LCFA_ECOLI
ID LCFA_ECOLI Reviewed; 561 AA.
AC P69451; P29212;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase;
DE EC=6.2.1.3 {ECO:0000269|PubMed:15213221};
DE AltName: Full=Long-chain acyl-CoA synthetase;
DE Short=Acyl-CoA synthetase;
GN Name=fadD; Synonyms=oldD; OrderedLocusNames=b1805, JW1794;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8107670; DOI=10.1007/bf00280412;
RA Fulda M., Heinz E., Wolter F.P.;
RT "The fadD gene of Escherichia coli K12 is located close to rnd at 39.6 min
RT of the chromosomal map and is a new member of the AMP-binding protein
RT family.";
RL Mol. Gen. Genet. 242:241-249(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC STRAIN=K12;
RX PubMed=1460045; DOI=10.1016/s0021-9258(19)74070-8;
RA Black P.N., Dirusso C.C., Metzger A.K., Heimert T.L.;
RT "Cloning, sequencing, and expression of the fadD gene of Escherichia coli
RT encoding acyl coenzyme A synthetase.";
RL J. Biol. Chem. 267:25513-25520(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP IDENTIFICATION OF ATP-BINDING MOTIF, AND MUTAGENESIS OF TYR-213; THR-214;
RP GLY-216; THR-217; GLY-219; LYS-222 AND GLU-361.
RX PubMed=12034706; DOI=10.1074/jbc.m107022200;
RA Weimar J.D., DiRusso C.C., Delio R., Black P.N.;
RT "Functional role of fatty acyl-coenzyme A synthetase in the transmembrane
RT movement and activation of exogenous long-chain fatty acids. Amino acid
RT residues within the ATP/AMP signature motif of Escherichia coli FadD are
RT required for enzyme activity and fatty acid transport.";
RL J. Biol. Chem. 277:29369-29376(2002).
RN [7]
RP FUNCTION IN AEROBIC BETA-OXIDATION PATHWAY, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12535077; DOI=10.1046/j.1365-2958.2003.03341.x;
RA Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr.;
RT "A new Escherichia coli metabolic competency: growth on fatty acids by a
RT novel anaerobic beta-oxidation pathway.";
RL Mol. Microbiol. 47:793-805(2003).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, PROTEOLYTIC CLEAVAGE, AND
RP PATHWAY.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=15213221; DOI=10.1074/jbc.m405233200;
RA Morgan-Kiss R.M., Cronan J.E.;
RT "The Escherichia coli fadK (ydiD) gene encodes an anerobically regulated
RT short chain acyl-CoA synthetase.";
RL J. Biol. Chem. 279:37324-37333(2004).
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. Activity is the highest with fatty acid substrates of >
CC 10 carbon atoms (PubMed:15213221). Is involved in the aerobic beta-
CC oxidative degradation of fatty acids, which allows aerobic growth of
CC E.coli on fatty acids as a sole carbon and energy source
CC (PubMed:12535077). {ECO:0000269|PubMed:12535077,
CC ECO:0000269|PubMed:15213221}.
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:0000269|PubMed:15213221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000269|PubMed:15213221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15213221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000269|PubMed:15213221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA;
CC Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15213221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC Evidence={ECO:0000269|PubMed:15213221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15213221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000269|PubMed:15213221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetradecanoate = AMP + diphosphate +
CC tetradecanoyl-CoA; Xref=Rhea:RHEA:33619, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15213221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC Evidence={ECO:0000269|PubMed:15213221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + decanoate = AMP + decanoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:33627, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15213221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628;
CC Evidence={ECO:0000269|PubMed:15213221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15213221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC Evidence={ECO:0000269|PubMed:15213221};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15213221};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-7.8. {ECO:0000269|PubMed:15213221};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:12535077, ECO:0000305|PubMed:15213221}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WQ37}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=Partially membrane-associated.
CC {ECO:0000250}.
CC -!- INDUCTION: Well expressed during log and stationary phase aerobic
CC growth but only poorly expressed during anaerobic growth (at protein
CC level); aerobic expression is suppressed by glucose or C8 fatty acids
CC (PubMed:15213221). {ECO:0000269|PubMed:15213221}.
CC -!- PTM: Post-translationally cleaved by OmpT (PubMed:15213221).
CC {ECO:0000269|PubMed:15213221}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are completely blocked in
CC aerobic growth on fatty acids. The double fadD fadK deletion mutant
CC fails to grow on fatty acids under either aerobic or anaerobic
CC conditions, although fadD mutants grow on fatty acids under anaerobic
CC conditions. {ECO:0000269|PubMed:12535077}.
CC -!- MISCELLANEOUS: The enzymatic mechanism is a two-step reaction that
CC proceeds via the intermediate formation of an acyl-adenylate (acyl-AMP)
CC intermediate. {ECO:0000269|PubMed:15213221}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; X70994; CAA50321.1; -; Genomic_DNA.
