ID I1IPU8_BRADI Unreviewed; 722 AA.
AC I1IPU8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=4-coumarate--CoA ligase {ECO:0000256|ARBA:ARBA00012959};
DE EC=6.2.1.12 {ECO:0000256|ARBA:ARBA00012959};
GN Name=100836680 {ECO:0000313|EnsemblPlants:KQJ90101};
GN ORFNames=BRADI_4g29410v3 {ECO:0000313|EMBL:KQJ90101.1};
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:KQJ90101.1};
RN [1] {ECO:0000313|EMBL:KQJ90101.1, ECO:0000313|EnsemblPlants:KQJ90101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ90101.1,
RC ECO:0000313|EnsemblPlants:KQJ90101};
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:KQJ90101.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ90101.1};
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:KQJ90101}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ90101};
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 -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000883; KQJ90101.1; -; Genomic_DNA.
DR RefSeq; XP_003576487.1; XM_003576439.3.
DR AlphaFoldDB; I1IPU8; -.
DR STRING; 15368.I1IPU8; -.
DR EnsemblPlants; KQJ90101; KQJ90101; BRADI_4g29410v3.
DR GeneID; 100836680; -.
DR Gramene; KQJ90101; KQJ90101; BRADI_4g29410v3.
DR KEGG; bdi:100836680; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_8_1; -.
DR InParanoid; I1IPU8; -.
DR OMA; TGWIMYM; -.
DR OrthoDB; 760232at2759; -.
DR Proteomes; UP000008810; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR032387; ACAS_N.
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; PTHR44378; ACYL-ACTIVATING ENZYME 17, PEROXISOMAL-RELATED; 1.
DR PANTHER; PTHR44378:SF2; ACYL-ACTIVATING ENZYME 17, PEROXISOMAL-RELATED; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 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:UP000008810};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 244..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 121..177
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 188..552
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 722 AA; 78103 MW; 88129DAE7261D967 CRC64;
MAAAASHKPL AAITADDLAA AGAAEAAALH SAVSRALGAK GSGGPAAVWA ELSRAALRPD
VPFAVHRMLY YGCYAGFPSP APPAWMPDPE EAALTNVGRV LEARGRELIG EAYKDPITSF
RDFHKFSNEN PEAYWKMIFE EMGITFSVEP SCILRDNDAY PGGEWLPGAV LNAAANCLNA
KPGRRSSDVA IVWRDEGKDS EPLNVVTLEE LRKKVCLVAN ALDSLDLTKG SAIAIDMPMN
VNAVIIYLAI VLAGYVVVSI ADSFAAPAIS TRLKISEAKA IFTQDCILRD DKELPLYSRV
LEAKAPMAIV IPARGSTPIK GLRTDDLSWQ DFLGRADRTK ADIYTTVEQP VYEFSNILFS
SGTTGEPKAI PWTHLTPLKA AADGWCHMDI RKGDVVAWPT NLGWMMGPWL VYASLLNGAS
MALYNGSPNS SGFAKFVQDA KVTMLGVVPS IVRTWKNTDC TAGFDWSTIR CFSSTGEASS
VDDYLWLMGR ACYKPVIEYC GGTEIGGGFI TGCLLQPQAL SAFSTPAMGC NLFILDSNGK
PLPQDSAGIG ELALDPTLFG SSTMLLNADH HEVYFSGMPE WNAKVLRRHG DEFERTADGY
YRAHGRADDT MNLGGIKVSS IEIERICNRV NDDILETAAI GVPPVGGGPE QLTIAVVFKD
QRPQAEDLNQ LKLMFNSALK KLNPLFKVSS VIVVSSLPRT ASNKVMRRVL RKELTLAKHS
KI
//
