ID   FAC15_MYCBO             Reviewed;         600 AA.
AC   Q7TYX8; A0A1R3Y0F3; X2BK09;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 2.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase FadD15;
DE            Short=FACL;
DE            EC=6.2.1.3 {ECO:0000250|UniProtKB:O53521};
DE   AltName: Full=Acyl-CoA synthetase;
GN   Name=fadD15; OrderedLocusNames=BQ2027_MB2210;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Catalyzes the activation of long-chain fatty acids as acyl-
CC       coenzyme A (acyl-CoA), which are then transferred to the
CC       multifunctional polyketide synthase (PKS) type III for further chain
CC       extension. {ECO:0000250|UniProtKB:O53521}.
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:O53521};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC         Evidence={ECO:0000250|UniProtKB:O53521};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000250|UniProtKB:O53521}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=SIU00818.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; LT708304; SIU00818.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q7TYX8; -.
DR   SMR; Q7TYX8; -.
DR   EnsemblBacteria; SIU00818; SIU00818; BQ2027_MB2210.
DR   PATRIC; fig|233413.5.peg.2425; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001419; 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   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
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   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Nucleotide-binding.
FT   CHAIN           1..600
FT                   /note="Long-chain-fatty-acid--CoA ligase FadD15"
FT                   /id="PRO_0000406785"
SQ   SEQUENCE   600 AA;  64119 MW;  35DBF7534995F6C8 CRC64;
     MREISVPAPF TVGEHDNVAA MVFEHERDDP DYVIYQRLID GVWTDVTCAE AANQIRAAAL
     GLISLGVQAG DRVVIFSATR YEWAILDFAI LAVGAVTVPI YETSSAEQVR WVLQDSEAVV
     LFAETDSHAT MVAELSGSVP ALREVLQIAG SGPNALDRLT EAGASVDPAE LTARLAALRS
     TDPATLIYTS GTTGRPKGCQ LTQSNLVHEI KGARAYHPTL LRKGERLLVF LPLAHVLARA
     ISMAAFHSKV TVGFTSDIKN LLPMLAVFKP TVVVSVPRVF EKVYNTAEQN AANAGKGRIF
     AIAAQTAVDW SEACDRGGPG LLLRAKHAVF DRLVYRKLRA ALGGNCRAAV SGGAPLGARL
     GHFYRGAGLT IYEGYGLSET SGGVAISQFN DLKIGTVGKP VPGNSLRIAD DGELLVRGGV
     VFSGYWRNEQ ATTEAFTDGW FKTGDLGAVD EDGFLTITGR KKEIIVTAGG KNVAPAVLED
     QLRAHPLISQ AVVVGDAKPF IGALITIDPE AFEGWKQRNS KTAGASVGDL ATDPDLIAEI
     DAAVKQANLA VSHAESIRKF RILPVDFTED TGELTPTMKV KRKVVAEKFA SDIEAIYNKE