UniProtKB - Q6PQJ9 (5BPOR_DIGLA)
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>sp|Q6PQJ9|5BPOR_DIGLA 3-oxo-Delta(4,5)-steroid 5-beta-reductase OS=Digitalis lanata OX=49450 PE=1 SV=1 MSWWWAGAIGAAKKRLEEDDAQPKHSSVALIVGVTGIIGNSLAEILPLADTPGGPWKVYG VARRTRPAWHEDNPINYVQCDISDPDDSQAKLSPLTDVTHVFYVTWANRSTEQENCEANS KMFRNVLDAVIPNCPNLKHISLQTGRKHYMGPFESYGKIESHDPPYTEDLPRLKYMNFYY DLEDIMLEEVEKKEGLTWSVHRPGNIFGFSPYSMMNLVGTLCVYAAICKHEGKVLRFTGC KAAWDGYSDCSDADLIAEHHIWAAVDPYAKNEAFNVSNGDVFKWKHFWKVLAEQFGVGCG EYEEGVDLKLQDLMKGKEPVWEEIVRENGLTPTKLKDVGIWWFGDVILGNECFLDSMNKS KEHGFLGFRNSKNAFISWIDKAKAYKIVPOther tutorials and videosHelp videoFeedback
Protein
3-oxo-Delta(4,5)-steroid 5-beta-reductase
Gene
N/A
Organism
Digitalis lanata (Grecian foxglove)
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>Select a section on the left to see content.
<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
Involved in cardenolide biosynthesis. Catalyzes the stereospecific conversion of progesterone to 5-beta-pregnane-3,20-dione. Can use progesterone, testosterone, 4-androstene-3,17-dione, cortisol and cortisone as substrates, but not pregnenolone, 21-OH-pregnenolone or isoprogesterone. NADPH could not be replaced by NADH.2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.3"The crystal structure of progesterone 5beta-reductase from Digitalis lanata defines a novel class of short chain dehydrogenases/reductases."
Thorn A., Egerer-Sieber C., Jager C.M., Herl V., Muller-Uri F., Kreis W., Muller Y.A.
J. Biol. Chem. 283:17260-17269(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 26-389 IN COMPLEX WITH NADP, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITES, MUTAGENESIS OF TYR-179.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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
- 5β-cholestan-3-oneEC:1.3.1.3
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Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.3"The crystal structure of progesterone 5beta-reductase from Digitalis lanata defines a novel class of short chain dehydrogenases/reductases."
Thorn A., Egerer-Sieber C., Jager C.M., Herl V., Muller-Uri F., Kreis W., Muller Y.A.
J. Biol. Chem. 283:17260-17269(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 26-389 IN COMPLEX WITH NADP, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITES, MUTAGENESIS OF TYR-179.
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Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.3"The crystal structure of progesterone 5beta-reductase from Digitalis lanata defines a novel class of short chain dehydrogenases/reductases."
Thorn A., Egerer-Sieber C., Jager C.M., Herl V., Muller-Uri F., Kreis W., Muller Y.A.
J. Biol. Chem. 283:17260-17269(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 26-389 IN COMPLEX WITH NADP, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITES, MUTAGENESIS OF TYR-179.
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5β-cholestan-3-one- Search proteins in UniProtKB for this molecule.
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=cholest-4-en-3-one- Search proteins in UniProtKB for this molecule.
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- 4,5β-dihydrocortisoneEC:1.3.1.3
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Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.3"The crystal structure of progesterone 5beta-reductase from Digitalis lanata defines a novel class of short chain dehydrogenases/reductases."
Thorn A., Egerer-Sieber C., Jager C.M., Herl V., Muller-Uri F., Kreis W., Muller Y.A.
J. Biol. Chem. 283:17260-17269(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 26-389 IN COMPLEX WITH NADP, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITES, MUTAGENESIS OF TYR-179.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.3"The crystal structure of progesterone 5beta-reductase from Digitalis lanata defines a novel class of short chain dehydrogenases/reductases."
