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LCFA_HAEIN
ID   LCFA_HAEIN              Reviewed;         562 AA.
AC   P46450;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, 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=HI_0390.1;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   IDENTIFICATION.
RA   Koonin E.V., Rudd K.E.;
RL   Submitted (SEP-1995) to UniProtKB.
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; L42023; AAC22049.1; -; Genomic_DNA.
DR   RefSeq; NP_438551.1; NC_000907.1.
DR   RefSeq; WP_005693780.1; NC_000907.1.
DR   AlphaFoldDB; P46450; -.
DR   SMR; P46450; -.
DR   STRING; 71421.HI_0390.1; -.
DR   EnsemblBacteria; AAC22049; AAC22049; HI_0390.1.
DR   KEGG; hin:HI_0390.1; -.
DR   PATRIC; fig|71421.8.peg.408; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_9_6; -.
DR   OMA; KQSDMKA; -.
DR   PhylomeDB; P46450; -.
DR   BioCyc; HINF71421:G1GJ1-405-MON; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000000579; 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_0000193131"
SQ   SEQUENCE   562 AA;  63479 MW;  74BE7C8E9D711F12 CRC64;
     MEKIWFQNYP KGSEKFLDTS KYESILDMFD KAVREHPDRP AYINMGQVLT FRKLEERSRA
     FAAYLQNEFK LQRGDRVALM MPNLLQYPIA LFGILRAGLI AVNVNPLYTP RELELQLQDS
     GAVAIVVVSN FASTLEKVVF NTNVKHVILT RMGDQLSFGK RTLVNFVVKY VKKLVPKYKL
     PHAVTFREVL SIGKYRQYVR PEISREDLAF LQYTGGTTGV AKGAMLTHGN IITNVFQAKW
     IAEPFIGDHS RTRSAILALP LYHVFALTVN CLLFLELGVT AILITNPRDI EGFVKELKKY
     RFEAITGVNT LFNALLNNEN FKEVDFSALK LSVGGGMAIQ QSVATRWHEL TGCNIIEGYG
     MTECSPLIAA CPINVVKHNG TIGVPVPNTD IKIIKDDGSD AKIGEAGELW VKGDQVMRGY
     WQRPEATSEV LKDGWMATGD IVIMDESYSL RIVDRKKDII LVSGFNVYPN EIEDVVMLNY
     KVSEAVAIGV PHAVSGETIK IFVVKKDDSL TRDELRNHCR QYLTGYKVPK EIEFRDELPK
     TNVGKILRRV LRDEEIAKRP KH
 
 
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