ID   IPDC_RHOJR              Reviewed;         353 AA.
AC   Q0S7Q1;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=(3aS,4S,5R,7aS)-5-hydroxy-7a-methyl-1-oxo-octahydro-1H-indene-4-carboxyl-CoA dehydrogenase {ECO:0000305};
DE            Short=5OH-HIC-CoA dehydrogenase {ECO:0000305};
DE            EC=1.3.1.- {ECO:0000250|UniProtKB:P71847};
GN   Name=ipdC {ECO:0000303|PubMed:28377529};
GN   OrderedLocusNames=RHA1_ro04649 {ECO:0000312|EMBL:ABG96435.1};
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, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=RHA1;
RX   PubMed=28377529; DOI=10.1128/mbio.00321-17;
RA   Crowe A.M., Casabon I., Brown K.L., Liu J., Lian J., Rogalski J.C.,
RA   Hurst T.E., Snieckus V., Foster L.J., Eltis L.D.;
RT   "Catabolism of the last two steroid rings in Mycobacterium tuberculosis and
RT   other bacteria.";
RL   MBio 8:e00321-e00321(2017).
CC   -!- FUNCTION: Involved in the final steps of cholesterol and steroid
CC       degradation (PubMed:28377529). Probably catalyzes the introduction of a
CC       double bound into the C ring of 5OH-HIC-CoA, leading to the formation
CC       of (5R,7aS)-5-hydroxy-7a-methyl-1-oxo-3,5,6,7-tetrahydro-2H-indene-4-
CC       carboxyl-CoA (By similarity). {ECO:0000250|UniProtKB:P71847,
CC       ECO:0000269|PubMed:28377529}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3aS,4S,5R,7aS)-5-hydroxy-7a-methyl-1-oxo-octahydro-1H-indene-
CC         4-carboxyl-CoA + NAD(+) = (5R,7aS)-5-hydroxy-7a-methyl-1-oxo-
CC         2,3,5,6,7,7a-hexahydro-1H-indene-carboxyl-CoA + H(+) + NADH;
CC         Xref=Rhea:RHEA:66352, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:167058, ChEBI:CHEBI:167096;
CC         Evidence={ECO:0000250|UniProtKB:P71847};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66353;
CC         Evidence={ECO:0000250|UniProtKB:P71847};
CC   -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC       {ECO:0000269|PubMed:28377529}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant does not grow on cholesterol or
CC       HIP, but grows as the wild-type on pyruvate. In the presence of
CC       cholesterol, disruption mutant accumulates 5OH-HIC-CoA.
CC       {ECO:0000269|PubMed:28377529}.
CC   -!- SIMILARITY: Belongs to the nitronate monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000431; ABG96435.1; -; Genomic_DNA.
DR   RefSeq; WP_011597003.1; NC_008268.1.
DR   AlphaFoldDB; Q0S7Q1; -.
DR   SMR; Q0S7Q1; -.
DR   STRING; 101510.RHA1_ro04649; -.
DR   EnsemblBacteria; ABG96435; ABG96435; RHA1_ro04649.
DR   KEGG; rha:RHA1_ro04649; -.
DR   PATRIC; fig|101510.16.peg.4692; -.
DR   eggNOG; COG2070; Bacteria.
DR   HOGENOM; CLU_038732_1_1_11; -.
DR   OMA; IDDLPSC; -.
DR   UniPathway; UPA01058; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006707; P:cholesterol catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04730; NPD_like; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR004136; NMO.
DR   Pfam; PF03060; NMO; 2.
PE   3: Inferred from homology;
KW   Cholesterol metabolism; Flavoprotein; FMN; Lipid metabolism; NAD;
KW   Nucleotide-binding; Oxidoreductase; Reference proteome; Steroid metabolism;
KW   Sterol metabolism.
FT   CHAIN           1..353
FT                   /note="(3aS,4S,5R,7aS)-5-hydroxy-7a-methyl-1-oxo-octahydro-
FT                   1H-indene-4-carboxyl-CoA dehydrogenase"
FT                   /id="PRO_0000452308"
FT   BINDING         22..24
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I4V0"
FT   BINDING         171..173
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I4V0"
FT   BINDING         194..195
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I4V0"
SQ   SEQUENCE   353 AA;  36550 MW;  2AF75DACC9596EB7 CRC64;
     MSTLRTALTE LVGVQHPVVQ TGMGWVAGPR LVAGTANAGG LGILASATMT YTELESAITK
     TKTLTDKPFG VNIRADASDA PHRIDLLIRE SVRVASFALA PKQELIAKLK AAGVVVIPSI
     GAAKHAKKVA SWGADAVIVQ GGEGGGHTGP VATTLLLPSV LDAVDIPVVA AGGFYDGRGL
     AAALAYGAAG VAMGTRFLLT QESTVPDSVK HEYLARGLQD TTVSRKVDGM PHRVLNTDLV
     NSLEHSGNMR GLVAAARNAS KFKAMTGMKW STLVKDGLAM KKSSDRTWQQ IIMAANTPML
     LKAGLVEGNT HAGVLASGQV VGLLDDLPTC KDLIDGIVAD AIKRIDALGA LRA