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P12676

- CHOD_STRS0

UniProt

P12676 - CHOD_STRS0

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Protein

Cholesterol oxidase

Gene

choA

Organism
Streptomyces sp. (strain SA-COO)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MTAQQHLSRR RMLGMAAFGA AALAGGTTIA APRAAAAAKS AADNGGYVPA
60 70 80 90 100
VVIGTGYGAA VSALRLGEAG VQTLMLEMGQ LWNQPGPDGN IFCGMLNPDK
110 120 130 140 150
RSSWFKNRTE APLGSFLWLD VVNRNIDPYA GVLDRVNYDQ MSVYVGRGVG
160 170 180 190 200
GGSLVNGGMA VEPKRSYFEE ILPRVDSSEM YDRYFPRANS MLRVNHIDTK
210 220 230 240 250
WFEDTEWYKF ARVSREQAGK AGLGTVFVPN VYDFGYMQRE AAGEVPKSAL
260 270 280 290 300
ATEVIYGNNH GKQSLDKTYL AAALGTGKVT IQTLHQVKTI RQTKDGGYAL
310 320 330 340 350
TVEQKDTDGK LLATKEISCR YLFLGAGSLG STELLVRARD TGTLPNLNSE
360 370 380 390 400
VGAGWGPNGN IMTARANHMW NPTGAHQSSI PALGIDAWDN SDSSVFAEIA
410 420 430 440 450
PMPAGLETWV SLYLAITKNP QRGTFVYDAA TDRAKLNWTR DQNAPAVNAA
460 470 480 490 500
KALFDRINKA NGTIYRYDLF GTQLKAFADD FCYHPLGGCV LGKATDDYGR
510 520 530 540
VAGYKNLYVT DGSLIPGSVG VNPFVTITAL AERNVERIIK QDVTAS
Length:546
Mass (Da):58,994
Last modified:October 1, 1989 - v1
Checksum:iEF22A1FE5EA68D21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31939 Genomic DNA. Translation: AAA26719.1.
PIRiA32260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31939 Genomic DNA. Translation: AAA26719.1 .
PIRi A32260.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Chemistry

DrugBanki DB03147. Flavin adenine dinucleotide.

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: November 26, 2014
This is version 106 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