UniProtKB - P07445 (SDIS_PSEPU)
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- BLAST>sp|P07445|SDIS_PSEPU Steroid Delta-isomerase OS=Pseudomonas putida OX=303 GN=ksi PE=1 SV=1 MNLPTAQEVQGLMARYIELVDVGDIEAIVQMYADDATVEDPFGQPPIHGREQIAAFYRQG LGGGKVRACLTGPVRASHNGCGAMPFRVEMVWNGQPCALDVIDVMRFDEHGRIQTMQAYW SEVNLSVREPQ
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Steroid Delta-isomerase
ksi
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
<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. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ 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 | 16 | Proton donor | 1 | |
| <p>This subsection of the ‘Function’ 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 | 40 | Proton acceptor | 1 | |
| <p>This subsection of the ‘Function’ 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 | 103 | Substrate1 Publication <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
| 1 |
<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
- steroid delta-isomerase activity Source: UniProtKB-EC
<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 - Biological processi
- steroid metabolic process 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 | Isomerase |
| Biological process | Lipid metabolism, Steroid metabolism |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 5.3.3.1 5092 |
<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: Steroid Delta-isomerase (EC:5.3.3.1)Alternative name(s): Delta(5)-3-ketosteroid isomerase |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:ksi |
| <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 | Pseudomonas putida (Arthrobacter siderocapsulatus) |
| <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 | 303 [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 › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas putida group |
<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 | 16 | Y → F: Reduces activity 2000-fold. Reduces activity 10000-fold; when associated with E-103; N-103 or L-103. 3 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
| 1 | |
| <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 | 16 | Y → S: Reduces activity 20-fold. 3 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
| 1 | |
| <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 | 32 | Y → S: Reduces activity 4-fold. 1 Publication <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
| 1 | |
| <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 | 57 | Y → S: Reduces activity 100-fold. | 1 | |
| <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 | 92 | W → A: Slightly reduces activity. Reduces protein stability. | 1 | |
| <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 | 103 | D → A or L: Reduces activity 100-fold. Reduces activity 10000-fold; when associated with F-16. 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
| 1 | |
| <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 | 103 | D → E: Slightly reduces activity. Reduces activity 10000-fold; when associated with F-16. 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
| 1 | |
| <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 | 103 | D → N: Reduces activity 4-fold. Reduces activity 10000-fold; when associated with F-16. 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
| 1 | |
| <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 | 125 | L → A: Slightly reduces activity and reduces protein stability; when associated with A-127. 1 Publication <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
| 1 | |
| <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 | 127 | V → A: Slightly reduces activity and reduces protein stability; when associated with A-125. 1 Publication <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
| 1 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2321641 |
Drug and drug target database More...DrugBanki | DB03619 Deoxycholic Acid DB03515 Equilenin DB01708 Prasterone |
<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_0000097646 | 1 – 131 | Steroid Delta-isomeraseAdd BLAST | 131 |
Proteomic databases
PRoteomics IDEntifications database More...PRIDEi | P07445 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<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
<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.3"High-resolution crystal structures of delta5-3-ketosteroid isomerase with and without a reaction intermediate analogue."
Kim S.-W., Cha S.-S., Cho H.-S., Kim J.-S., Ha N.-C., Cho M.-J., Joo S., Kim K.-K., Choi K.-Y., Oh B.-H.
Biochemistry 36:14030-14036(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH REACTION INTERMEDIATE ANALOG, MUTAGENESIS OF TYR-16 AND ASP-103. - Ref.5"Asp-99 donates a hydrogen bond not to Tyr-14 but to the steroid directly in the catalytic mechanism of delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B."
Choi G., Ha N.-C., Kim S.W., Kim D.-H., Park S., Oh B.-H., Choi K.-Y.
Biochemistry 39:903-909(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT ASN-40/GLU-103 IN COMPLEX WITH REACTION INTERMEDIATE ANALOG, MUTAGENESIS OF TYR-16 AND ASP-103. - Ref.6"Detection of large pKa perturbations of an inhibitor and a catalytic group at an enzyme active site, a mechanistic basis for catalytic power of many enzymes."
Ha N.-C., Kim M.-S., Lee W., Choi K.-Y., Oh B.-H.
