ID A0A0D3GBZ5_9ORYZ Unreviewed; 1081 AA.
AC A0A0D3GBZ5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=4-coumarate--CoA ligase {ECO:0000256|ARBA:ARBA00012959};
DE EC=6.2.1.12 {ECO:0000256|ARBA:ARBA00012959};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART06G00740.4};
RN [1] {ECO:0000313|EnsemblPlants:OBART06G00740.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART06G00740.4};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART06G00740.4}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-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 -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR AlphaFoldDB; A0A0D3GBZ5; -.
DR EnsemblPlants; OBART06G00740.4; OBART06G00740.4; OBART06G00740.
DR Gramene; OBART06G00740.4; OBART06G00740.4; OBART06G00740.
DR Proteomes; UP000026960; Chromosome 6.
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 Gene3D; 2.40.10.480; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR036736; ACP-like_sf.
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 InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR44394; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR44394:SF1; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13360; PQQ_2; 2.
DR Pfam; PF13570; PQQ_3; 1.
DR SMART; SM00564; PQQ; 5.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000026960}.
FT DOMAIN 97..216
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 217..344
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 1081 AA; 118072 MW; 36E38A19F649B342 CRC64;
MAAEAAAAKE EEPCCISHAF DRAARRNPTG LAVIHAASSS SSGSDSERRF TCADLLAAVS
TLSRHIAAEL SSSTSRHRDE SPGCSGRPVE AAAAPRVVGV YASPSVEYIA AVLAVLRCGE
AFLPLDPSWP EERIRWATSS SNAVLVVSSG GLGAAHVFAS SSCSVIHMDD DLWQVFEDEK
GGIGRDELAW PCECKKPREF CYVMFTSGST GKPKGAYGIS RMNLVPSLME IILPSLEKNL
SWGHNPLKML IFSGENLSIL LWKRVHEILP ETTIVNLYGT TEVSGDCTFF DCTDLPILLK
REELTSVPIG FPISNCEVCI ATDAEVADEG EMHVTGACLF AGYLEESMAS NHTEDNGSST
YYRTGDFARR LKSGEFIFLG RKDRTVKIYG QRFSLQEVES TLNEHPDVSA AAVTFQNNEF
LDFRAYLVLK SSTASVEDCQ RRKRYKSSEV IMPSIRSWLI MKLPPAMIPR FFLPMESLPL
TSSGKIDYMK LSSLKCALES CETETERITV NPHLQVIKKA FSDALLVDEV SEFDDFFTLG
GNSISAAHVA HKLEIDMRML YIYSTPSKLL DALFTKHGCL LSSSREPHPK KGLDISSSIH
SSFNPIATSV DDNFPEVKAH INGDGECAHD AISGNYANEV DGQLNRNVPL SNDRYQTKSL
LLDTCSNDRN SVDVSPWILN FCLVKKWSIG RCNRFMHGYE DKLQIEDVCS YVPYNKRGYL
QALWNIPLGS CVDASPLLVS NNGMLSIFIG SHSHRFLCID GCSGSVRWSV KLEGRVECSA
AITGDFSEVV VGCYKGKIYF LDLLTGKQAW TIQTDGEVKM QPAVDMIRNL IWCGSYDHHL
YALNYKDRCC TYKISCGGSI YGSPAIDMTH NMIYVASTSG LVTAISLEVS SFKIIWQYEA
GAPIFGSLAI HHHGGKVICC LVNGLVIALN SHGSVVWKAS VGGPIFAGAC LSSGLPTQVL
IPSRDGRLYS FDTTSGALLW KYEVGDPITA SAFVDEVLTA TSPGASERFA CICTSSGQVH
VIRIRADAKE EKVNGSICND LVQGFAAIDL PGDIFSSPLM VGGRIFVGCR DDQLHCLTIS
S
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