Q0S7M1 (CP125_RHOSR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Steroid C26-monooxygenase
EC=1.14.13.141

Alternative name(s):
Cholest-4-en-3-one 26-monooxygenase
Cytochrome P450 125
Steroid C27-monooxygenase

Gene names

Name:	cyp125
Ordered Locus Names:	RHA1_ro04679

Organism

Rhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP]

Taxonomic identifier

101510 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus › Rhodococcus jostii

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the C-27 hydroxylation of cholest-4-en-3-one and cholesterol and subsequently oxidizes the alcohol of the former to the cholest-4-en-3-one-27-oic acid via the aldehyde intermediate. Required to incorporate the cholesterol side-chain carbon atoms into cellular lipids. Ref.2
Catalytic activity	Cholest-4-en-3-one + NADH + O2 = 26-hydroxycholest-4-en-3-one + NAD+ + H2O.
Cofactor	Heme group. Ref.2
Disruption phenotype	Cells lacking this gene fail to grow in the presence of cholesterol. Ref.2
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Ligand	Heme Iron Metal-binding NAD
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular_function	cholest-4-en-3-one 26-monooxygenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 471	471	Steroid C26-monooxygenase		PRO_0000405334
Regions
	Region	160 – 164	5	Heme binding By similarity
	Region	236 – 238	3	Substrate binding By similarity
	Region	410 – 412	3	Heme binding By similarity
Sites
	Metal binding	412	1	Iron (heme axial ligand) By similarity
	Binding site	353	1	Heme By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0S7M1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: FB4819AAC2C52CF7	FASTA	471	52,795
	10 20 30 40 50 60 MGSFPCPQKI EQVLLSGQGL NELSFASRPA CASMLVERVP HHGVVYGLGQ ETAVAQPNLP 70 80 90 100 110 120 EGFDFTDPDV YAERIPYQEF AELRKTAPIW WNPQPPEIGG FHDDGYWVVS KLEDVKEVSR 130 140 150 160 170 180 RSDVFSTHEN TAIVRFADDI PRENIEMQRF ILINKDAPEH TKLRKLVSRG FTPRAINSLR 190 200 210 220 230 240 EELTERAEKI VKEAAESGAG DFVTQVACEL PLQAIAELLG VPQEDRLKVF DWSNQMTGYD 250 260 270 280 290 300 DPELDIDPQA ASMEILGYAY QMADERKKCP ADDIVTTLIE ADIDGNELSP EEFGFFVILL 310 320 330 340 350 360 AVAGNETTRN AITHGMMAFL DHPDQWELYK KERPKTTADE IVRWATPVNS FQRTALEDTE 370 380 390 400 410 420 LGGVQIKKGQ RVVMLYGSAN FDEDAFENPE KFDIMRENNP HVGFGGTGAH FCLGANLARL 430 440 450 460 470 EIDLIFNAIA DHLPDISKLG DPRRLRSGWL NGIKEFQVDY KTASGGCPVR H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse." McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H. , Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W., Eltis L.D. Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RHA1.
[2]	"Cytochrome P450 125 (CYP125) catalyses C26-hydroxylation to initiate sterol side-chain degradation in Rhodococcus jostii RHA1." Rosloniec K.Z., Wilbrink M.H., Capyk J.K., Mohn W.W., Ostendorf M., van der Geize R., Dijkhuizen L., Eltis L.D. Mol. Microbiol. 74:1031-1043(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CHOLESTEROL CATABOLISM, COFACTOR, DISRUPTION PHENOTYPE. Strain: RHA1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000431 Genomic DNA. Translation: ABG96465.1.
RefSeq	YP_704623.1. NC_008268.1.
3D structure databases
ProteinModelPortal	Q0S7M1.
ModBase	Search...
Protein-protein interaction databases
STRING	101510.RHA1_ro04679.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABG96465; ABG96465; RHA1_ro04679.
GeneID	4222230.
KEGG	rha:RHA1_ro04679.
PATRIC	23208275. VBIRhoJos26306_4722.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2124.
HOGENOM	HOG000243680.
KO	K15981.
OMA	QVDYTGK.
ProtClustDB	CLSK872196.
Enzyme and pathway databases
BioCyc	MetaCyc:RHA1_RO04679-MONOMER. RJOS101510:GJJ1-4676-MONOMER.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR002397. Cyt_P450_B. [Graphical view]
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00359. BP450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CP125_RHOSR

Accession

Primary (citable) accession number: Q0S7M1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 8, 2011
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program