LCFA_BACSU
ID LCFA_BACSU Reviewed; 560 AA.
AC P94547;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase;
DE EC=6.2.1.3;
DE AltName: Full=Long-chain acyl-CoA synthetase;
GN Name=lcfA; OrderedLocusNames=BSU28560;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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 -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; Z75208; CAA99571.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14816.1; -; Genomic_DNA.
DR PIR; D69649; D69649.
DR RefSeq; NP_390734.1; NC_000964.3.
DR RefSeq; WP_004399166.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P94547; -.
DR SMR; P94547; -.
DR STRING; 224308.BSU28560; -.
DR PaxDb; P94547; -.
DR PRIDE; P94547; -.
DR EnsemblBacteria; CAB14816; CAB14816; BSU_28560.
DR GeneID; 936505; -.
DR KEGG; bsu:BSU28560; -.
DR PATRIC; fig|224308.179.peg.3103; -.
DR eggNOG; COG0318; Bacteria.
DR InParanoid; P94547; -.
DR OMA; KQSDMKA; -.
DR PhylomeDB; P94547; -.
DR BioCyc; BSUB:BSU28560-MON; -.
DR Proteomes; UP000001570; Chromosome.
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 Gene3D; 3.30.300.30; -; 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 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;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..560
FT /note="Long-chain-fatty-acid--CoA ligase"
FT /id="PRO_0000193124"
SQ SEQUENCE 560 AA; 62692 MW; 416A664E5926C7EA CRC64;
MQSQKPWLAE YPNDIPHELP LPNKTLQSIL TDSAARFPDK TAISFYGKKL TFHDILTDAL
KLAAFLQCNG LQKGDRVAVM LPNCPQTVIS YYGVLFAGGI VVQTNPLYTE HELEYQLRDA
QVSVIITLDL LFPKAIKMKT LSIVDQILIT SVKDYLPFPK NILYPLTQKQ KVHIDFDKTA
NIHTFASCMK QEKTELLTIP KIDPEHDIAV LQYTGGTTGA PKGVMLTHQN ILANTEMCAA
WMYDVKEGAE KVLGIVPFFH VYGLTAVMNY SIKLGFEMIL LPKFDPLETL KIIDKHKPTL
FPGAPTIYIG LLHHPELQHY DLSSIKSCLS GSAALPVEVK QKFEKVTGGK LVEGYGLSEA
SPVTHANFIW GKNKPGSIGC PWPSTDAAIY SEETGELAAP YEHGEIIVKG PQVMKGYWNK
PEETAAVLRD GWLFTGDMGY MDEEGFFYIA DRKKDIIIAG GYNIYPREVE EALYEHEAIQ
EIVVAGVPDS YRGETVKAFV VLKKGAKADT EELDAFARSR LAPYKVPKAY EFRKELPKTA
VGKILRRRLL EEETENHHIK