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P22637

- CHOD_BREST

UniProt

P22637 - CHOD_BREST

Protein

Cholesterol oxidase

Gene

choB

Organism
Brevibacterium sterolicum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (01 May 1992)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidation and isomerization of cholesterol to cholestenone (4-cholesten-3-one), which is an initial step in the cholesterol degradation process.

    Catalytic activityi

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

    Cofactori

    FAD.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei406 – 4061Proton acceptor
    Active sitei492 – 4921By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi63 – 7917FADAdd
    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

    BioCyciMetaCyc:MONOMER-16891.
    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:choB
    OrganismiBrevibacterium sterolicum
    Taxonomic identifieri1702 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeBrevibacteriaceaeBrevibacterium

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4545Tat-type signal1 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Chaini46 – 552507Cholesterol oxidasePRO_0000012332Add
    BLAST

    Post-translational modificationi

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

    Structurei

    Secondary structure

    1
    552
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi56 – 627
    Helixi66 – 7712
    Beta strandi82 – 854
    Beta strandi104 – 1063
    Beta strandi111 – 1144
    Beta strandi140 – 1456
    Beta strandi150 – 1545
    Helixi159 – 1624
    Helixi173 – 1797
    Helixi185 – 1906
    Helixi192 – 2009
    Helixi207 – 2126
    Helixi214 – 2163
    Helixi217 – 22812
    Beta strandi233 – 2353
    Beta strandi238 – 2403
    Helixi242 – 2498
    Turni257 – 2604
    Beta strandi267 – 2704
    Turni273 – 2764
    Helixi277 – 2837
    Beta strandi287 – 2904
    Beta strandi292 – 3009
    Beta strandi302 – 31312
    Beta strandi319 – 33214
    Helixi335 – 34814
    Turni357 – 3604
    Beta strandi368 – 3747
    Beta strandi391 – 3944
    Beta strandi403 – 4086
    Beta strandi418 – 4258
    Beta strandi433 – 4364
    Turni437 – 4404
    Beta strandi441 – 4444
    Helixi448 – 4514
    Helixi452 – 46918
    Beta strandi484 – 4863
    Beta strandi488 – 4914
    Turni499 – 5013
    Beta strandi515 – 5173
    Helixi520 – 5223
    Helixi532 – 54918

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1COYX-ray1.80A46-552[»]
    3COXX-ray1.80A46-552[»]
    ProteinModelPortaliP22637.
    SMRiP22637. Positions 49-551.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22637.

    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.

    P22637-1 [UniParc]FASTAAdd to Basket

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    MTDSRANRAD ATRGVASVSR RRFLAGAGLT AGAIALSSMS TSASAAPSRT    50
    LADGDRVPAL VIGSGYGGAV AALRLTQAGI PTQIVEMGRS WDTPGSDGKI 100
    FCGMLNPDKR SMWLADKTDQ PVSNFMGFGI NKSIDRYVGV LDSERFSGIK 150
    VYQGRGVGGG SLVNGGMAVT PKRNYFEEIL PSVDSNEMYN KYFPRANTGL 200
    GVNNIDQAWF ESTEWYKFAR TGRKTAQRSG FTTAFVPNVY DFEYMKKEAA 250
    GQVTKSGLGG EVIYGNNAGK KSLDKTYLAQ AAATGKLTIT TLHRVTKVAP 300
    ATGSGYSVTM EQIDEQGNVV ATKVVTADRV FFAAGSVGTS KLLVSMKAQG 350
    HLPNLSSQVG EGWGNNGNIM VGRANHMWDA TGSKQATIPT MGIDNWADPT 400
    APIFAEIAPL PAGLETYVSL YLAITKNPER ARFQFNSGTG KVDLTWAQSQ 450
    NQKGIDMAKK VFDKINQKEG TIYRTDLFGV YFKTWGDDFT YHPLGGVLLN 500
    KATDNFGRLP EYPGLYVVDG SLVPGNVGVN PFVTITRLAE RNMDKIISSD 550
    IQ 552
    Length:552
    Mass (Da):59,358
    Last modified:May 1, 1992 - v2
    Checksum:i74913FAED74B4F09
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00712 Genomic DNA. Translation: BAA00617.1.
    PIRiJQ1193.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00712 Genomic DNA. Translation: BAA00617.1 .
    PIRi JQ1193.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1COY X-ray 1.80 A 46-552 [» ]
    3COX X-ray 1.80 A 46-552 [» ]
    ProteinModelPortali P22637.
    SMRi P22637. Positions 49-551.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00296 .
    BioCyci MetaCyc:MONOMER-16891.

    Miscellaneous databases

    EvolutionaryTracei P22637.

    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. "Sequence of gene choB encoding cholesterol oxidase of Brevibacterium sterolicum: comparison with choA of streptomyces sp. SA-COO."
      Ohta T., Fujishiro K., Yamaguchi K., Tamura Y., Aisaka K., Uwajima T., Hasegawa M.
      Gene 103:93-96(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 46-55.
      Strain: ATCC 21387 / NCIB 11161.
    2. "Isolation and identification of the gene of cholesterol oxidase from Brevibacterium sterolicum ATCC 21387, a widely used enzyme in clinical analysis."
      Fujishiro K., Ota T., Hasegawa M., Yamaguchi K., Mizukami T., Uwajima T.
      Biochem. Biophys. Res. Commun. 172:721-727(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-552, PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 21387 / NCIB 11161.
    3. Erratum
      Fujishiro K., Ota T., Hasegawa M., Yamaguchi K., Mizukami T., Uwajima T.
      Biochem. Biophys. Res. Commun. 173:1384-1384(1990)
    4. "Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8-A resolution."
      Vrielink A., Lloyld L.F., Blow D.M.
      J. Mol. Biol. 219:533-554(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiCHOD_BREST
    AccessioniPrimary (citable) accession number: P22637
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 101 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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