LCFA_YERPE
ID LCFA_YERPE Reviewed; 562 AA.
AC Q8ZES9; Q0WF82;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, 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;
GN Name=fadD; OrderedLocusNames=YPO2074, y2236, YP_1917;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(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. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM85796.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS62135.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL20709.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM85796.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS62135.1; ALT_INIT; Genomic_DNA.
DR PIR; AB0253; AB0253.
DR RefSeq; WP_002211182.1; NZ_UHIZ01000001.1.
DR RefSeq; YP_002347056.1; NC_003143.1.
DR AlphaFoldDB; Q8ZES9; -.
DR SMR; Q8ZES9; -.
DR STRING; 214092.YPO2074; -.
DR PaxDb; Q8ZES9; -.
DR DNASU; 1147183; -.
DR EnsemblBacteria; AAM85796; AAM85796; y2236.
DR EnsemblBacteria; AAS62135; AAS62135; YP_1917.
DR GeneID; 57976587; -.
DR KEGG; ype:YPO2074; -.
DR KEGG; ypk:y2236; -.
DR KEGG; ypl:CH46_3036; -.
DR KEGG; ypm:YP_1917; -.
DR KEGG; ypv:BZ15_1462; -.
DR KEGG; ypw:CH59_4048; -.
DR PATRIC; fig|1028802.3.peg.2; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_9_6; -.
DR OMA; KQSDMKA; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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..562
FT /note="Long-chain-fatty-acid--CoA ligase"
FT /id="PRO_0000193130"
FT BINDING 213..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT VARIANT 504
FT /note="N -> K (in strain: KIM5 and 91001)"
SQ SEQUENCE 562 AA; 62639 MW; 812A872B3713D3FD CRC64;
MEKVWLKRYP ADVPAEIDPD RYSSLIEMFE NAALRYADQP AFINMGEVMT FRKLEERSRA
FAAYLQQGLG LQKGDRVALM MPNLLQYPIA LFGVLRAGMI VVNVNPLYTP RELEHQLSDS
GAVAIVIVSN FAHTLEKVVF KTQVRHVILT RMGDQLSAAK GTLVNFVVKY IKRLVPKYYL
PDAISFRTVL QKGRRMQYVK PDVINTDTAF LQYTGGTTGV AKGAILTHRN MQSNLEQAKA
AYAPLLQPGR DLVVTALPLY HIFALTVNCL LFIELGGRSL LITNPRDIPG MVKELSRYPF
TAITGVNTLF NALLNNEEFT HLDFSTLRLS VGGGMPVQKA VAEKWETLTG KHLLEGYGLT
ECSPLVTGNP YDLKHYSGSI GLPVPSTDVR LRDDDGNDVE LGKPGELWVR GPQVMLGYWQ
RPDATDDVLK DGWLATGDIA TMDEDGFLRI VDRKKDMILV SGFNVYPNEI EEVVALHAKV
LESAVIGVPN EVSGEAVKVF VVKNDASLTP EELLTHCRRY LTGYKVPKIV EFRDELPKSN
VGKILRRELR DEEVKVGTTD AA
