ID   FAD3_RHOJR              Reviewed;         515 AA.
AC   Q0S7V5;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoyl:CoA ligase {ECO:0000303|PubMed:23146019};
DE            Short=HIP:CoA ligase {ECO:0000303|PubMed:23146019};
DE            EC=6.2.1.41 {ECO:0000269|PubMed:23146019};
GN   Name=fadD3 {ECO:0000303|PubMed:23146019};
GN   OrderedLocusNames=RHA1_ro04595 {ECO:0000312|EMBL:ABG96381.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=RHA1;
RX   PubMed=23146019; DOI=10.1111/mmi.12095;
RA   Casabon I., Crowe A.M., Liu J., Eltis L.D.;
RT   "FadD3 is an acyl-CoA synthetase that initiates catabolism of cholesterol
RT   rings C and D in actinobacteria.";
RL   Mol. Microbiol. 87:269-283(2013).
CC   -!- FUNCTION: Involved in the catabolism of the rings C and D of
CC       cholesterol. Catalyzes the ATP-dependent CoA thioesterification of
CC       3aalpha-H-4alpha(3'-propanoate)-7abeta-methylhexahydro-1,5-indanedione
CC       (HIP). {ECO:0000269|PubMed:23146019}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-
CC         yl]propanoate + ATP + CoA = 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-
CC         octahydro-1H-inden-4-yl]propanoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:41640, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:63692, ChEBI:CHEBI:78357,
CC         ChEBI:CHEBI:456215; EC=6.2.1.41;
CC         Evidence={ECO:0000269|PubMed:23146019};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene completely degrade
CC       cholesterol to half the yield of wild-type and accumulate HIP.
CC       {ECO:0000269|PubMed:23146019}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; CP000431; ABG96381.1; -; Genomic_DNA.
DR   RefSeq; WP_011596962.1; NC_008268.1.
DR   AlphaFoldDB; Q0S7V5; -.
DR   SMR; Q0S7V5; -.
DR   STRING; 101510.RHA1_ro04595; -.
DR   EnsemblBacteria; ABG96381; ABG96381; RHA1_ro04595.
DR   KEGG; rha:RHA1_ro04595; -.
DR   PATRIC; fig|101510.16.peg.4634; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_7_11; -.
DR   OMA; YIMPKFD; -.
DR   BioCyc; MetaCyc:MON-18451; -.
DR   Proteomes; UP000008710; Chromosome.
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-KW.
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; Reference proteome; Steroid metabolism;
KW   Sterol metabolism.
FT   CHAIN           1..515
FT                   /note="3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-
FT                   inden-4-yl]propanoyl:CoA ligase"
FT                   /id="PRO_0000430641"
FT   BINDING         185..193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         398
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         504
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   515 AA;  55543 MW;  78B31F34645B9D03 CRC64;
     MTEQPTTTPS ALKRAAREFG ELTAVADGDV RLTFTQLHDR VRDFAAALSS QDVRPGDHVA
     VWSPNTYHWV VAALGIHYAG ATLVPINTRY TATEALDILE RTKTTALVVA GNFLGTDRYA
     SLRDESSTFD LPTVVRVPVD GGDAELPGVF DFDDFLALAD EDTRAEADAR AAAVSPDDVS
     DVMFTSGTTG RSKGVMSAHR QSVGIAQAWG ECAEVTSDDN YLIINPFFHT FGYKAGFLVC
     LLNGATVVPM AVFDVPKVMA TVHDEQITVL PGAPTIFQSI LDHPDRPKYD LSSLRVAITG
     AAAVPVALVE RMQSELSFDA VLTAYGQTEA VVVTMCRTDD DPVTVSTTSG RAIPGMEVRI
     GDQGEILVRG ENVMLGYLDD PESTAKTIDA DGWLHTGDVG TLDDRGYVDI TDRLKDMYIS
     GGFNVYPAEV ENALARLDGV AESAVIGVPD ERMGEVGRAY VVAKPGVTLA EDDVVAFCKE
     RLANFKVPRS VRFVDSLPRN PSGKVMKNVL REEKK