Thorn A., Egerer-Sieber C., Jager C.M., Herl V., Muller-Uri F., Kreis W., Muller Y.A.
J. Biol. Chem. 283:17260-17269(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 26-389 IN COMPLEX WITH NADP, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITES, MUTAGENESIS OF TYR-179.
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4,5β-dihydrocortisone- Search proteins in UniProtKB for this molecule.
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<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
- KM=120 µM for progesterone1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=291 µM for cortisol1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=228 µM for 4-androstene-3,17-dione1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=1.597 mM for cortexone1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=8 µM for NADPH1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=45 nmol/sec/mg enzyme with progesterone as substrate1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=81.2 nmol/sec/mg enzyme with cortisol as substrate1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=18.5 nmol/sec/mg enzyme with 4-androstene-3,17-dione as substrate1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=63.3 nmol/sec/mg enzyme with cortexone as substrate1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=31.1 nmol/sec/mg enzyme with NADPH as substrate1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
pH dependencei
Optimum pH is 7.8.1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
Temperature dependencei
Optimum temperature is 40 degrees Celsius.1 Publication
Manual assertion based on experiment ini
- Ref.1"Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh."
Herl V., Fischer G., Muller-Uri F., Kreis W.
Phytochemistry 67:225-231(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei | 105 | NADP1 Publication Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 143 | NADP1 Publication Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei | 147 | 1 Publication Manual assertion based on experiment ini
| 1 | |
| Active sitei | 179 | 1 Publication Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 179 | NADP1 Publication Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 206 | NADP; via amide nitrogen1 Publication Manual assertion based on experiment ini
| 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi | 35 – 37 | NADP1 Publication Manual assertion based on experiment ini
| 3 | |
| Nucleotide bindingi | 63 – 64 | NADP1 Publication Manual assertion based on experiment ini
| 2 | |
| Nucleotide bindingi | 81 – 82 | NADP1 Publication Manual assertion based on experiment ini
| 2 | |
| Nucleotide bindingi | 213 – 215 | NADP1 Publication Manual assertion based on experiment ini
| 3 |
<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
- coenzyme binding Source: InterPro
- delta4-3-oxosteroid 5beta-reductase activity Source: UniProtKB-EC
- nucleotide binding Source: UniProtKB-KW
<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 function | Oxidoreductase |
| Ligand | NADP, Nucleotide-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:MONOMER-14261 |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.3.99.6 1947 |
<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_and_taxonomy_section">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: 3-oxo-Delta(4,5)-steroid 5-beta-reductase (EC:1.3.1.3
Manual assertion based on experiment ini
Alternative name(s): Delta(4)-3-oxosteroid 5-beta-reductase Delta-4,5-steroid 5-beta-reductase Short name: At5beta-StR Progesterone 5-beta-reductase Short name: 5beta-POR |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>Organismi | Digitalis lanata (Grecian foxglove) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri | 49450 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineagei | cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliopsida › Mesangiospermae › eudicotyledons › Gunneridae › Pentapetalae › asterids › lamiids › Lamiales › Plantaginaceae › Digitalideae › Digitalis |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi | 179 | Y → A or F: Complete loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000420239 | 1 – 389 | 3-oxo-Delta(4,5)-steroid 5-beta-reductaseAdd BLAST | 389 |
<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer.
1 PublicationManual assertion based on experiment ini
- Ref.3"The crystal structure of progesterone 5beta-reductase from Digitalis lanata defines a novel class of short chain dehydrogenases/reductases."
Thorn A., Egerer-Sieber C., Jager C.M., Herl V., Muller-Uri F., Kreis W., Muller Y.A.
J. Biol. Chem. 283:17260-17269(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 26-389 IN COMPLEX WITH NADP, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITES, MUTAGENESIS OF TYR-179.
