LCFA_SALTI
ID LCFA_SALTI Reviewed; 561 AA.
AC P63522; Q8XGG8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=STY1948, t1059;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD05501.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68725.1; -; Genomic_DNA.
DR RefSeq; NP_456325.1; NC_003198.1.
DR RefSeq; WP_000758418.1; NZ_WSUR01000004.1.
DR AlphaFoldDB; P63522; -.
DR SMR; P63522; -.
DR STRING; 220341.16503005; -.
DR EnsemblBacteria; AAO68725; AAO68725; t1059.
DR KEGG; stt:t1059; -.
DR KEGG; sty:STY1948; -.
DR PATRIC; fig|220341.7.peg.1965; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_7_6; -.
DR OMA; KQSDMKA; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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.
FT CHAIN 1..561
FT /note="Long-chain-fatty-acid--CoA ligase"
FT /id="PRO_0000193128"
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