ID A0A0D9XT80_9ORYZ Unreviewed; 667 AA.
AC A0A0D9XT80;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|RuleBase:RU369030};
DE EC=6.2.1.3 {ECO:0000256|RuleBase:RU369030};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR11G13650.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR11G13650.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR11G13650.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR11G13650.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: Catalyzes the conversion of long-chain fatty acids to their
CC active form acyl-CoAs for both synthesis of cellular lipids, and
CC degradation via beta-oxidation. {ECO:0000256|RuleBase:RU369030}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000256|RuleBase:RU369030};
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, ECO:0000256|RuleBase:RU369030}.
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DR AlphaFoldDB; A0A0D9XT80; -.
DR STRING; 77586.A0A0D9XT80; -.
DR EnsemblPlants; LPERR11G13650.1; LPERR11G13650.1; LPERR11G13650.
DR EnsemblPlants; LPERR11G13650.2; LPERR11G13650.2; LPERR11G13650.
DR Gramene; LPERR11G13650.1; LPERR11G13650.1; LPERR11G13650.
DR Gramene; LPERR11G13650.2; LPERR11G13650.2; LPERR11G13650.
DR eggNOG; KOG1256; Eukaryota.
DR HOGENOM; CLU_000022_45_4_1; -.
DR Proteomes; UP000032180; Chromosome 11.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblPlants.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:EnsemblPlants.
DR GO; GO:0106290; F:trans-cinnamate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IEA:EnsemblPlants.
DR GO; GO:0010143; P:cutin biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0050832; P:defense response to fungus; IEA:EnsemblPlants.
DR GO; GO:0010311; P:lateral root formation; IEA:EnsemblPlants.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProt.
DR CDD; cd05927; LC-FACS_euk; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR045311; LC-FACS_euk.
DR PANTHER; PTHR43272:SF4; LONG CHAIN ACYL-COA SYNTHETASE 2; 1.
DR PANTHER; PTHR43272; 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 ATP-binding {ECO:0000256|RuleBase:RU369030};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU369030};
KW Ligase {ECO:0000256|RuleBase:RU369030};
KW Lipid metabolism {ECO:0000256|RuleBase:RU369030};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU369030};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180}.
FT DOMAIN 64..486
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 538..607
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 667 AA; 74087 MW; 0DA298C666B0B824 CRC64;
MEQVYTVKVG EATPAGGGKP SAGPVYRSIY AKDGLMELPE DILSPWDFFS GAAKKYPKNK
MLGQRQVSDG KAGDYAWLSY EQVYQKVIKI GSAIRSLGVK QGGHCGIYGS NCPEWVMSMQ
ACNSQGLCYV PLYDTLGANA VEFIMDHAEI SIAFVQDSKI KSVLSAVQKC RAHIKAIVSF
GNVTSELKSE AEQLGLSCFS WEEFSAMGKQ DYELPKKRKD DICTIMYTSG TTGDPKGVII
TNRALIAGVM TTEHLLKVTD KALILNMKVA EDDSYFSYLP LAHIFDQVIG NYCISKGASV
GFWQGDVRYL MEDVQVMKPT IFCGVPRVYD RIYTGINQKI QSGGMIAKSL FQYAYNYKLG
NLSKGLKQHE ASPFFDKIVF SKIKEGLGGR IRLLLSGAAP LPRHIEEFMR VTSCGVLVQG
YGLTESTSGC FTSIANVFSM IGTVGPPVTT IEARLESIPE MGYDALSNVP RGEICLRGHT
LFSGYYKRPD LTEEVFSDGW FHTGDIGEWQ PDGTMKIIDR KKNIFKLSQG EYVAVEVLES
AYMQSPLVTS VWVYGNSFES FLVAVVVPEK QAIEDWAAQN NKTGDFAKLC NDPKARMYIQ
DELNKTGKKL GLRGFEMLKA VHLETVPFSI DKDLVTPTFK LKRPQLLKYY KDCIDKLYKD
AKEGTKQ
//
