ID A0A3B6JNV4_WHEAT Unreviewed; 551 AA.
AC A0A3B6JNV4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=4-coumarate--CoA ligase {ECO:0000256|ARBA:ARBA00012959};
DE EC=6.2.1.12 {ECO:0000256|ARBA:ARBA00012959};
GN ORFNames=CFC21_063259 {ECO:0000313|EMBL:KAF7055777.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS4D02G323500.1};
RN [1] {ECO:0000313|EMBL:KAF7055777.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7055777.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS4D02G323500.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS4D02G323500.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS4D02G323500.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7055777.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7055777.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00034252};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19642;
CC Evidence={ECO:0000256|ARBA:ARBA00034252};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumarate + ATP + H(+) = (E)-4-coumaroyl-AMP +
CC diphosphate; Xref=Rhea:RHEA:72419, ChEBI:CHEBI:12876,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:192348; Evidence={ECO:0000256|ARBA:ARBA00034219};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72420;
CC Evidence={ECO:0000256|ARBA:ARBA00034219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumaroyl-AMP + CoA = (E)-4-coumaroyl-CoA + AMP + H(+);
CC Xref=Rhea:RHEA:72423, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:85008, ChEBI:CHEBI:192348, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000256|ARBA:ARBA00034223};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72424;
CC Evidence={ECO:0000256|ARBA:ARBA00034223};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; CM022222; KAF7055777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6JNV4; -.
DR SMR; A0A3B6JNV4; -.
DR STRING; 4565.A0A3B6JNV4; -.
DR PaxDb; 4565-Traes_4DL_BAA3F5089-1; -.
DR EnsemblPlants; TraesCS4D02G323500.1; TraesCS4D02G323500.1; TraesCS4D02G323500.
DR Gramene; TraesCAD_scaffold_010880_01G000300.1; TraesCAD_scaffold_010880_01G000300.1; TraesCAD_scaffold_010880_01G000300.
DR Gramene; TraesCLE_scaffold_013604_01G001100.1; TraesCLE_scaffold_013604_01G001100.1; TraesCLE_scaffold_013604_01G001100.
DR Gramene; TraesCS4D02G323500.1; TraesCS4D02G323500.1; TraesCS4D02G323500.
DR Gramene; TraesCS4D03G0754000.1; TraesCS4D03G0754000.1.CDS; TraesCS4D03G0754000.
DR Gramene; TraesKAR4D01G0350330.1; cds.TraesKAR4D01G0350330.1; TraesKAR4D01G0350330.
DR Gramene; TraesPAR_scaffold_012472_01G000300.1; TraesPAR_scaffold_012472_01G000300.1; TraesPAR_scaffold_012472_01G000300.
DR Gramene; TraesROB_scaffold_008682_01G000300.1; TraesROB_scaffold_008682_01G000300.1; TraesROB_scaffold_008682_01G000300.
DR OMA; AREMEHQ; -.
DR OrthoDB; 1404660at2759; -.
DR Proteomes; UP000019116; Chromosome 4D.
DR Proteomes; UP000815260; Chromosome 4D.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0106290; F:trans-cinnamate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProt.
DR CDD; cd05904; 4CL; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR24096:SF413; 4-COUMARATE--COA LIGASE-LIKE 5; 1.
DR PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 252..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..411
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 462..537
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 551 AA; 59036 MW; 8760C2585A09E253 CRC64;
MATAAAAADP RSGYCAATGA FRSKRAEVPL PAGRDLDVVT FLASRRHSGV VALVDASTGR
RTTFAELWRA VAGAATALAA PPFGLRKGHV ALILSPNSVH FPVAALAAMS LGAVVTTANP
LNTAAEVAKQ VADARPVLAF TTRDLLPKLP RAADGLRVVL LESSSSPAPA DPRIVATIDE
ISATAPDPAR RRDRVTQDDQ ATLLYSSGTT GPSKGVVATH RNLISMVQIV MNRFRLEDSD
TTETFLCTVP MFHVYGLVAF ATGLLGCGAT IVVLSKFELP EMLRCISAYG VTYLPLVPPI
LVAMVAHPKP LPLGNLRKVL SGGAPLSKEL IEGFREKYPQ VEILQGYGLT ESTAIGASTD
SAEESRRYGT AGLLSPNTEA KIVDPDTGEA LPVNRTGELW IRGPYVMKGY FNNTEATQAT
VTPDGWLKTG DLCYIDEDGY LFVVDRLKEL IKYKGYQVPP AELEALLLTH PEVSDVAVIP
FPDRDVGQFP MAYVVRKKGS NLSAQEVMEF VAKQVAPYKK VRKVAFVTDI PKNASGKILR
KDLIKLATSK L
//
