ID   FAC17_MYCMM             Reviewed;         503 AA.
AC   B2HHZ8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Medium/long-chain-fatty-acid--CoA ligase FadD17;
DE            Short=FACL;
DE            EC=6.2.1.2 {ECO:0000250|UniProtKB:O53551};
DE            EC=6.2.1.3 {ECO:0000250|UniProtKB:O53551};
DE   AltName: Full=Acyl-CoA synthetase;
GN   Name=fadD17; OrderedLocusNames=MMAR_4994;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
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 medium/long-chain fatty acids as
CC       acyl-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:O53551}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC         acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC         Evidence={ECO:0000250|UniProtKB:O53551};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC         Evidence={ECO:0000250|UniProtKB:O53551};
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:O53551};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC         Evidence={ECO:0000250|UniProtKB:O53551};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000250|UniProtKB:O53551}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; CP000854; ACC43398.1; -; Genomic_DNA.
DR   RefSeq; WP_012396518.1; NC_010612.1.
DR   AlphaFoldDB; B2HHZ8; -.
DR   SMR; B2HHZ8; -.
DR   STRING; 216594.MMAR_4994; -.
DR   KEGG; mmi:MMAR_4994; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_10_11; -.
DR   OrthoDB; 9803968at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05934; FACL_DitJ_like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43107:SF15; FATTY ACID TRANSPORT PROTEIN 3, ISOFORM A; 1.
DR   PANTHER; PTHR43107; LONG-CHAIN FATTY ACID TRANSPORT PROTEIN; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 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..503
FT                   /note="Medium/long-chain-fatty-acid--CoA ligase FadD17"
FT                   /id="PRO_0000406789"
SQ   SEQUENCE   503 AA;  53652 MW;  AE37B92E9C5024F3 CRC64;
     MSADPTVPQL LVPLAEIGDR GIYFEDSFTS WADHIGHGAA IAAALRERLD PTRPPHVGVL
     LQNTPFFSAM LAAAGMSGII PVGLNPVRRG AALARDIEHA DCQMVLADTA SASTLDGIEH
     VNVDSAEWAE VIDAHRNSEI SFQNAAPADL FMLIYTSGTS GDPKAVKCSH SKVAIAGVTM
     TQRFGLGRDD VCYVSMPLFH SNAVLVGWAV AVACQGSMAL RRKFSASQFL SDVRRYGATY
     ANYVGKPLSY VLATPERPDD ADNPLRAVYG NEGVPGDSER FGCRFGCVVQ DGFGSTEGGV
     AIARTPDTPA GSLGPLPENI EILDPETGQQ CPVGAVGELV NTAGPGRFEG YYNDEAASAQ
     RMSGGVYHSG DLAYRDAAGY AYFAGRLGDW MRVDGENLGT APIERVLLRY PDAIEVAVYA
     IPDPVVGDQV MAAMVLTPGA KFDVDKFRAF LAGQSDLGPK QWPSYVRICS ALPRTETFKV
     LKRQLAADGV DCGDPVWPIR DQS
//