ID I1IA43_BRADI Unreviewed; 705 AA.
AC I1IA43;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KQJ99673.1, ECO:0000313|EnsemblPlants:KQJ99673};
GN Name=100839844 {ECO:0000313|EnsemblPlants:KQJ99673};
GN ORFNames=BRADI_3g44620v3 {ECO:0000313|EMBL:KQJ99673.1};
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:KQJ99673.1};
RN [1] {ECO:0000313|EMBL:KQJ99673.1, ECO:0000313|EnsemblPlants:KQJ99673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ99673.1,
RC ECO:0000313|EnsemblPlants:KQJ99673};
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:KQJ99673.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ99673.1};
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:KQJ99673}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ99673};
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; CM000882; KQJ99673.1; -; Genomic_DNA.
DR RefSeq; XP_003575051.1; XM_003575003.3.
DR AlphaFoldDB; I1IA43; -.
DR STRING; 15368.I1IA43; -.
DR EnsemblPlants; KQJ99673; KQJ99673; BRADI_3g44620v3.
DR GeneID; 100839844; -.
DR Gramene; KQJ99673; KQJ99673; BRADI_3g44620v3.
DR KEGG; bdi:100839844; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; I1IA43; -.
DR OMA; INVSYNC; -.
DR OrthoDB; 144557at2759; -.
DR Proteomes; UP000008810; Chromosome 3.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106290; F:trans-cinnamate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProt.
DR CDD; cd05966; ACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR HAMAP; MF_01123; Ac_CoA_synth; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
DR InterPro; IPR032387; ACAS_N.
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 NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 1.
DR Pfam; PF16177; ACAS_N; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810}.
FT DOMAIN 71..132
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 139..527
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 589..667
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 705 AA; 77849 MW; 8E0FB1C596AABBCC CRC64;
MGTASADQPA GASPDKLRHV ESMSELPSGA GKISGINGVV LGESLADEEH DLVFPSPEFS
ANALVSSPKQ YREMYERSIK DPSGFWSEIA ESFYWKEKWN PSEVCSENLD VTKGPVQITW
FKGGKTNICY NAVDRNIEAG NGDKIAMYWE GNEPGQDGKL TYSELLDKVC QLANYLKSVG
VGKGDAVVIY LPMLLELPIA MLACARIGAV HSVVFAGFSA DSLAQRIVDC KPKVVLTCNS
VKRGAKPILL KDIVDAALVE SEKNGFSVGL CLTYENQSAM KREDTKWQAG RDVWWQDVVT
DFPTKCDVEW MDAEDPLFLL YTSGSTGKPK GVMHTSGGYM VYTATTFKYA FDYKPTDIYW
CTADCGWITG HSYVTYGPLL NGAAVLVFEG TPNYPDSGRC WDIVDKYNVT IFYTAPTLVR
SLMRDGTEYV TRYSRKSLRV LGSVGEPINP SAWRWFYNVV GDSKCPISDT WWQTETGGFM
MTPLPGAWPQ KPGSATFPFF GVQPVIVDEK GQEIEGECSG YLCIKKSWPG AFRTLYGDHD
RYETTYFKPF AGYYFTGDGC SRDKDGYHWL TGRVDDVINV SGHRIGTAEV ESALVSHPQC
AEAAVVGVEH EVKGQGIYAF VTLVDGVPYS EELRKSLIAK VRNQIGAFAA PDRIHWAPGL
PKTRSGKIMR RILRKIASKQ LDELGDISTL ADPSVVDQLI ALKDC
//
