ID A0A453J1R3_AEGTS Unreviewed; 567 AA.
AC A0A453J1R3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=4-coumarate--CoA ligase {ECO:0000256|ARBA:ARBA00012959};
DE EC=6.2.1.12 {ECO:0000256|ARBA:ARBA00012959};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET4Gv20768200.2, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET4Gv20768200.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
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 AlphaFoldDB; A0A453J1R3; -.
DR EnsemblPlants; AET4Gv20768200.2; AET4Gv20768200.2; AET4Gv20768200.
DR Gramene; AET4Gv20768200.2; AET4Gv20768200.2; AET4Gv20768200.
DR Proteomes; UP000015105; Chromosome 4D.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0106290; F:trans-cinnamate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProt.
DR CDD; cd12118; ttLC_FACS_AEE21_like; 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; PTHR43859; ACYL-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR43859:SF2; BUTYRATE--COA LIGASE AAE11, PEROXISOMAL; 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 Reference proteome {ECO:0000313|Proteomes:UP000015105}.
FT DOMAIN 22..403
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 453..529
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 567 AA; 61272 MW; ED3DB0FE843850EE CRC64;
MDQLPKLAAN YAPLSPVGFL PRANAVYGDR ASLVYGRVRF TWSQTHERCR RLASSLLLTL
GVRKNDVVSV LAPNVPALYE MHFAVPMAGA VLNTVNTRLD AAAVAAILRH AEAKLFFVDY
DYVRLASDAL QLLAAAGAPV PLVAVIDDLD RPTGVRLGEL EYEALVAHGD PTVELPQLQD
EWDAVTLNYT SGTTSAPKGV VYSHRGAYLS TTSLLMSWEV GTEPVYLWTL PMFHCNGWTF
TWGMAARGGV NVCIRENRPA EVYRAIARYG VTHMCCAPVV FNILLEGGDA TARLAKPVNV
LTGGAPPPAA LLERVEKIGF NVTHAYGLTE ATGPALACEW RAQWDNLPIS ERARLKARQG
VSVLSLADAD VVTDDDAMAR VPRDGKTLGE IVLRGSSIMK GYLNNPEANA QAFRGGWFMT
GDVGVVHPDG YIEIKDRSKD VIISGGENIC SKEVEEALFR HPAVADAAVV AMPHAHWGET
PCAFVVAKDK AAGVCEDDVM AFCRKRMSRF MVPKKVVVWD VLPRNALGKV EKVKLREEAR
KLVPAVAVAP APGRAPGGAS HGHVKAI
//
