ID   LCFA_SALTY              Reviewed;         561 AA.
AC   P63521; Q8XGG8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase;
DE            EC=6.2.1.3 {ECO:0000250|UniProtKB:P69451};
DE   AltName: Full=Long-chain acyl-CoA synthetase;
GN   Name=fadD; OrderedLocusNames=STM1818;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Catalyzes the esterification, concomitant with transport, of
CC       exogenous long-chain fatty acids into metabolically active CoA
CC       thioesters for subsequent degradation or incorporation into
CC       phospholipids. {ECO:0000250|UniProtKB:P69451}.
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:0000250|UniProtKB:P69451};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P69451};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000250|UniProtKB:P69451}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}. Note=Partially membrane-associated.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AE006468; AAL20733.1; -; Genomic_DNA.
DR   RefSeq; NP_460774.1; NC_003197.2.
DR   RefSeq; WP_000758418.1; NC_003197.2.
DR   AlphaFoldDB; P63521; -.
DR   SMR; P63521; -.
DR   STRING; 99287.STM1818; -.
DR   PaxDb; P63521; -.
DR   EnsemblBacteria; AAL20733; AAL20733; STM1818.
DR   GeneID; 1253337; -.
DR   KEGG; stm:STM1818; -.
DR   PATRIC; fig|99287.12.peg.1918; -.
DR   HOGENOM; CLU_000022_59_7_6; -.
DR   OMA; KQSDMKA; -.
DR   PhylomeDB; P63521; -.
DR   BioCyc; SENT99287:STM1818-MON; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 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.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium;
KW   Membrane; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..561
FT                   /note="Long-chain-fatty-acid--CoA ligase"
FT                   /id="PRO_0000193129"
FT   BINDING         213..224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   561 AA;  62223 MW;  4000B2948FE38D15 CRC64;
     MKKVWLNRYP ADVPAEINPD RYQSLVELFE HAATRYADQP AFVNMGEVMT FRKLEERSRA
     FAAYLQQGLG LKKGDRVALM MPNLLQYPVA LFGILRAGMI VVNVNPLYTP RELEHQLNDS
     GAAAIIIVSN FAHTLEKVVE KTSVQHVILT RMGDQLSTAK GTVVNFVVKY IKRLVPKYHL
     PDAISFRSAL QHGYRMQYVK PEVVAEDLAF LQYTGGTTGV AKGAMLTHRN MLANLEQVKA
     TYGPLLHPGK ELVVTALPLY HIFALTMNCL LFIELGGQNL LITNPRDIPG LVKELAKYPF
     TAMTGVNTLF NALLNNKEFQ QLDFSSLHLS AGGGMPVQNV VAERWVKLTG QYLLEGYGLT
     ECAPLVSVNP HDIDYHSGSI GLPVPSTEAK LVDDDDNEVA PGEAGELCVK GPQVMLGYWQ
     RPDATDEIIK DGWLHTGDIA VMDEDGFLRI VDRKKDMILV SGFNVYPNEI EDVVMQHSGV
     QEVAAVGVPS GSSGEAVKLF VVKKDPALTD DALITFCRRH LTGYKVPKQV EFREELPKSN
     VGKILRRELR DEARGKVDNK A