FAC19_MYCMM
ID FAC19_MYCMM Reviewed; 550 AA.
AC B2HI05;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Medium/long-chain-fatty-acid--CoA/3-oxocholest-4-en-26-oate--CoA ligase {ECO:0000250|UniProtKB:P9WQ51};
DE Short=FACL {ECO:0000250|UniProtKB:P9WQ51};
DE EC=6.2.1.2 {ECO:0000250|UniProtKB:P9WQ51};
DE EC=6.2.1.3 {ECO:0000250|UniProtKB:P9WQ51};
DE EC=6.2.1.42 {ECO:0000250|UniProtKB:P9WQ51};
DE AltName: Full=Acyl-CoA synthetase {ECO:0000250|UniProtKB:P9WQ51};
DE AltName: Full=Steroid-CoA ligase {ECO:0000250|UniProtKB:P9WQ51};
DE AltName: Full=Steroid-coenzyme A ligase {ECO:0000250|UniProtKB:P9WQ51};
GN Name=fadD19 {ECO:0000250|UniProtKB:P9WQ51}; Synonyms=fadD19_1;
GN OrderedLocusNames=MMAR_5001;
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. Also involved in the degradation of cholesterol via the
CC degradation of the side chains of C-24 branched-chain sterols.
CC Catalyzes the ATP-dependent CoA thioesterification of the sterol 3-
CC oxocholest-4-en-26-oate to yield 3-oxocholest-4-en-26-oyl-CoA.
CC {ECO:0000250|UniProtKB:P9WQ51}.
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:P9WQ51};
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:P9WQ51};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25S)-3-oxocholest-4-en-26-oate + ATP + CoA = (25S)-3-
CC oxocholest-4-en-26-oyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:29291,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:71541, ChEBI:CHEBI:83819, ChEBI:CHEBI:456215;
CC EC=6.2.1.42; Evidence={ECO:0000250|UniProtKB:P9WQ51};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P9WQ51}.
CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC {ECO:0000250|UniProtKB:P9WQ51}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CP000854; ACC43405.1; -; Genomic_DNA.
DR RefSeq; WP_012396525.1; NC_010612.1.
DR AlphaFoldDB; B2HI05; -.
DR SMR; B2HI05; -.
DR STRING; 216594.MMAR_5001; -.
DR EnsemblBacteria; ACC43405; ACC43405; MMAR_5001.
DR KEGG; mmi:MMAR_5001; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_11; -.
DR OMA; WRHEDVW; -.
DR OrthoDB; 377638at2; -.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00296; -.
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:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
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 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; Cholesterol metabolism; Fatty acid metabolism; Ligase;
KW Lipid metabolism; Nucleotide-binding; Reference proteome;
KW Steroid metabolism; Sterol metabolism.
FT CHAIN 1..550
FT /note="Medium/long-chain-fatty-acid--CoA/3-oxocholest-4-en-
FT 26-oate--CoA ligase"
FT /id="PRO_0000406792"
FT REGION 525..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 550 AA; 59946 MW; 6BA317E6E7E31ACB CRC64;
MAVALNIADL AEHAIDAVPD RVALICGDEQ LTYAQLEEKA NRLAHHLIDQ GVGKGDKVGL
YCRNRIEIVI AMLGIIKAGA ILINVNFRYV EGELKYLFDN SDMVALVHER QYADRVANVL
PDTPNVKTIL VVQDGSDKDY RRYGGVEFYS AIADSSPERD FAELQRERSA DDIYILYTGG
TTGFPKGVMW RHEDIYRVLF GGTDFATGEF IKDEYDLAKA AAANPPMIRY PIPPMIHGAT
QSATWMSIFS GQTTVLAPEF DADQVWRTIS DRKVNLLFFT GDAMARPLLD ALMKDNDYDL
SSLFLLASTA ALFSPSIKEK LLELLPNRVI TDSIGSSETG FGGTSIVGAG QATTGGPRVT
IDHRTVVLDE EGNEVKPGSG VRGIIAKKGN IPVGYYKDEK KTAETFKTIN GVRYAIPGDY
AMVEADGTVT MLGRGSVSIN SGGEKIYPEE VEAALKGHPD VFDALVVGVP DPRYGQHVAA
VVAPRPGSRP SLAELDGFVR SAIAGYKVPR SLWFVDEVKR SPAGKPDYRW AKEQTEARPA
DDVHAAHVSA