J. Biol. Chem. 275:41100-41106(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P07445 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ 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 | 6 – 22 | 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 | 17 | |
| <p>This subsection of the ‘Structure’ 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 | 25 – 31 | 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 ‘Structure’ 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 | 32 – 41 | 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 | 10 | |
| <p>This subsection of the ‘Structure’ 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 | 49 – 61 | 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 | 13 | |
| <p>This subsection of the ‘Structure’ 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 | 62 – 64 | 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 | 3 | |
| <p>This subsection of the ‘Structure’ 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 | 67 – 72 | 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 | 6 | |
| <p>This subsection of the ‘Structure’ 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 | 78 – 107 | 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 | 30 | |
| <p>This subsection of the ‘Structure’ 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 | 113 – 119 | 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 ‘Structure’ 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 | 122 – 124 | 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 | 3 | |
| <p>This subsection of the ‘Structure’ 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 | 125 – 127 | 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 | 3 |
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 |
| 1C7H | X-ray | 2.50 | A | 1-131 | [»] | |
| 1CQS | X-ray | 1.90 | A/B | 1-131 | [»] | |
| 1DMM | X-ray | 1.90 | A | 1-131 | [»] | |
| 1DMN | X-ray | 2.05 | A | 1-131 | [»] | |
| 1DMQ | X-ray | 2.15 | A | 1-131 | [»] | |
| 1E3R | X-ray | 2.50 | A/B | 1-131 | [»] | |
| 1E3V | X-ray | 2.00 | A/B | 1-131 | [»] | |
| 1E97 | X-ray | 2.00 | A | 1-131 | [»] | |
| 1EA2 | X-ray | 1.80 | A | 1-131 | [»] | |
| 1GS3 | X-ray | 2.10 | A | 1-131 | [»] | |
| 1K41 | X-ray | 2.20 | A/B | 1-131 | [»] | |
| 1OGX | X-ray | 2.00 | A/B | 1-131 | [»] | |
| 1OH0 | X-ray | 1.10 | A/B | 1-131 | [»] | |
| 1OHO | X-ray | 1.90 | A | 1-131 | [»] | |
| 1OPY | X-ray | 1.90 | A | 1-131 | [»] | |
| 1VZZ | X-ray | 2.30 | A/B | 1-131 | [»] | |
| 1W00 | X-ray | 2.20 | A/B | 1-131 | [»] | |
| 1W01 | X-ray | 2.20 | A/B | 1-131 | [»] | |
| 1W02 | X-ray | 2.30 | A | 1-131 | [»] | |
| 1W6Y | X-ray | 2.10 | A | 1-131 | [»] | |
| 2INX | X-ray | 1.50 | A | 1-131 | [»] | |
| 2PZV | X-ray | 1.25 | A/B/C/D | 1-131 | [»] | |
| 3CPO | X-ray | 1.24 | A | 1-131 | [»] | |
| 3FZW | X-ray | 1.32 | A/B | 1-131 | [»] | |
| 3IPT | X-ray | 1.63 | A/B/C/D | 1-131 | [»] | |
| 3OWS | X-ray | 1.71 | A/B/C/D | 1-131 | [»] | |
| 3OWU | X-ray | 1.70 | A/B/C/D | 1-131 | [»] | |
| 3OWY | X-ray | 2.30 | A/B/C/D/E/F/G/H | 1-131 | [»] | |
| 3OX9 | X-ray | 2.00 | A/B/C/D | 1-131 | [»] | |
| 3OXA | X-ray | 1.89 | A/B/C/D | 1-131 | [»] | |
| 3RGR | X-ray | 1.59 | A | 1-131 | [»] | |
| 3SED | X-ray | 1.30 | A | 3-127 | [»] | |
| 3T8N | X-ray | 1.47 | A/B/D/F | 1-131 | [»] | |
| 3VGN | X-ray | 1.30 | A/B | 1-131 | [»] | |
| 3VSY | X-ray | 1.50 | A/B | 3-131 | [»] | |
| 4CDL | X-ray | 2.50 | A | 1-131 | [»] | |
| 4K1U | X-ray | 2.00 | A/B | 1-131 | [»] | |
| 4K1V | X-ray | 1.80 | A | 1-131 | [»] | |
| 5AI1 | X-ray | 2.10 | A | 1-131 | [»] | |
| 5D81 | X-ray | 1.39 | A | 1-131 | [»] | |
| 5D82 | X-ray | 1.37 | A/B | 1-131 | [»] | |
| 5D83 | X-ray | 1.70 | A/B | 1-131 | [»] | |
| 5G2G | X-ray | 1.60 | A/B | 2-128 | [»] | |
| 5KP1 | X-ray | 1.22 | A/B/C/D | 1-131 | [»] | |
| 5KP3 | X-ray | 1.70 | A/B | 1-131 | [»] | |
| 5KP4 | X-ray | 1.71 | A/B | 1-131 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P07445 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P07445 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P07445 |
<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
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR032710 NTF2-like_dom_sf IPR037401 SnoaL-like |
Pfam protein domain database More...Pfami | View protein in Pfam PF12680 SnoaL_2, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54427 SSF54427, 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>.<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.
