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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

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

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 databases

DrugBankiDB03147. Flavin adenine dinucleotide.

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.

Structurei

Secondary structure

1552
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi56 – 62Combined sources7
Helixi66 – 77Combined sources12
Beta strandi82 – 85Combined sources4
Beta strandi104 – 106Combined sources3
Beta strandi111 – 114Combined sources4
Beta strandi140 – 145Combined sources6
Beta strandi150 – 154Combined sources5
Helixi159 – 162Combined sources4
Helixi173 – 179Combined sources7
Helixi185 – 190Combined sources6
Helixi192 – 200Combined sources9
Helixi207 – 212Combined sources6
Helixi214 – 216Combined sources3
Helixi217 – 228Combined sources12
Beta strandi233 – 235Combined sources3
Beta strandi238 – 240Combined sources3
Helixi242 – 249Combined sources8
Turni257 – 260Combined sources4
Beta strandi267 – 270Combined sources4
Turni273 – 276Combined sources4
Helixi277 – 283Combined sources7
Beta strandi287 – 290Combined sources4
Beta strandi292 – 300Combined sources9
Beta strandi302 – 313Combined sources12
Beta strandi319 – 332Combined sources14
Helixi335 – 348Combined sources14
Turni357 – 360Combined sources4
Beta strandi368 – 374Combined sources7
Beta strandi391 – 394Combined sources4
Beta strandi403 – 408Combined sources6
Beta strandi418 – 425Combined sources8
Beta strandi433 – 436Combined sources4
Turni437 – 440Combined sources4
Beta strandi441 – 444Combined sources4
Helixi448 – 451Combined sources4
Helixi452 – 469Combined sources18
Beta strandi484 – 486Combined sources3
Beta strandi488 – 491Combined sources4
Turni499 – 501Combined sources3
Beta strandi515 – 517Combined sources3
Helixi520 – 522Combined sources3
Helixi532 – 549Combined sources18

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...

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. 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.

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

Chemistry databases

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

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_BREST
AccessioniPrimary (citable) accession number: P22637
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: May 1, 1992
Last modified: November 2, 2016
This is version 112 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

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.