DR EMBL; L02649; AAA23752.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74875.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15609.1; -; Genomic_DNA.
DR PIR; E64941; S41589.
DR RefSeq; NP_416319.1; NC_000913.3.
DR RefSeq; WP_000758422.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P69451; -.
DR SMR; P69451; -.
DR BioGRID; 4259150; 224.
DR IntAct; P69451; 6.
DR STRING; 511145.b1805; -.
DR SwissLipids; SLP:000001723; -.
DR TCDB; 4.C.1.1.4; the fatty acid group translocation (fat) family.
DR jPOST; P69451; -.
DR PaxDb; P69451; -.
DR PRIDE; P69451; -.
DR EnsemblBacteria; AAC74875; AAC74875; b1805.
DR EnsemblBacteria; BAA15609; BAA15609; BAA15609.
DR GeneID; 66674306; -.
DR GeneID; 946327; -.
DR KEGG; ecj:JW1794; -.
DR KEGG; eco:b1805; -.
DR PATRIC; fig|511145.12.peg.1881; -.
DR EchoBASE; EB1492; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_9_6; -.
DR InParanoid; P69451; -.
DR OMA; KQSDMKA; -.
DR PhylomeDB; P69451; -.
DR BioCyc; EcoCyc:ACYLCOASYN-MON; -.
DR BioCyc; MetaCyc:ACYLCOASYN-MON; -.
DR SABIO-RK; P69451; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:P69451; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; TAS:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0102391; F:decanoate-CoA ligase activity; IEA:RHEA.
DR GO; GO:0005504; F:fatty acid binding; IMP:EcoliWiki.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:EcoCyc.
DR GO; GO:0070538; F:oleic acid binding; IMP:EcoliWiki.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:EcoCyc.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:EcoCyc.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:EcoliWiki.
DR GO; GO:0015908; P:fatty acid transport; IMP:EcoCyc.
DR GO; GO:0006629; P:lipid metabolic process; IMP:EcoliWiki.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0009411; P:response to UV; IMP:EcoCyc.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Direct protein sequencing;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..561
FT /note="Long-chain-fatty-acid--CoA ligase"
FT /id="PRO_0000193125"
FT BINDING 213..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 213
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12034706"
FT MUTAGEN 214
FT /note="T->A: 10% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:12034706"
FT MUTAGEN 216
FT /note="G->A: Decreases activity."
FT /evidence="ECO:0000269|PubMed:12034706"
FT MUTAGEN 217
FT /note="T->A: Decreases activity."
FT /evidence="ECO:0000269|PubMed:12034706"
FT MUTAGEN 219
FT /note="G->A: Decreases activity."
FT /evidence="ECO:0000269|PubMed:12034706"
FT MUTAGEN 222
FT /note="K->A: Decreases activity."
FT /evidence="ECO:0000269|PubMed:12034706"
FT MUTAGEN 361
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12034706"
FT CONFLICT 34..51
FT /note="ARYADQPAFVNMGEVMTF -> GALRRSTCVCEYGGGNDL (in Ref. 2;
FT AAA23752)"
FT /evidence="ECO:0000305"
FT CONFLICT 468..490
FT /note="NEIEDVVMQHPGVQEVAAVGVPS -> TRLKMSSCSMVAYRKSRLLAYLP
FT (in Ref. 2; AAA23752)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="A -> G (in Ref. 2; AAA23752)"
FT /evidence="ECO:0000305"
FT CONFLICT 555..561
FT /note="GKVDNKA -> QSGQ (in Ref. 2; AAA23752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 62332 MW; 249B0AA54B3DBFA5 CRC64;
MKKVWLNRYP ADVPTEINPD RYQSLVDMFE QSVARYADQP AFVNMGEVMT FRKLEERSRA
FAAYLQQGLG LKKGDRVALM MPNLLQYPVA LFGILRAGMI VVNVNPLYTP RELEHQLNDS
GASAIVIVSN FAHTLEKVVD KTAVQHVILT RMGDQLSTAK GTVVNFVVKY IKRLVPKYHL
PDAISFRSAL HNGYRMQYVK PELVPEDLAF LQYTGGTTGV AKGAMLTHRN MLANLEQVNA
TYGPLLHPGK ELVVTALPLY HIFALTINCL LFIELGGQNL LITNPRDIPG LVKELAKYPF
TAITGVNTLF NALLNNKEFQ QLDFSSLHLS AGGGMPVQQV VAERWVKLTG QYLLEGYGLT
ECAPLVSVNP YDIDYHSGSI GLPVPSTEAK LVDDDDNEVP PGQPGELCVK GPQVMLGYWQ
RPDATDEIIK NGWLHTGDIA VMDEEGFLRI VDRKKDMILV SGFNVYPNEI EDVVMQHPGV
QEVAAVGVPS GSSGEAVKIF VVKKDPSLTE ESLVTFCRRQ LTGYKVPKLV EFRDELPKSN
VGKILRRELR DEARGKVDNK A
