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Database: UniProt
Entry: I1HUA9_BRADI
LinkDB: I1HUA9_BRADI
Original site: I1HUA9_BRADI 
ID   I1HUA9_BRADI            Unreviewed;       554 AA.
AC   I1HUA9;
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=100846491 {ECO:0000313|EnsemblPlants:KQK11060};
GN   ORFNames=BRADI_2g57860v3 {ECO:0000313|EMBL:KQK11060.1};
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|EnsemblPlants:KQK11060};
RN   [1] {ECO:0000313|EMBL:KQK11060.1, ECO:0000313|EnsemblPlants:KQK11060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK11060.1,
RC   ECO:0000313|EnsemblPlants:KQK11060};
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:KQK11060.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK11060.1};
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:KQK11060}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK11060};
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; CM000881; KQK11060.1; -; Genomic_DNA.
DR   RefSeq; XP_003564855.1; XM_003564807.3.
DR   AlphaFoldDB; I1HUA9; -.
DR   STRING; 15368.I1HUA9; -.
DR   EnsemblPlants; KQK11060; KQK11060; BRADI_2g57860v3.
DR   GeneID; 100846491; -.
DR   Gramene; KQK11060; KQK11060; BRADI_2g57860v3.
DR   KEGG; bdi:100846491; -.
DR   eggNOG; KOG1176; Eukaryota.
DR   HOGENOM; CLU_000022_59_2_1; -.
DR   InParanoid; I1HUA9; -.
DR   OMA; WMGKYEW; -.
DR   OrthoDB; 1404660at2759; -.
DR   Proteomes; UP000008810; Chromosome 2.
DR   GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProt.
DR   GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR   GO; GO:0106290; F:trans-cinnamate-CoA ligase activity; IEA:UniProt.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProt.
DR   CDD; cd05904; 4CL; 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; PTHR24096:SF251; 4-COUMARATE--COA LIGASE-LIKE 9; 1.
DR   PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 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          54..409
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          461..536
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   554 AA;  58535 MW;  9C56AA794F26A9C6 CRC64;
     MAEPPPAGID PRSGFCAATR TFHSLRSAAA LPPESLPVTA AAYAFSLLSS PLTDRPALVD
     AATGIAVSYP SFLAAVRSLA GGLWSSLGLR PGHVALVVAP SRLEVPVLHF ALMSIGAVVS
     PANPASTAEE YAHQVALSRP VVAFAAPEVA AKLPNHVRRV VIGSDAYKRL ASAGVDAAPP
     PVAVKQSDTA AVLYSSGTTG RVKAVAVTHR NLIALICAHS ENRETVAADA IKAGEEPPPP
     AVTLVPLPLF HVFGFMMILR SVSMGETAVL MERFDFGAAL RAIERYRVTL LPAAPPLLVA
     MVKSEEAHRR DLSSLLVIGV GGAPLGREVA ERFAAVFPDV QIVQGYGLTE SSGSVASTVG
     PEESMAYGSV GKLASHLQAK IVDPSTGEAV GPGQRGELWI RGPVVMKGYV GDDKATAETV
     DSEGWLKTGD LCYFNEDGFL YIVDRLKELI KYKGYQVPPA ELEHILQSHP GIADAAVIPY
     PDEDVGQLPM AFIVRQPGSN LTEQQVMDYV AKQVAPYKKV RRVTFVTSIP KSPAGKILRR
     ELVQQAVSMG ASKL
//
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