FAC19_MYCBO
ID FAC19_MYCBO Reviewed; 548 AA.
AC Q7TWB7; A0A1R3Y4F6; X2BNN2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
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};
GN OrderedLocusNames=BQ2027_MB3544C;
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 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; LT708304; SIU02171.1; -; Genomic_DNA.
DR RefSeq; NP_857183.1; NC_002945.3.
DR RefSeq; WP_003901660.1; NC_002945.4.
DR AlphaFoldDB; Q7TWB7; -.
DR SMR; Q7TWB7; -.
DR EnsemblBacteria; SIU02171; SIU02171; BQ2027_MB3544C.
DR PATRIC; fig|233413.5.peg.3883; -.
DR OMA; WRHEDVW; -.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00296; -.
DR Proteomes; UP000001419; 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; Steroid metabolism;
KW Sterol metabolism.
FT CHAIN 1..548
FT /note="Medium/long-chain-fatty-acid--CoA/3-oxocholest-4-en-
FT 26-oate--CoA ligase"
FT /id="PRO_0000406791"
FT REGION 520..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 548 AA; 59741 MW; E574B4BFA86F324E CRC64;
MAVALNIADL AEHAIDAVPD RVAVICGDEQ LTYAQLEDKA NRLAHHLIDQ GVQKDDKVGL
YCRNRIEIVI AMLGIVKAGA ILVNVNFRYV EGELRYLFDN SDMVALVHER RYADRVANVL
PDTPHVRTIL VVEDGSDQDY RRYGGVEFYS AIAAGSPERD FGERSADAIY LLYTGGTTGF
PKGVMWRHED IYRVLFGGTD FATGEFVKDE YDLAKAAAAN PPMIRYPIPP MIHGATQSAT
WMALFSGQTT VLAPEFNADE VWRTIHKHKV NLLFFTGDAM ARPLVDALVK GNDYDLSSLF
LLASTAALFS PSIKEKLLEL LPNRVITDSI GSSETGFGGT SVVAAGQAHG GGPRVRIDHR
TVVLDDDGNE VKPGSGMRGV IAKKGNIPVG YYKDEKKTAE TFRTINGVRY AIPGDYAQVE
EDGTVTMLGR GSVSINSGGE KVYPEEVEAA LKGHPDVFDA LVVGVPDPRY GQQVAAVVQA
RPGCRPSLAE LDSFVRSEIA GYKVPRSLWF VDEVKRSPAG KPDYRWAKEQ TEARPADDVH
AGHVTSGG
