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Protein

Cholesterol oxidase

Gene

choA

Organism
Streptomyces sp. (strain SA-COO)
Status
Reviewed-Annotation score: 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: cholesterol metabolism

This protein is involved in the pathway cholesterol metabolism, which is part of Steroid metabolism.
View all proteins of this organism that are known to be involved in the pathway cholesterol metabolism and in Steroid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei398Proton acceptor1
Active sitei484Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi54 – 70FADSequence analysisAdd BLAST17

GO - Molecular functioni

GO - Biological processi

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

BRENDAi1.1.3.6. 1284.
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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi398E → Q: Reduced activity. 1 Publication1
Mutagenesisi484H → N or Q: Reduced activity. 1 Publication1

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 42Tat-type signalAdd BLAST42
ChainiPRO_000001233343 – 546Cholesterol oxidaseAdd BLAST504

Post-translational modificationi

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

Proteomic databases

PRIDEiP12676.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1546
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni42 – 44Combined sources3
Beta strandi47 – 53Combined sources7
Helixi57 – 68Combined sources12
Beta strandi73 – 79Combined sources7
Beta strandi89 – 92Combined sources4
Beta strandi95 – 97Combined sources3
Helixi100 – 102Combined sources3
Beta strandi103 – 105Combined sources3
Helixi116 – 119Combined sources4
Helixi120 – 122Combined sources3
Beta strandi132 – 137Combined sources6
Beta strandi142 – 146Combined sources5
Helixi151 – 154Combined sources4
Helixi165 – 171Combined sources7
Helixi177 – 182Combined sources6
Helixi184 – 191Combined sources8
Helixi199 – 204Combined sources6
Helixi206 – 208Combined sources3
Helixi209 – 220Combined sources12
Beta strandi225 – 227Combined sources3
Beta strandi230 – 232Combined sources3
Helixi234 – 241Combined sources8
Helixi249 – 251Combined sources3
Beta strandi259 – 262Combined sources4
Turni265 – 268Combined sources4
Helixi269 – 275Combined sources7
Beta strandi278 – 292Combined sources15
Beta strandi296 – 305Combined sources10
Beta strandi311 – 324Combined sources14
Helixi327 – 340Combined sources14
Turni349 – 352Combined sources4
Beta strandi361 – 366Combined sources6
Beta strandi383 – 387Combined sources5
Beta strandi395 – 400Combined sources6
Beta strandi410 – 417Combined sources8
Beta strandi425 – 428Combined sources4
Turni429 – 432Combined sources4
Beta strandi433 – 436Combined sources4
Helixi440 – 443Combined sources4
Helixi444 – 461Combined sources18
Beta strandi468 – 473Combined sources6
Beta strandi476 – 478Combined sources3
Beta strandi480 – 484Combined sources5
Turni491 – 493Combined sources3
Beta strandi499 – 501Combined sources3
Beta strandi505 – 509Combined sources5
Helixi512 – 514Combined sources3
Helixi524 – 542Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4REKX-ray0.74A46-544[»]
4U2LX-ray1.34A43-546[»]
4U2SX-ray1.12A43-546[»]
4U2TX-ray1.22A43-546[»]
4XWRX-ray1.10A43-546[»]
4XXGX-ray0.85A43-546[»]
ProteinModelPortaliP12676.
SMRiP12676.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12676.

Family & Domainsi

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR000172. 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]
SUPFAMiSSF51905. SSF51905. 2 hits.
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.
PIRiA32260.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4REKX-ray0.74A46-544[»]
4U2LX-ray1.34A43-546[»]
4U2SX-ray1.12A43-546[»]
4U2TX-ray1.22A43-546[»]
4XWRX-ray1.10A43-546[»]
4XXGX-ray0.85A43-546[»]
ProteinModelPortaliP12676.
SMRiP12676.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Proteomic databases

PRIDEiP12676.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00296.
BRENDAi1.1.3.6. 1284.

Miscellaneous databases

EvolutionaryTraceiP12676.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR000172. 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]
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS00623. GMC_OXRED_1. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 118 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.