ID M5XXB3_PRUPE Unreviewed; 695 AA.
AC M5XXB3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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};
GN ORFNames=PRUPE_1G155800 {ECO:0000313|EMBL:ONI28697.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI28697.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI28697.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
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: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000256|RuleBase:RU369030}.
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 EMBL; CM007651; ONI28697.1; -; Genomic_DNA.
DR RefSeq; XP_007225174.1; XM_007225112.1.
DR AlphaFoldDB; M5XXB3; -.
DR STRING; 3760.M5XXB3; -.
DR EnsemblPlants; ONI28697; ONI28697; PRUPE_1G155800.
DR GeneID; 18788595; -.
DR Gramene; ONI28697; ONI28697; PRUPE_1G155800.
DR KEGG; pper:18788595; -.
DR eggNOG; KOG1256; Eukaryota.
DR HOGENOM; CLU_000022_45_4_1; -.
DR OMA; ARATMAH; -.
DR OrthoDB; 22305at2759; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000006882; Chromosome g1.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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 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 PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43272:SF3; LONG-CHAIN-FATTY-ACID--COA LIGASE 5; 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 Nucleotide-binding {ECO:0000256|RuleBase:RU369030};
KW Reference proteome {ECO:0000313|Proteomes:UP000006882}.
FT DOMAIN 109..508
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 695 AA; 76271 MW; 336CD38B75C92BA8 CRC64;
MDSTPAERRL QAIHGHLTTA AADSESPLRP NLTAGEFVSE QGYSVVLPEK LQTGKWNVYR
SARSPLKLVS RFPDHPEIGT LHDNFVHAVD TFRDYKYLGT RIRVDGTVGE YKWMTYGEAS
TARSAIGSGL IYHGIPKGAG IGLYFINRPE WLIVDHACSA YSYISVPLYD TLGPDAVKYI
VNHAVVQVIF CVPETLNSLL SFLADIPTVR LIVVVGGIDD QIPSLPSSTG VKVVTYSKLL
SQGNSSLQPF FPPEPEDVAT ICYTSGTTGT PKGAVLTHGN LIANVSGATM AIKFYPSDVY
ISYLPLAHIY ERANQVMTVY FGVAVGFFQG DSLKLMDDMA ALRPTIFCSV PRLYNRIYAG
IINAVKTSGV LRERLFNAAY NAKKQALLSG KNPSPMWDRL VFNKIKAKLG GRVRFMASGA
SPLSPDVMEF LKICFGGEVS EGYGMTETSC VISSVDGGDN LYGHVGSPNP ACEIKLVDVP
EMNYMSEDQP YPRGEICVRG PIIFQGYHKD EVQTREVIDE DGWLHTGDIG LWSPGGRLKI
IDRKKNIFKL AQGEYIAPEK IENVYAKCKF VAQCFVHGDS LNSSLVAIVS VDPDVLKAWA
DSEGIKYQDL GQLCNDPRAR AAVLADMDAV GREAQLRGFE FVKAVTLVLE PFTIENGLLT
PTFKIKRPQA KEYFAKEIST MYSELSTSNP APSKL
//
