ID A0A3Q7HWQ1_SOLLC Unreviewed; 1051 AA.
AC A0A3Q7HWQ1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|ARBA:ARBA00026121, ECO:0000256|RuleBase:RU369030};
DE EC=6.2.1.3 {ECO:0000256|ARBA:ARBA00026121, ECO:0000256|RuleBase:RU369030};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc08g082280.3.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc08g082280.3.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc08g082280.3.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc08g082280.3.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc08g082280.3.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) 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=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 -!- PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene
CC biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004930}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003945}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU003945}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU369030}.
CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family.
CC {ECO:0000256|RuleBase:RU003945}.
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DR AlphaFoldDB; A0A3Q7HWQ1; -.
DR STRING; 4081.A0A3Q7HWQ1; -.
DR PaxDb; 4081-Solyc08g082280-2-1; -.
DR EnsemblPlants; Solyc08g082280.3.1; Solyc08g082280.3.1; Solyc08g082280.3.
DR Gramene; Solyc08g082280.3.1; Solyc08g082280.3.1; Solyc08g082280.3.
DR InParanoid; A0A3Q7HWQ1; -.
DR OMA; LECCWDI; -.
DR UniPathway; UPA00372; UER00547.
DR Proteomes; UP000004994; Chromosome 8.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd20069; 5TM_Oxa1-like; 1.
DR CDD; cd05927; LC-FACS_euk; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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 InterPro; IPR028055; YidC/Oxa/ALB_C.
DR PANTHER; PTHR43272:SF105; LONG CHAIN ACYL-COA SYNTHETASE 4; 1.
DR PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF02096; 60KD_IMP; 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU369030};
KW Phenylpropanoid metabolism {ECO:0000256|ARBA:ARBA00023051};
KW Reference proteome {ECO:0000313|Proteomes:UP000004994};
KW Transmembrane {ECO:0000256|RuleBase:RU003945, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 164..306
FT /note="Membrane insertase YidC/Oxa/ALB C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02096"
FT DOMAIN 449..875
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 1051 AA; 117304 MW; E9CCFBF681409D79 CRC64;
MAYRRSITTR AKLLYQQQRV TPSFSYFHKD DDDRKSCPEP TFENLRITSF SQSRYMGSVS
GVNSFIGSRS PYQDRRFCAS GLMIPMSYGS SLTRNMSTDI GGEADKINYM TDVAEVLADK
AVEAVVSQAP ALNEVANAAA DCYLPVKALM YLMDYVHIFT GFEWWGSIVV TSIMIRLVIL
PLMINQLKAT SKLTLSSVLL RYFSFCPTVS QCNHDVIGTR YGVTPFTPLK GLLIQGPIFI
SFFMAIRNMV DAVPSLKTGG PLWFTDLTTP DDMYILPVLT ALTFWITVEL NAQEGLEGNP
AGKTIKNVSR AFAVLTVPLT ASFAKSLSMQ TAYQKQRTPF LHVCTHSFKR DVLLILLEHV
IKEIVSVIGH MCTLLLVSGW IFLRRKKKEE GSRMAPEKFI VEVEPAKPAK DGRPSMGPVY
RSLFAKDGFP PPIPGLDSCW DIFRLSVEKY PNNRMLGHRE IVDGKPGKYV WMSYKEVYDI
VIKVGNSIRS CGVNKGDKCG IYGANCAEWI ISMEACNAHG LYCVPLYDTL GAGAVEFIIS
HAEVTIAFVE EKKLPELLKT FPDASKYLKT IVSFGKVTPQ QKEEVEKFGV VLYSWDEFLQ
LGSEKQFDLP VKKKEDICTI MYTSGTTGDP KGVLISNTSI VTLIAGVKRL LGSVNESLTV
DDVYLSYLPL AHIFDRVIEE CFINHGASIG FWRGDVKLLT EDIGELKPTI FCAVPRVLDR
IYSGLQHKIT SGGMLKSTLF NLAYAYKHRN LKKGQSHVEA SPLSDKVVFS KVKEGLGGRV
RLILSGAAPL ASHVEAFLRV VGCCHVLQGY GLTETCAGTF VSLPNHYDML GTVGPPVPNV
DVCLESVPEM SYDALSSTPR GEVCVRGDTL FSGYFKREDL TKEVMIDGWF HTGDVGEWQP
NGSLKIIDRK KNIFKLSQGE YVAVENLENI YGDNPVIDSI WIYGNSFESF LVAVINPNER
AIEHWAEHNG ISGDFASLCE NAKVKEYIIG ELAKTGKEKK LKGFEFIKAV HLDPLPFDME
RDLLTPTFKK KRPQMLKFYK DVIDNMYKST K
//
