Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 132 (23 Feb 2022)
Sequence version 1 (01 Oct 1989)
Previous versions | rss
Add a publicationFeedback
Protein

Cholesterol oxidase

Gene

choA

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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, producing cholest-4-en-3-one. These reactions are part of a cholesterol degradation pathway that allows the bacterium to utilize cholesterol as its sole source of carbon and energy.

1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FAD1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 44 sec(-1) for the oxidation of cholesterol. kcat is 64 sec(-1) for the isomerization of cholest-5-en-3-one.1 Publication
  1. KM=3.0 µM for cholesterol1 Publication
  2. KM=6.2 µM for cholest-5-en-3-one1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: cholesterol degradation

This protein is involved in the pathway cholesterol degradation, which is part of Steroid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway cholesterol degradation and in Steroid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei77FADCombined sources1
Binding sitei152FAD; via amide nitrogenCombined sources1
Binding sitei287FAD; via amide nitrogen and carbonyl oxygenCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei398Proton acceptor1 Publication1
Binding sitei483FADCombined sources1
Active sitei484Proton acceptor1 Publication1
Binding sitei512FAD; via amide nitrogenCombined sources1
Binding sitei524FAD; via amide nitrogenCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi57 – 58FADCombined sources2
Nucleotide bindingi156 – 159FADCombined sources4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.3.6, 1284

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA01058

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cholesterol oxidase (EC:1.1.3.61 Publication)
Short name:
CHOD
Alternative name(s):
Cholesterol isomerase (EC:5.3.3.11 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:choA
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiStreptomyces sp. (strain SA-COO)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri74576 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi398E → Q: Mutant does not catalyze isomerization (>10000-fold reduced), and oxidation activity is 30-fold lower than wild type. 1 Publication1
Mutagenesisi484H → D or E: Mutants do not catalyze oxidation (>100000-fold reduced), but do catalyze isomerization, 10000 times slower than wild type. 1 Publication1
Mutagenesisi484H → K: Mutant is inactive in both oxidation (>100000-fold reduced) and isomerization assays (>10000-fold reduced). 1 Publication1
Mutagenesisi484H → N: Mutant activity is 4400-fold lower than wild type for oxidation, and is 30-fold lower than wild type for isomerization. 1 Publication1
Mutagenesisi484H → Q: Mutant activity is 120-fold lower than wild type for oxidation, and the same as wild type for isomerization. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03147, Flavin adenine dinucleotide
DB02332, Flavin-N7 protonated-adenine dinucleotide

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 42Tat-type signalAdd BLAST42
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001233343 – 546Cholesterol oxidaseAdd BLAST504

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1546
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P12676

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P12676

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.50.50.60, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036188, FAD/NAD-bd_sf
IPR000172, GMC_OxRdtase_N
IPR007867, GMC_OxRtase_C
IPR006311, TAT_signal

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05199, GMC_oxred_C, 1 hit
PF00732, GMC_oxred_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51905, SSF51905, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00623, GMC_OXRED_1, 1 hit
PS51318, TAT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iEF22A1FE5EA68D21
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M31939 Genomic DNA Translation: AAA26719.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A32260

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B4VX-ray1.50A43-546[»]
1B8SX-ray1.65A43-546[»]
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[»]
5KWFOther1.50A43-546[»]
SMRiP12676
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

DrugBankiDB03147, Flavin adenine dinucleotide
DB02332, Flavin-N7 protonated-adenine dinucleotide

Enzyme and pathway databases

UniPathwayiUPA01058
BRENDAi1.1.3.6, 1284

Miscellaneous databases

EvolutionaryTraceiP12676

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

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCHOD_STRS0
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P12676
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: February 23, 2022
This is version 132 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again