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Protein

Cholesterol oxidase

Gene

choB

Organism
Brevibacterium sterolicum
Status
Reviewed-Annotation score: -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-Delta5-steroid = a 3-oxo-Delta4-steroid.

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 sitei406Proton acceptor1
Active sitei492Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi63 – 79FADAdd BLAST17

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Oxidoreductase
Biological processCholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16891
BRENDAi1.1.3.6 978
UniPathwayi
UPA00296

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147 Flavin adenine dinucleotide
DB01708 Prasterone

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 45Tat-type signalPROSITE-ProRule annotation1 PublicationAdd BLAST45
ChainiPRO_000001233246 – 552Cholesterol oxidaseAdd BLAST507

Post-translational modificationi

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

Proteomic databases

PRIDEiP22637

Structurei

Secondary structure

1552
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP22637
SMRiP22637
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22637

Family & Domainsi

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.50.50.60, 1 hit
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR000172 GMC_OxRdtase_N
IPR007867 GMC_OxRtase_C
IPR006311 TAT_signal
PfamiView protein in Pfam
PF05199 GMC_oxred_C, 1 hit
PF00732 GMC_oxred_N, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
PROSITEiView protein in PROSITE
PS00623 GMC_OXRED_1, 1 hit
PS51318 TAT, 1 hit

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

Similar proteinsi

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1COYX-ray1.80A46-552[»]
3COXX-ray1.80A46-552[»]
ProteinModelPortaliP22637
SMRiP22637
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB03147 Flavin adenine dinucleotide
DB01708 Prasterone

Proteomic databases

PRIDEiP22637

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00296

BioCyciMetaCyc:MONOMER-16891
BRENDAi1.1.3.6 978

Miscellaneous databases

EvolutionaryTraceiP22637

Family and domain databases

Gene3Di3.50.50.60, 1 hit
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR000172 GMC_OxRdtase_N
IPR007867 GMC_OxRtase_C
IPR006311 TAT_signal
PfamiView protein in Pfam
PF05199 GMC_oxred_C, 1 hit
PF00732 GMC_oxred_N, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
PROSITEiView protein in PROSITE
PS00623 GMC_OXRED_1, 1 hit
PS51318 TAT, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCHOD_BREST
AccessioniPrimary (citable) accession number: P22637
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: May 1, 1992
Last modified: November 7, 2018
This is version 119 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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