FAC17_MYCMM
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 25-MAY-2022, entry version 69.
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; 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 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 EnsemblBacteria; ACC43398; ACC43398; MMAR_4994.
DR KEGG; mmi:MMAR_4994; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_10_11; -.
DR OMA; NAIMAGW; -.
DR OrthoDB; 377638at2; -.
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:0005324; F:long-chain fatty acid transporter activity; IEA:InterPro.
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 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 InterPro; IPR030310; FadD17/FadD6-like.
DR PANTHER; PTHR43107:SF15; PTHR43107:SF15; 1.
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..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
