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4CL1_PETHY
ID   4CL1_PETHY              Reviewed;         544 AA.
AC   I3PB37;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=4-coumarate:CoA ligase 1 {ECO:0000303|PubMed:22649270};
DE            Short=Ph-4CL1 {ECO:0000303|PubMed:22649270};
DE            Short=Ph4CL1 {ECO:0000303|PubMed:22649270};
DE            EC=6.2.1.12 {ECO:0000269|PubMed:22649270};
DE   AltName: Full=(E)-caffeate:CoA ligase 4CL1 {ECO:0000305};
DE            EC=6.2.1.- {ECO:0000269|PubMed:22649270};
DE   AltName: Full=Benzoate:CoA ligase 4CL1 {ECO:0000305};
DE            EC=6.2.1.25 {ECO:0000269|PubMed:22649270};
DE   AltName: Full=Trans-cinnamate:CoA ligase 4CL1 {ECO:0000305};
DE            EC=6.2.1.- {ECO:0000269|PubMed:22649270};
DE   AltName: Full=Trans-ferulate:CoA ligase 4CL1 {ECO:0000305};
DE            EC=6.2.1.- {ECO:0000269|PubMed:22649270};
GN   Name=4CL1 {ECO:0000303|PubMed:22649270};
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], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP   ACTIVITY, PATHWAY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION,
RP   SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
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: Catalyzes the formation of CoA esters of trans-cinnamic acid,
CC       4-coumaric acid, ferulic acid, benzoic acid and caffeic acid.
CC       {ECO:0000269|PubMed:22649270}.
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=ATP + benzoate + CoA = AMP + benzoyl-CoA + diphosphate;
CC         Xref=Rhea:RHEA:10132, ChEBI:CHEBI:16150, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57369,
CC         ChEBI:CHEBI:456215; EC=6.2.1.25;
CC         Evidence={ECO:0000269|PubMed:22649270};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10133;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-ferulate + ATP + CoA = (E)-feruloyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:36251, ChEBI:CHEBI:29749,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:87305, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:22649270};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36252;
CC         Evidence={ECO:0000269|PubMed:22649270};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=149.4 uM for trans-cinnamic acid {ECO:0000269|PubMed:22649270};
CC         KM=16.4 uM for 4-coumaric acid {ECO:0000269|PubMed:22649270};
CC         KM=47.8 uM for caffeic acid {ECO:0000269|PubMed:22649270};
CC         KM=15.2 uM for ferulic acid {ECO:0000269|PubMed:22649270};
CC         KM=9008 uM for benzoic acid {ECO:0000269|PubMed:22649270};
CC         KM=9.9 uM for CoA {ECO:0000269|PubMed:22649270};
CC         Vmax=14680 pmol/sec/mg enzyme with trans-cinnamic acid as substrate
CC         {ECO:0000269|PubMed:22649270};
CC         Vmax=25797 pmol/sec/mg enzyme with 4-coumaric acid as substrate
CC         {ECO:0000269|PubMed:22649270};
CC         Vmax=63200 pmol/sec/mg enzyme with caffeic acid as substrate
CC         {ECO:0000269|PubMed:22649270};
CC         Vmax=41377 pmol/sec/mg enzyme with ferulic acid as substrate
CC         {ECO:0000269|PubMed:22649270};
CC         Vmax=95.9 pmol/sec/mg enzyme with benzoic acid as substrate
CC         {ECO:0000269|PubMed:22649270};
CC         Vmax=8451 pmol/sec/mg enzyme with CoA acid as substrate
CC         {ECO:0000269|PubMed:22649270};
CC         Note=kcat is 0.847 sec(-1) with trans-cinnamic acid as substrate
CC         (PubMed:22649270). kcat is 1.488 sec(-1) with 4-coumaric acid as
CC         substrate (PubMed:22649270). kcat is 3.645 sec(-1) with caffeic acid
CC         as substrate (PubMed:22649270). kcat is 2.39 sec(-1) with ferulic
CC         acid as substrate (PubMed:22649270). kcat is 0.0007 sec(-1) with
CC         benzoic acid as substrate (PubMed:22649270). kcat is 0.487 sec(-1)
CC         with CoA as substrate (PubMed:22649270).
CC         {ECO:0000269|PubMed:22649270};
CC       pH dependence:
CC         Optimum pH is 8.5 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: Cytoplasm, cytosol {ECO:0000269|PubMed:22649270}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in flower organs, with highest
CC       levels in corollas, and, to a lesser extent, in tubes, sepals, pistils,
CC       stamen and ovaries (PubMed:22649270). Also present at low levels in
CC       leaves (PubMed:22649270). {ECO:0000269|PubMed:22649270}.
CC   -!- INDUCTION: Circadian-regulation with peak levels occurring late
CC       afternoon (e.g. 3 to 7 pm). {ECO:0000269|PubMed:22649270}.
CC   -!- DISRUPTION PHENOTYPE: Normal benzenoid scent profile in flowers.
CC       {ECO:0000269|PubMed:22649270}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; JN120849; AEO52694.1; -; mRNA.
DR   AlphaFoldDB; I3PB37; -.
DR   SMR; I3PB37; -.
DR   UniPathway; UPA00372; UER00547.
DR   UniPathway; UPA00713; -.
DR   GO; GO:0005829; C:cytosol; 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:0018858; F:benzoate-CoA ligase activity; IDA:UniProtKB.
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:0050563; F:trans-feruloyl-CoA synthase 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:0033494; P:ferulate metabolic process; IDA:UniProtKB.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; IDA:UniProtKB.
DR   GO; GO:0052315; P:phytoalexin biosynthetic process; IDA: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   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Phenylpropanoid metabolism.
FT   CHAIN           1..544
FT                   /note="4-coumarate:CoA ligase 1"
FT                   /id="PRO_0000451515"
SQ   SEQUENCE   544 AA;  59610 MW;  F94DDC67735D5F28 CRC64;
     MPMETETNQG DLIFRSKLPD IYIPKHLPLH SYCFENISEF SSRPCLINGA NNHIYTYADV
     ELTSRKVAAG LNKLGIQQKD TIMILLPNSP EFVFAFMGAS YLGAISTMAN PLFTPAEVVK
     QAKASNAKLI ITQACFVNKV KDYAFDNNLN VICIDSAPEG CIHFSELTQA DEHDIPDVKI
     QSDDVVALPY SSGTTGLPKG VMLTHKGLVT SVAQQVDGEN ANLYMHSEDV LMCVLPLFHI
     YSLNSVLLCG LRVGAAILIM QKFDIVQFCE LIEKYKVTIG PFVPPIVLAI AKSPVVDNYD
     LSSVRTVMSG AAPLGKELED AVRIKFPNAK LGQGYGMTEA GPVLAMCLAF AKEPFDIKSG
     ACGTVVRNAE MKIVDPDTGC SLPRNQPGEI CIRGDQIMKG YLNDPAATTR TIDKEGWLHT
     GDIGYIDNDD ELFIVDRLKE LIKYKGFQVA PAELEALLLN HPNISDAAVV PMKDEQAGEV
     PVAFVVRSNG SDITEDEVKD FVSKQVIFYK RIKRVFFVET VPKSPSGKIL RKDLRARLAA
     GVPN
 
 
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