10 20 30 40 50
MNLPTAQEVQ GLMARYIELV DVGDIEAIVQ MYADDATVED PFGQPPIHGR
60 70 80 90 100
EQIAAFYRQG LGGGKVRACL TGPVRASHNG CGAMPFRVEM VWNGQPCALD
110 120 130
VIDVMRFDEH GRIQTMQAYW SEVNLSVREP Q
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 | L13127 Genomic DNA Translation: AAA64437.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A25216 SIPSDP |
<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 | |
|---|---|---|---|---|---|
| P07445 | UPI00084A2E7D | 135 | |||
| UPI000A1DFEC8 | 129 | ||||
| Steroid delta-isomerase | 127 | ||||
| UPI00083B5333 | 125 | ||||
| UPI000719A0C1 | 135 | ||||
| +27 | |||||
<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: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L13127 Genomic DNA Translation: AAA64437.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A25216 SIPSDP |
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 |
| 1C7H | X-ray | 2.50 | A | 1-131 | [»] | |
| 1CQS | X-ray | 1.90 | A/B | 1-131 | [»] | |
| 1DMM | X-ray | 1.90 | A | 1-131 | [»] | |
| 1DMN | X-ray | 2.05 | A | 1-131 | [»] | |
| 1DMQ | X-ray | 2.15 | A | 1-131 | [»] | |
| 1E3R | X-ray | 2.50 | A/B | 1-131 | [»] | |
| 1E3V | X-ray | 2.00 | A/B | 1-131 | [»] | |
| 1E97 | X-ray | 2.00 | A | 1-131 | [»] | |
| 1EA2 | X-ray | 1.80 | A | 1-131 | [»] | |
| 1GS3 | X-ray | 2.10 | A | 1-131 | [»] | |
| 1K41 | X-ray | 2.20 | A/B | 1-131 | [»] | |
| 1OGX | X-ray | 2.00 | A/B | 1-131 | [»] | |
| 1OH0 | X-ray | 1.10 | A/B | 1-131 | [»] | |
| 1OHO | X-ray | 1.90 | A | 1-131 | [»] | |
| 1OPY | X-ray | 1.90 | A | 1-131 | [»] | |
| 1VZZ | X-ray | 2.30 | A/B | 1-131 | [»] | |
| 1W00 | X-ray | 2.20 | A/B | 1-131 | [»] | |
| 1W01 | X-ray | 2.20 | A/B | 1-131 | [»] | |
| 1W02 | X-ray | 2.30 | A | 1-131 | [»] | |
| 1W6Y | X-ray | 2.10 | A | 1-131 | [»] | |
| 2INX | X-ray | 1.50 | A | 1-131 | [»] | |
| 2PZV | X-ray | 1.25 | A/B/C/D | 1-131 | [»] | |
| 3CPO | X-ray | 1.24 | A | 1-131 | [»] | |
| 3FZW | X-ray | 1.32 | A/B | 1-131 | [»] | |
| 3IPT | X-ray | 1.63 | A/B/C/D | 1-131 | [»] | |
| 3OWS | X-ray | 1.71 | A/B/C/D | 1-131 | [»] | |
| 3OWU | X-ray | 1.70 | A/B/C/D | 1-131 | [»] | |
| 3OWY | X-ray | 2.30 | A/B/C/D/E/F/G/H | 1-131 | [»] | |
| 3OX9 | X-ray | 2.00 | A/B/C/D | 1-131 | [»] | |
| 3OXA | X-ray | 1.89 | A/B/C/D | 1-131 | [»] | |
| 3RGR | X-ray | 1.59 | A | 1-131 | [»] | |
| 3SED | X-ray | 1.30 | A | 3-127 | [»] | |
| 3T8N | X-ray | 1.47 | A/B/D/F | 1-131 | [»] | |
| 3VGN | X-ray | 1.30 | A/B | 1-131 | [»] | |
| 3VSY | X-ray | 1.50 | A/B | 3-131 | [»] | |
| 4CDL | X-ray | 2.50 | A | 1-131 | [»] | |
| 4K1U | X-ray | 2.00 | A/B | 1-131 | [»] | |
| 4K1V | X-ray | 1.80 | A | 1-131 | [»] | |
| 5AI1 | X-ray | 2.10 | A | 1-131 | [»] | |
| 5D81 | X-ray | 1.39 | A | 1-131 | [»] | |
| 5D82 | X-ray | 1.37 | A/B | 1-131 | [»] | |
| 5D83 | X-ray | 1.70 | A/B | 1-131 | [»] | |
| 5G2G | X-ray | 1.60 | A/B | 2-128 | [»] | |
| 5KP1 | X-ray | 1.22 | A/B/C/D | 1-131 | [»] | |
| 5KP3 | X-ray | 1.70 | A/B | 1-131 | [»] | |
| 5KP4 | X-ray | 1.71 | A/B | 1-131 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P07445 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P07445 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P07445 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2321641 |
Drug and drug target database More...DrugBanki | DB03619 Deoxycholic Acid DB03515 Equilenin DB01708 Prasterone |
Proteomic databases
PRoteomics IDEntifications database More...PRIDEi | P07445 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 5.3.3.1 5092 |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P07445 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR032710 NTF2-like_dom_sf IPR037401 SnoaL-like |
Pfam protein domain database More...Pfami | View protein in Pfam PF12680 SnoaL_2, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54427 SSF54427, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | 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 | SDIS_PSEPU | |
| <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 | P07445Primary (citable) accession number: P07445 | |
| <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: | April 1, 1988 |
| Last sequence update: | April 1, 1988 | |
| Last modified: | May 23, 2018 | |
| This is version 103 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 | Prokaryotic 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
<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>Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references
