CP125_RHOJR
ID CP125_RHOJR Reviewed; 471 AA.
AC Q0S7M1;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Steroid C26-monooxygenase {ECO:0000303|PubMed:19843222};
DE EC=1.14.15.29 {ECO:0000250|UniProtKB:P9WPP1, ECO:0000305|PubMed:19843222};
DE AltName: Full=Cholest-4-en-3-one 26-monooxygenase {ECO:0000303|PubMed:19843222};
DE AltName: Full=Cholest-4-en-3-one C26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming] {ECO:0000250|UniProtKB:P9WPP1, ECO:0000305|PubMed:19843222};
DE AltName: Full=Cholesterol C26-monooxygenase {ECO:0000303|PubMed:19843222};
DE AltName: Full=Cholesterol C26-monooxygenase [(25S)-3beta-hydroxycholest-5-en-26-oate forming] {ECO:0000250|UniProtKB:P9WPP1, ECO:0000305|PubMed:19843222};
DE AltName: Full=Cytochrome P450 125 {ECO:0000303|PubMed:19843222};
DE AltName: Full=Steroid C27-monooxygenase {ECO:0000303|PubMed:19843222};
GN Name=cyp125; OrderedLocusNames=RHA1_ro04679;
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 IN CHOLESTEROL CATABOLISM, CATALYTIC ACTIVITY, COFACTOR,
RP DISRUPTION PHENOTYPE, INDUCTION, AND SUBSTRATE SPECIFICITY.
RC STRAIN=RHA1;
RX PubMed=19843222; DOI=10.1111/j.1365-2958.2009.06915.x;
RA Rosloniec K.Z., Wilbrink M.H., Capyk J.K., Mohn W.W., Ostendorf M.,
RA van der Geize R., Dijkhuizen L., Eltis L.D.;
RT "Cytochrome P450 125 (CYP125) catalyses C26-hydroxylation to initiate
RT sterol side-chain degradation in Rhodococcus jostii RHA1.";
RL Mol. Microbiol. 74:1031-1043(2009).
CC -!- FUNCTION: Involved in the utilization of cholesterol as the sole carbon
CC and energy source by degrading the side chain. Primarily catalyzes the
CC sequential oxidation of the terminal methyl of cholest-4-en-3-one into
CC (25S)-26-hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-
CC 3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-
CC oxocholest-4-en-26-oate. Also able to sequentially oxidize cholesterol
CC itself, not only cholest-4-en-3-one. {ECO:0000269|PubMed:19843222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholest-4-en-3-one + 5 H(+) + 3 O2 + 6 reduced [2Fe-2S]-
CC [ferredoxin] = (25S)-3-oxocholest-4-en-26-oate + 4 H2O + 6 oxidized
CC [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:51564, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16175, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:71541; EC=1.14.15.29;
CC Evidence={ECO:0000250|UniProtKB:P9WPP1, ECO:0000305|PubMed:19843222};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:19843222};
CC -!- INDUCTION: By cholesterol. {ECO:0000305|PubMed:19843222}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow in the
CC presence of cholesterol. {ECO:0000269|PubMed:19843222}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; CP000431; ABG96465.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0S7M1; -.
DR SMR; Q0S7M1; -.
DR STRING; 101510.RHA1_ro04679; -.
DR EnsemblBacteria; ABG96465; ABG96465; RHA1_ro04679.
DR KEGG; rha:RHA1_ro04679; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_0_0_11; -.
DR OMA; QRFILIN; -.
DR BioCyc; MetaCyc:RHA1_RO04679-MON; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0036199; F:cholest-4-en-3-one 26-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW Cholesterol metabolism; Heme; Iron; Lipid degradation; Lipid metabolism;
KW Metal-binding; Monooxygenase; NAD; Oxidoreductase; Reference proteome;
KW Steroid metabolism; Sterol metabolism.
FT CHAIN 1..471
FT /note="Steroid C26-monooxygenase"
FT /id="PRO_0000405334"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WPP1"
FT BINDING 412
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P9WPP1"
SQ SEQUENCE 471 AA; 52795 MW; FB4819AAC2C52CF7 CRC64;
MGSFPCPQKI EQVLLSGQGL NELSFASRPA CASMLVERVP HHGVVYGLGQ ETAVAQPNLP
EGFDFTDPDV YAERIPYQEF AELRKTAPIW WNPQPPEIGG FHDDGYWVVS KLEDVKEVSR
RSDVFSTHEN TAIVRFADDI PRENIEMQRF ILINKDAPEH TKLRKLVSRG FTPRAINSLR
EELTERAEKI VKEAAESGAG DFVTQVACEL PLQAIAELLG VPQEDRLKVF DWSNQMTGYD
DPELDIDPQA ASMEILGYAY QMADERKKCP ADDIVTTLIE ADIDGNELSP EEFGFFVILL
AVAGNETTRN AITHGMMAFL DHPDQWELYK KERPKTTADE IVRWATPVNS FQRTALEDTE
LGGVQIKKGQ RVVMLYGSAN FDEDAFENPE KFDIMRENNP HVGFGGTGAH FCLGANLARL
EIDLIFNAIA DHLPDISKLG DPRRLRSGWL NGIKEFQVDY KTASGGCPVR H
