ID I1HA56_BRADI Unreviewed; 596 AA.
AC I1HA56;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=4-coumarate--CoA ligase {ECO:0000256|ARBA:ARBA00012959};
DE EC=6.2.1.12 {ECO:0000256|ARBA:ARBA00012959};
GN Name=100831811 {ECO:0000313|EnsemblPlants:KQK23834};
GN ORFNames=BRADI_1g76430v3 {ECO:0000313|EMBL:KQK23834.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK23834.1};
RN [1] {ECO:0000313|EMBL:KQK23834.1, ECO:0000313|EnsemblPlants:KQK23834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK23834.1,
RC ECO:0000313|EnsemblPlants:KQK23834};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQK23834.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK23834.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK23834}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK23834};
RG EnsemblPlants;
RL Submitted (AUG-2018) 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 EMBL; CM000880; KQK23834.1; -; Genomic_DNA.
DR RefSeq; XP_010229258.1; XM_010230956.2.
DR AlphaFoldDB; I1HA56; -.
DR STRING; 15368.I1HA56; -.
DR EnsemblPlants; KQK23834; KQK23834; BRADI_1g76430v3.
DR GeneID; 100831811; -.
DR Gramene; KQK23834; KQK23834; BRADI_1g76430v3.
DR KEGG; bdi:100831811; -.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_5_1; -.
DR InParanoid; I1HA56; -.
DR OMA; FYYTANG; -.
DR OrthoDB; 2596785at2759; -.
DR Proteomes; UP000008810; Chromosome 1.
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:UP000008810}.
FT DOMAIN 22..408
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 458..539
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 548..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 64635 MW; DF52679B8061FB20 CRC64;
MEQLPKRAAN YVPLSPVGFL PRANAVYGDR TSLVYGRRVR FTWSQTHDRC RRLASSLLAL
GVRKNDVVSV LAPNVPAMYE MHFAVPMAGA VLNTVNTRLD AKAVAAILRH SEAKLFFVDY
EYVRLASDAL QLLVSDGASQ VPLVAVIDDL DRPTGVRLGE LEYEGLVSRG DPTVQLPMLA
DEWDAVTLNY TSGTTSAPKG VVYSHRGAYL STTSLLMSWE MGAEPVYLWT LPMFHCNGWT
FTWGVAARGG VNVCIRDARA ADVYGAIARH GVTHMCCAPV VFNILLEGAA ATSAPNQRQL
AAPVHVLTGG APPPAALLER VERIGFHVTH AYGLTEATGP ALACEWRAQW DHLPVSDRAR
LKARQGVSVL SLADADVINE DTMSSVQRDG KALGEIVLRG SSVMKGYLKN PEANEAAFKG
GWFMTGDVGV VHPDGYIEIK DRSKDVIISG GENICSKEVE EALFAHPAVA DAAVVAMPHP
HWGETPCAFV VPRKKEDGDQ NVQVCEEEVV DFCRKRMARF MVPRKVVLCE ALPRNALGKV
EKVKLRDAAR KLQPAPAQKT TTSNSKGSTK APAGKSGGGR RDEQNPVAHV MAMSRL
//
