ID   LCFA_ECO57              Reviewed;         561 AA.
AC   Q8XDR6;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 117.
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;
DE            Short=Acyl-CoA synthetase;
GN   Name=fadD; Synonyms=oldD; OrderedLocusNames=Z2848, ECs2514;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(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   -!- MISCELLANEOUS: Activity is the highest with fatty acid substrates of >
CC       10 carbon atoms. {ECO:0000250|UniProtKB:P69451}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB35937.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE005174; AAG56794.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35937.2; ALT_INIT; Genomic_DNA.
DR   PIR; B90943; B90943.
DR   PIR; F85791; F85791.
DR   RefSeq; NP_310541.1; NC_002695.1.
DR   RefSeq; WP_001302040.1; NZ_VOAI01000010.1.
DR   AlphaFoldDB; Q8XDR6; -.
DR   SMR; Q8XDR6; -.
DR   STRING; 155864.Z2848; -.
DR   GeneID; 912449; -.
DR   KEGG; ece:Z2848; -.
DR   KEGG; ecs:ECs_2514; -.
DR   PATRIC; fig|386585.9.peg.2634; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_9_6; -.
DR   OMA; KQSDMKA; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   CDD; cd05936; FC-FACS_FadD_like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43767:SF8; 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; 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_0000193127"
FT   BINDING         213..224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   561 AA;  62364 MW;  4DE944AB7DF40CF2 CRC64;
     MKKVWLNRYP ADVPTEINPD RYQSLVDMFE QSVARYADQP AFVNMGEVMT FRKLEERSRA
     FAAYLQQGLG LKKGDRVALM MPNLLQYPVA LFGILRAGMI VVNVNPLYTP RELEHQLNDS
     GASAIVIVSN FAHTLEKVVD KTAVQHVILT RMGDQLSTAK GTLVNFVVKY IKRLVPKYHL
     PDAISFRSAL HNGYRMQYVK PELVPEDLAF LQYTGGTTGV AKGAMLTHRN MLANLEQVNA
     TYGPLLHPGK ELVVTALPLY HIFALTINCL LFIELGGQNL LITNPRDIPG LVKELAKYPF
     TAITGVNTLF NALLNNKEFQ QLDFSSLHLS AGGGMPVQQV VAERWVKLTG QYLLEGYGLT
     ECAPLVSVNP YDIDYHSGSI GLPVPSTEAK LVDDDDNEVS PGQPGELCVR GPQVMLGYWQ
     RPDATDEIIK NGWLHTGDIA VMDEEGFLRI VDRKKDMILV SGFNVYPNEI EDVVMQHPGV
     QEVAAVGVPS GSSGEAVKIF VVKKDPSLTE ESLVTFCRRQ LTGYKVPKLV EFRDELPKSN
     VGKILRRELR DEARGKVDNK A
//