Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cholesterol oxidase

Gene

choB

Organism
Brevibacterium sterolicum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Pathway:icholesterol 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei406 – 4061Proton acceptor
Active sitei492 – 4921Proton acceptorBy similarity

Regions

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

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

BioCyciMetaCyc:MONOMER-16891.
BRENDAi1.1.3.6. 978.
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 lineageiBacteriaActinobacteriaMicrococcalesBrevibacteriaceaeBrevibacterium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4545Tat-type signalPROSITE-ProRule annotation1 PublicationAdd
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 – 627Combined sources
Helixi66 – 7712Combined sources
Beta strandi82 – 854Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi140 – 1456Combined sources
Beta strandi150 – 1545Combined sources
Helixi159 – 1624Combined sources
Helixi173 – 1797Combined sources
Helixi185 – 1906Combined sources
Helixi192 – 2009Combined sources
Helixi207 – 2126Combined sources
Helixi214 – 2163Combined sources
Helixi217 – 22812Combined sources
Beta strandi233 – 2353Combined sources
Beta strandi238 – 2403Combined sources
Helixi242 – 2498Combined sources
Turni257 – 2604Combined sources
Beta strandi267 – 2704Combined sources
Turni273 – 2764Combined sources
Helixi277 – 2837Combined sources
Beta strandi287 – 2904Combined sources
Beta strandi292 – 3009Combined sources
Beta strandi302 – 31312Combined sources
Beta strandi319 – 33214Combined sources
Helixi335 – 34814Combined sources
Turni357 – 3604Combined sources
Beta strandi368 – 3747Combined sources
Beta strandi391 – 3944Combined sources
Beta strandi403 – 4086Combined sources
Beta strandi418 – 4258Combined sources
Beta strandi433 – 4364Combined sources
Turni437 – 4404Combined sources
Beta strandi441 – 4444Combined sources
Helixi448 – 4514Combined sources
Helixi452 – 46918Combined sources
Beta strandi484 – 4863Combined sources
Beta strandi488 – 4914Combined sources
Turni499 – 5013Combined sources
Beta strandi515 – 5173Combined sources
Helixi520 – 5223Combined sources
Helixi532 – 54918Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

« Hide

        10         20         30         40         50
MTDSRANRAD ATRGVASVSR RRFLAGAGLT AGAIALSSMS TSASAAPSRT
60 70 80 90 100
LADGDRVPAL VIGSGYGGAV AALRLTQAGI PTQIVEMGRS WDTPGSDGKI
110 120 130 140 150
FCGMLNPDKR SMWLADKTDQ PVSNFMGFGI NKSIDRYVGV LDSERFSGIK
160 170 180 190 200
VYQGRGVGGG SLVNGGMAVT PKRNYFEEIL PSVDSNEMYN KYFPRANTGL
210 220 230 240 250
GVNNIDQAWF ESTEWYKFAR TGRKTAQRSG FTTAFVPNVY DFEYMKKEAA
260 270 280 290 300
GQVTKSGLGG EVIYGNNAGK KSLDKTYLAQ AAATGKLTIT TLHRVTKVAP
310 320 330 340 350
ATGSGYSVTM EQIDEQGNVV ATKVVTADRV FFAAGSVGTS KLLVSMKAQG
360 370 380 390 400
HLPNLSSQVG EGWGNNGNIM VGRANHMWDA TGSKQATIPT MGIDNWADPT
410 420 430 440 450
APIFAEIAPL PAGLETYVSL YLAITKNPER ARFQFNSGTG KVDLTWAQSQ
460 470 480 490 500
NQKGIDMAKK VFDKINQKEG TIYRTDLFGV YFKTWGDDFT YHPLGGVLLN
510 520 530 540 550
KATDNFGRLP EYPGLYVVDG SLVPGNVGVN PFVTITRLAE RNMDKIISSD

IQ
Length:552
Mass (Da):59,358
Last modified:May 1, 1992 - v2
Checksum:i74913FAED74B4F09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00712 Genomic DNA. Translation: BAA00617.1.
PIRiJQ1193.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00712 Genomic DNA. Translation: BAA00617.1.
PIRiJQ1193.

3D structure databases

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

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00296.
BioCyciMetaCyc:MONOMER-16891.
BRENDAi1.1.3.6. 978.

Miscellaneous databases

EvolutionaryTraceiP22637.

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]
ProtoNetiSearch...

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: July 22, 2015
This is version 107 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

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 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.