ID   FAC15_MYCMM             Reviewed;         600 AA.
AC   B2HGV4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=MMAR_3231;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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}.
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DR   EMBL; CP000854; ACC41657.1; -; Genomic_DNA.
DR   RefSeq; WP_012394891.1; NC_010612.1.
DR   AlphaFoldDB; B2HGV4; -.
DR   SMR; B2HGV4; -.
DR   STRING; 216594.MMAR_3231; -.
DR   EnsemblBacteria; ACC41657; ACC41657; MMAR_3231.
DR   KEGG; mmi:MMAR_3231; -.
DR   eggNOG; COG1022; Bacteria.
DR   HOGENOM; CLU_000022_45_5_11; -.
DR   OMA; PRIWTKF; -.
DR   OrthoDB; 164380at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001190; 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; Reference proteome.
FT   CHAIN           1..600
FT                   /note="Long-chain-fatty-acid--CoA ligase FadD15"
FT                   /id="PRO_0000406786"
SQ   SEQUENCE   600 AA;  64751 MW;  CB132BBBF2E36150 CRC64;
     MRQYSVPARF SVDERDNVAA MVFEHERDDP DHIIYQRQID GIWTDITCAE AARHIRSAAL
     GLIALGVQAG DRVSIFSATC YEWAILDLAI LAVGAVTVPI YETSSAEQVR WVLQNSEAVL
     AFAETDAHAA MIAELTGDLP ALRRVLVING SGPKALEQLA EEGGSVDRAE LTARLDALRS
     SDPATLIYTS GTTGRPKGCQ LTHSNLLHEI RGTQECLPTL LTPGQRLLVF LPLAHVLARA
     LTLSAFASKV TVGFTSDIKN LLPLFAVFKP TVVVSVPRVF EKVYNTAEQN ASNDGKGAIF
     KLAAQTAVDW SRAWDDGRPG LLLRAKHALF DRLVYHKLRA ALGGDCHAAV SGGAPLGARL
     GHFYRGVGLT IYEGYGLTET SAAVTVNQID ALKIGTVGKL VPGNSLRIAD DGELLVRGGV
     VFSGYWRNEQ ATDEAFTDGW FRTGDLGAID DDGFLSITGR KKELIVTAGG KNVAPAVLED
     QLRAHPLISQ AMVVGDAKPF IGALITIDPE AFGGWKQRNS KADHAAVRDL AEDPDLVAEV
     DAAVKEANLA VSHAESIRKF RILHVDFTED TGELTPTMKV KRNVVAEKFS VEIEAIYTKD