenylethylbenzoate, and methylbenzoate. {ECO:0000269|PubMed:22649270,
CC ECO:0000269|PubMed:22771854}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; JQ031717; AFK25809.1; -; mRNA.
DR EMBL; JN120848; AEO52693.1; -; mRNA.
DR AlphaFoldDB; I3PB36; -.
DR SMR; I3PB36; -.
DR BioCyc; MetaCyc:MON-17854; -.
DR UniPathway; UPA00372; UER00547.
DR UniPathway; UPA00713; -.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0106286; F:(E)-caffeate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IDA:UniProtKB.
DR GO; GO:0106290; F:trans-cinnamate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0009800; P:cinnamic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009803; P:cinnamic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IDA:UniProtKB.
DR GO; GO:0052315; P:phytoalexin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Ligase; Nucleotide-binding; Peroxisome;
KW Phenylpropanoid metabolism.
FT CHAIN 1..570
FT /note="Trans-cinnamate:CoA ligase, peroxisomal"
FT /id="PRO_0000451514"
FT MOTIF 568..570
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT VAR_SEQ 512
FT /note="C -> L (in isoform 2)"
FT /id="VSP_060792"
FT VAR_SEQ 513..570
FT /note="Missing (in isoform 2)"
FT /id="VSP_060793"
FT CONFLICT 429
FT /note="L -> F (in Ref. 1; AFK25809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 63740 MW; 0DC0931B58788E4F CRC64;
MDELPKCGAN YVPLTPLTFL TRAFKSYANR TSIIYAGARF TWEQTYKRCC RLASSLQSLN
IVKNDVVSVL APNVPATYEM HFAVPMAGAV LNTINTRLDP MNIAIILKHS EAKLLFVDYE
YLEKARKALE LLMSTNFITA QNSKKISMPQ VILIDDLYSP TRIQQQDQLE YEQLVHQGNP
EYAPENIVDD EWDPIVLNYT SGTTSEPKGV VYSHRGAFLS TLNTIMGWEM GTEPVYLWSL
PMFHINGWTL TWGIAARGGT NVCIRNTTAQ EIYSNITLHK VTHMCCAPTV FNILLEAKPH
ERREITTPVQ VMVGGAPPPT TLIGKIEELG FHVVHCYGIT EAGGTTLVCE WQSEWNKLSR
EDQANLKARQ GISVLALEDV DVKNSKTMQS VPHNGKTMGE ICLRGSSIMK GYFKNDKANS
QVFKNGWFLT GDVAVIHQDG YLEIKDRCKD IIISGGENIS SIEVENAILK HPSVIEAAVV
AMPHPRWGET PCAFVIKTKN PEIKEADIIV HCKKELPGFM VPKHVQFLEE LPKTGTGKVK
KLQLREMAKS FGIFDNANQT SQILDLPARL
