ID I1QR60_ORYGL Unreviewed; 577 AA.
AC I1QR60;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=4-coumarate--CoA ligase {ECO:0000256|ARBA:ARBA00012959};
DE EC=6.2.1.12 {ECO:0000256|ARBA:ARBA00012959};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA09G0153900.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA09G0153900.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) 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; I1QR60; -.
DR STRING; 4538.I1QR60; -.
DR EnsemblPlants; ORGLA09G0153900.1; ORGLA09G0153900.1; ORGLA09G0153900.
DR Gramene; ORGLA09G0153900.1; ORGLA09G0153900.1; ORGLA09G0153900.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_5_1; -.
DR OMA; FKCPRRV; -.
DR Proteomes; UP000007306; Unassembled WGS sequence.
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:SF12; OS09G0555800 PROTEIN; 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;
FT DOMAIN 21..409
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 459..538
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 557..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 62925 MW; E86C0B86B646164B CRC64;
MDSLPKRDAN YVPLSPITFL HRAASVYADR TSVVYGATSF TWRQTHHRCL RLAAALQSLA
VSKNDVVSVI APNTPALYEM HFAVPMAGAV LNAINTRLDA ANVAAIVRHA EPKVLFVDYQ
FIRVATDALK AVMGDGDGDG GEVRAPLPLL VVIDDADKPT GARVGELEYE QLVARGDPAR
YPPRPVEDEW DAVALNYTSG TTSAPKGVVY SHRGAYLNTM GLLLQWGVGH EPVYLWSLPM
FHCNGWTFTW GVAARGGTNV CIRAPTADAM YAAFAAHGVT HMCAAPVLFN ILLDGVCREP
LRRPVEVLTG GAPPPAALLE RVERLGFHVT HAYGMTEATG VVMVCEWREQ WDALLPSERA
RLKARQGVSA LTLADADVKD LKTMESVPRD GATMGEVVLR GSNVMKGYFK NPRATADAFR
DGWFLTGDVG VVHPDGYVEI KDRSKDVIIS GGENISSVEV EAALYQHPAV REAAVVAMPH
PHWGETPCAF VSLKREFAGT GEVSEQEVVS FCRNRMAHYM VPRKVVFVDE LPKNSTGKVQ
KLALRDMARR LRLRAPDKAR PVAAPARHGP LTQTARL
//