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 27 – 33 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 37 – 45 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 55 – 64 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 76 – 79 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 85 – 92 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 100 – 103 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 112 – 130 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 131 – 133 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 139 – 143 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 147 – 150 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 153 – 155 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 156 – 158 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 164 – 166 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 168 – 170 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 178 – 190 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 197 – 207 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 217 – 231 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| Helixi | 241 – 245 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 253 – 265 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Helixi | 267 – 269 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 272 – 276 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 284 – 295 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Beta strandi | 304 – 306 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 310 – 313 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 314 – 316 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 318 – 327 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 335 – 338 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 341 – 348 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 358 – 362 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 371 – 384 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q6PQJ9 |
Database of comparative protein structure models More...ModBasei | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q6PQJ9 |
<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
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001509 Epimerase_deHydtase IPR036291 NAD(P)-bd_dom_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF01370 Epimerase, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51735 SSF51735, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.
Q6PQJ9-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MSWWWAGAIG AAKKRLEEDD AQPKHSSVAL IVGVTGIIGN SLAEILPLAD
60 70 80 90 100
TPGGPWKVYG VARRTRPAWH EDNPINYVQC DISDPDDSQA KLSPLTDVTH
110 120 130 140 150
VFYVTWANRS TEQENCEANS KMFRNVLDAV IPNCPNLKHI SLQTGRKHYM
160 170 180 190 200
GPFESYGKIE SHDPPYTEDL PRLKYMNFYY DLEDIMLEEV EKKEGLTWSV
210 220 230 240 250
HRPGNIFGFS PYSMMNLVGT LCVYAAICKH EGKVLRFTGC KAAWDGYSDC
260 270 280 290 300
SDADLIAEHH IWAAVDPYAK NEAFNVSNGD VFKWKHFWKV LAEQFGVGCG
310 320 330 340 350
EYEEGVDLKL QDLMKGKEPV WEEIVRENGL TPTKLKDVGI WWFGDVILGN
360 370 380
ECFLDSMNKS KEHGFLGFRN SKNAFISWID KAKAYKIVP
Length:389
Mass (Da):44,071
Last modified:July 5, 2004 - 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:i184B9EDCDDC26E04
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AY574950 mRNA Translation: AAS76634.1 AY585867 Genomic DNA Translation: AAS93804.1 |
<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
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q6PQJ9 | Putative progesterone 5-beta-reductase | 389 | UniRef90_Q6PQJ9 | |||
| Progesterone 5-beta-reductase | 389 | |||||
| Progesterone 5-beta-reductase | 389 | |||||
| Progesterone 5-beta-reductase | 389 | |||||
| Progesterone 5 beta reductase | 389 | |||||
| +25 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q6PQJ9 | 3-oxo-Delta(4,5)-steroid 5-beta-reductase | ) | 388 | UniRef50_Q9STX2 | ||
| Iridoid synthase CYC2 | 390 | |||||
| Putative progesterone 5beta-reductase | 392 | |||||
| Putative enone 5-beta-reductase | 392 | |||||
| 3-oxo-Delta(4,5)-steroid 5-beta-reductase | 391 | |||||
| +437 | ||||||
<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 | AY574950 mRNA Translation: AAS76634.1 AY585867 Genomic DNA Translation: AAS93804.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2V6F | X-ray | 2.40 | A | 26-389 | [»] | |
| 2V6G | X-ray | 2.30 | A | 26-389 | [»] | |
| SMRi | Q6PQJ9 | |||||
| ModBasei | Search... | |||||
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Enzyme and pathway databases
| BioCyci | MetaCyc:MONOMER-14261 |
| BRENDAi | 1.3.99.6 1947 |
Miscellaneous databases
| EvolutionaryTracei | Q6PQJ9 |
Family and domain databases
| InterProi | View protein in InterPro IPR001509 Epimerase_deHydtase IPR036291 NAD(P)-bd_dom_sf |
| Pfami | View protein in Pfam PF01370 Epimerase, 1 hit |
| SUPFAMi | SSF51735 SSF51735, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
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 namei | 5BPOR_DIGLA | |
| <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>Accessioni | Q6PQJ9Primary (citable) accession number: Q6PQJ9 | |
| <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 28, 2012 |
| Last sequence update: | July 5, 2004 | |
| Last modified: | July 31, 2019 | |
| This is version 62 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Plant 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-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
