ID   FAC19_RHORH             Reviewed;         555 AA.
AC   E3UUE6;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=3-oxocholest-4-en-26-oate--CoA ligase {ECO:0000303|PubMed:21602385};
DE            EC=6.2.1.42 {ECO:0000269|PubMed:21602385};
DE   AltName: Full=Steroid-CoA ligase {ECO:0000303|PubMed:21602385};
DE   AltName: Full=Steroid-coenzyme A ligase {ECO:0000303|PubMed:21602385};
GN   Name=fadD19 {ECO:0000303|PubMed:21602385};
OS   Rhodococcus rhodochrous.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP   PHENOTYPE, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=DSM43269;
RX   PubMed=21602385; DOI=10.1128/aem.00380-11;
RA   Wilbrink M.H., Petrusma M., Dijkhuizen L., van der Geize R.;
RT   "FadD19 of Rhodococcus rhodochrous DSM43269, a steroid-coenzyme A ligase
RT   essential for degradation of C-24 branched sterol side chains.";
RL   Appl. Environ. Microbiol. 77:4455-4464(2011).
RN   [2]
RP   FUNCTION.
RC   STRAIN=DSM43269;
RX   PubMed=24244004; DOI=10.1128/jb.01012-13;
RA   Casabon I., Swain K., Crowe A.M., Eltis L.D., Mohn W.W.;
RT   "Actinobacterial acyl coenzyme A synthetases involved in steroid side-chain
RT   catabolism.";
RL   J. Bacteriol. 196:579-587(2014).
CC   -!- FUNCTION: Involved in the degradation of the side chains of C-24
CC       branched-chain sterols. Catalyzes the ATP-dependent CoA
CC       thioesterification of the sterol 3-oxocholest-4-en-26-oate to yield 3-
CC       oxocholest-4-en-26-oyl-CoA. It can also use beta-sitosterol,
CC       campesterol and 3beta-hydroxy-5-cholesten-26-oate.
CC       {ECO:0000269|PubMed:21602385, ECO:0000269|PubMed:24244004}.
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:0000269|PubMed:21602385};
CC   -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC       {ECO:0000305|PubMed:21602385}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to degrade the
CC       side chain of C-24 branched sterols such as beta-sitosterol and
CC       campesterol. {ECO:0000269|PubMed:21602385}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; HM588719; ADP09625.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3UUE6; -.
DR   SMR; E3UUE6; -.
DR   KEGG; ag:ADP09625; -.
DR   BioCyc; MetaCyc:MON-16899; -.
DR   UniPathway; UPA00296; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008203; P:cholesterol metabolic 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   1: Evidence at protein level;
KW   ATP-binding; Cholesterol metabolism; Ligase; Lipid metabolism;
KW   Nucleotide-binding; Steroid metabolism; Sterol metabolism.
FT   CHAIN           1..555
FT                   /note="3-oxocholest-4-en-26-oate--CoA ligase"
FT                   /id="PRO_0000430658"
FT   REGION          525..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         172..180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         418
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         433
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         524
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   555 AA;  60602 MW;  0C884C255591F0E3 CRC64;
     MALNIADLVE HAIDLVPERV ALASDGREVT YAQLEERANR LAHYLREQGV EPGDKVGIYS
     RNTIEAVEAM IAVFKIRAIM INVNYRYVEN ELQYIFDNSD MVALIHERRY SDKVANVLPS
     TPLVKTVVVV EDGTDVDFSA YGGIEYEAAL AQSSPERDFE DRSADDIYIL YTGGTTGHPK
     GVMWRHEDVW RVLGGGINFM TGEWVKDEWQ LAKEGAENPG LVRYPIPPMI HGGAQWALFQ
     SLFSGGKVIM HPEFSGHEVW RIIDDHKVNV IFITGDAMAR PMLDALEEGN PKTGKPYDLS
     TLFAMASSAA LFSPSIKDRF LDLLPGKIIT DSIGSSETGF GGIGIAEKGK TLGGGPTVKI
     DESTTVLDDD GNPIEPGSGK VGMVARTGNI PLGYYKDEAK TKATFREYNG IRYSIPGDYA
     RVEADGTVTM LGRGSVSINS GGEKVYPEEV EGALKQHPAV FDALVVGVPD ERFGERVSAV
     VALRDGEQVT LDELMTTARS KIAGYKVPRA VWFVDEIKRS PAGKPDYRWA KDQTGLRPAD
     EVYNNGDGNG AAATG