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P12676 (CHOD_STRS0) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cholesterol oxidase

Short name=CHOD
EC=1.1.3.6
Alternative name(s):
Cholesterol isomerase
EC=5.3.3.1
Gene names
Name:choA
OrganismStreptomyces sp. (strain SA-COO)
Taxonomic identifier74576 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme that catalyzes the oxidation of the 3-beta-hydroxy group of cholesterol and the isomerization of the double bond of the resulting product.

Catalytic activity

Cholesterol + O2 = cholest-5-en-3-one + H2O2. Ref.2

A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid. Ref.2

Cofactor

FAD.

Pathway

Steroid metabolism; cholesterol metabolism.

Subunit structure

Monomer.

Subcellular location

Secreted.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Sequence similarities

Belongs to the GMC oxidoreductase family.

Ontologies

Keywords
   Biological processCholesterol metabolism
Lipid metabolism
Steroid metabolism
Sterol metabolism
   Cellular componentSecreted
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionIsomerase
Oxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcholesterol metabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncholesterol oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

steroid delta-isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4242Tat-type signal
Chain43 – 546504Cholesterol oxidase
PRO_0000012333

Regions

Nucleotide binding54 – 7017FAD Potential

Sites

Active site3981Proton acceptor
Active site4841

Experimental info

Mutagenesis3981E → Q: Reduced activity.
Mutagenesis4841H → N or Q: Reduced activity.

Secondary structure

.......................................................................................... 546
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12676 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: EF22A1FE5EA68D21

FASTA54658,994
        10         20         30         40         50         60 
MTAQQHLSRR RMLGMAAFGA AALAGGTTIA APRAAAAAKS AADNGGYVPA VVIGTGYGAA 

        70         80         90        100        110        120 
VSALRLGEAG VQTLMLEMGQ LWNQPGPDGN IFCGMLNPDK RSSWFKNRTE APLGSFLWLD 

       130        140        150        160        170        180 
VVNRNIDPYA GVLDRVNYDQ MSVYVGRGVG GGSLVNGGMA VEPKRSYFEE ILPRVDSSEM 

       190        200        210        220        230        240 
YDRYFPRANS MLRVNHIDTK WFEDTEWYKF ARVSREQAGK AGLGTVFVPN VYDFGYMQRE 

       250        260        270        280        290        300 
AAGEVPKSAL ATEVIYGNNH GKQSLDKTYL AAALGTGKVT IQTLHQVKTI RQTKDGGYAL 

       310        320        330        340        350        360 
TVEQKDTDGK LLATKEISCR YLFLGAGSLG STELLVRARD TGTLPNLNSE VGAGWGPNGN 

       370        380        390        400        410        420 
IMTARANHMW NPTGAHQSSI PALGIDAWDN SDSSVFAEIA PMPAGLETWV SLYLAITKNP 

       430        440        450        460        470        480 
QRGTFVYDAA TDRAKLNWTR DQNAPAVNAA KALFDRINKA NGTIYRYDLF GTQLKAFADD 

       490        500        510        520        530        540 
FCYHPLGGCV LGKATDDYGR VAGYKNLYVT DGSLIPGSVG VNPFVTITAL AERNVERIIK 


QDVTAS 

« Hide

References

[1]"Nucleotide sequence of the gene for cholesterol oxidase from a Streptomyces sp."
Ishizaki T., Hirayama N., Shinkawa H., Nimi O., Murooka Y.
J. Bacteriol. 171:596-601(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants."
Yue Q.K., Kass I.J., Sampson N.S., Vrielink A.
Biochemistry 38:4277-4286(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), CATALYTIC ACTIVITY, MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31939 Genomic DNA. Translation: AAA26719.1.
PIRA32260.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4VX-ray1.50A43-546[»]
1B8SX-ray1.65A43-536[»]
1CBOX-ray1.80A43-546[»]
1CC2X-ray2.20A43-546[»]
1IJHX-ray1.53A43-546[»]
1MXTX-ray0.95A43-546[»]
1N1PX-ray0.95A43-546[»]
1N4UX-ray0.95A43-546[»]
1N4VX-ray1.00A43-546[»]
1N4WX-ray0.92A43-546[»]
2GEWX-ray0.97A43-546[»]
3B3RX-ray0.98A42-546[»]
3B6DX-ray1.20A43-546[»]
3CNJX-ray0.95A45-543[»]
3GYIX-ray1.00A43-546[»]
3GYJX-ray0.92A43-546[»]
ProteinModelPortalP12676.
SMRP12676. Positions 45-545.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00296.

Family and domain databases

InterProIPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
IPR006311. TAT_signal.
[Graphical view]
PfamPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PROSITEPS00623. GMC_OXRED_1. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12676.

Entry information

Entry nameCHOD_STRS0
AccessionPrimary (citable) accession number: P12676
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways