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P12676

- CHOD_STRS0

UniProt

P12676 - CHOD_STRS0

Protein

Cholesterol oxidase

Gene

choA

Organism
Streptomyces sp. (strain SA-COO)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    Functioni

    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 activityi

    Cholesterol + O2 = cholest-5-en-3-one + H2O2.1 Publication
    A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid.1 Publication

    Cofactori

    FAD.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei398 – 3981Proton acceptor
    Active sitei484 – 4841

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi54 – 7017FADSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. cholesterol oxidase activity Source: UniProtKB-EC
    2. flavin adenine dinucleotide binding Source: InterPro
    3. steroid delta-isomerase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cholesterol metabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase, Oxidoreductase

    Keywords - Biological processi

    Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    UniPathwayiUPA00296.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cholesterol oxidase (EC:1.1.3.6)
    Short name:
    CHOD
    Alternative name(s):
    Cholesterol isomerase (EC:5.3.3.1)
    Gene namesi
    Name:choA
    OrganismiStreptomyces sp. (strain SA-COO)
    Taxonomic identifieri74576 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi398 – 3981E → Q: Reduced activity. 1 Publication
    Mutagenesisi484 – 4841H → N or Q: Reduced activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4242Tat-type signalAdd
    BLAST
    Chaini43 – 546504Cholesterol oxidasePRO_0000012333Add
    BLAST

    Post-translational modificationi

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

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    546
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni42 – 443
    Beta strandi47 – 537
    Helixi57 – 6812
    Beta strandi73 – 797
    Beta strandi89 – 924
    Beta strandi95 – 973
    Helixi100 – 1023
    Beta strandi103 – 1053
    Helixi116 – 1194
    Helixi120 – 1223
    Beta strandi132 – 1376
    Beta strandi142 – 1465
    Helixi151 – 1544
    Helixi165 – 1717
    Helixi177 – 1826
    Helixi184 – 1929
    Helixi199 – 2046
    Helixi206 – 2083
    Helixi209 – 22012
    Beta strandi225 – 2273
    Beta strandi230 – 2323
    Helixi234 – 2418
    Helixi249 – 2513
    Beta strandi259 – 2624
    Turni265 – 2684
    Helixi269 – 2757
    Beta strandi278 – 29215
    Beta strandi296 – 30510
    Beta strandi311 – 32414
    Helixi327 – 34014
    Turni349 – 3524
    Beta strandi361 – 3666
    Beta strandi383 – 3875
    Beta strandi395 – 4006
    Beta strandi410 – 4178
    Beta strandi425 – 4284
    Turni429 – 4324
    Beta strandi433 – 4364
    Helixi440 – 4434
    Helixi444 – 46118
    Beta strandi468 – 4736
    Beta strandi476 – 4783
    Beta strandi480 – 4845
    Turni491 – 4933
    Beta strandi499 – 5013
    Beta strandi505 – 5095
    Helixi512 – 5143
    Helixi524 – 54219

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP12676.
    SMRiP12676. Positions 45-545.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12676.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GMC oxidoreductase family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR000172. GMC_OxRdtase_N.
    IPR007867. GMC_OxRtase_C.
    IPR006311. TAT_signal.
    [Graphical view]
    PfamiPF05199. GMC_oxred_C. 1 hit.
    PF00732. GMC_oxred_N. 1 hit.
    [Graphical view]
    PROSITEiPS00623. GMC_OXRED_1. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P12676-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAQQHLSRR RMLGMAAFGA AALAGGTTIA APRAAAAAKS AADNGGYVPA    50
    VVIGTGYGAA VSALRLGEAG VQTLMLEMGQ LWNQPGPDGN IFCGMLNPDK 100
    RSSWFKNRTE APLGSFLWLD VVNRNIDPYA GVLDRVNYDQ MSVYVGRGVG 150
    GGSLVNGGMA VEPKRSYFEE ILPRVDSSEM YDRYFPRANS MLRVNHIDTK 200
    WFEDTEWYKF ARVSREQAGK AGLGTVFVPN VYDFGYMQRE AAGEVPKSAL 250
    ATEVIYGNNH GKQSLDKTYL AAALGTGKVT IQTLHQVKTI RQTKDGGYAL 300
    TVEQKDTDGK LLATKEISCR YLFLGAGSLG STELLVRARD TGTLPNLNSE 350
    VGAGWGPNGN IMTARANHMW NPTGAHQSSI PALGIDAWDN SDSSVFAEIA 400
    PMPAGLETWV SLYLAITKNP QRGTFVYDAA TDRAKLNWTR DQNAPAVNAA 450
    KALFDRINKA NGTIYRYDLF GTQLKAFADD FCYHPLGGCV LGKATDDYGR 500
    VAGYKNLYVT DGSLIPGSVG VNPFVTITAL AERNVERIIK QDVTAS 546
    Length:546
    Mass (Da):58,994
    Last modified:October 1, 1989 - v1
    Checksum:iEF22A1FE5EA68D21
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31939 Genomic DNA. Translation: AAA26719.1.
    PIRiA32260.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31939 Genomic DNA. Translation: AAA26719.1 .
    PIRi A32260.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B4V X-ray 1.50 A 43-546 [» ]
    1B8S X-ray 1.65 A 43-536 [» ]
    1CBO X-ray 1.80 A 43-546 [» ]
    1CC2 X-ray 2.20 A 43-546 [» ]
    1IJH X-ray 1.53 A 43-546 [» ]
    1MXT X-ray 0.95 A 43-546 [» ]
    1N1P X-ray 0.95 A 43-546 [» ]
    1N4U X-ray 0.95 A 43-546 [» ]
    1N4V X-ray 1.00 A 43-546 [» ]
    1N4W X-ray 0.92 A 43-546 [» ]
    2GEW X-ray 0.97 A 43-546 [» ]
    3B3R X-ray 0.98 A 42-546 [» ]
    3B6D X-ray 1.20 A 43-546 [» ]
    3CNJ X-ray 0.95 A 45-543 [» ]
    3GYI X-ray 1.00 A 43-546 [» ]
    3GYJ X-ray 0.92 A 43-546 [» ]
    ProteinModelPortali P12676.
    SMRi P12676. Positions 45-545.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00296 .

    Miscellaneous databases

    EvolutionaryTracei P12676.

    Family and domain databases

    InterProi IPR000172. GMC_OxRdtase_N.
    IPR007867. GMC_OxRtase_C.
    IPR006311. TAT_signal.
    [Graphical view ]
    Pfami PF05199. GMC_oxred_C. 1 hit.
    PF00732. GMC_oxred_N. 1 hit.
    [Graphical view ]
    PROSITEi PS00623. GMC_OXRED_1. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiCHOD_STRS0
    AccessioniPrimary (citable) accession number: P12676
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3