UniProtKB - P77444 (SUFS_ECOLI)
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- BLAST>sp|P77444|SUFS_ECOLI Cysteine desulfurase OS=Escherichia coli (strain K12) OX=83333 GN=sufS PE=1 SV=1 MIFSVDKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHT LSAQATEKMENVRKRASLFINARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISQ MEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTLFDEKTRLLAITHVSNVLGTE NPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE ALLQEMPPWEGGGSMIATVSLSEGTTWTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLN NIAEYEQNLMHYALSQLESVPDLTLYGPQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRT GHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVTGLQRIHRLLG
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Cysteine desulfurase
sufS
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>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.6"Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate."
Lacourciere G.M., Mihara H., Kurihara T., Esaki N., Stadtman T.C.
J. Biol. Chem. 275:23769-23773(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.8"A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids."
Takahashi Y., Tokumoto U.
J. Biol. Chem. 277:28380-28383(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN FE-S CLUSTER SYSTEM. - Ref.9"The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H."
Mihara H., Kato S., Lacourciere G.M., Stadtman T.C., Kennedy R.A.J.D., Kurihara T., Tokumoto U., Takahashi Y., Esaki N.
Proc. Natl. Acad. Sci. U.S.A. 99:6679-6683(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.10"Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase."
Loiseau L., Ollagnier-de-Choudens S., Nachin L., Fontecave M., Barras F.
J. Biol. Chem. 278:38352-38359(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH SUFE AND SUFBCD COMPLEX. - Ref.11"The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli."
Outten F.W., Wood M.J., Munoz F.M., Storz G.
J. Biol. Chem. 278:45713-45719(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH SUFE AND SUFBCD COMPLEX.
<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
<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
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<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.10"Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase."
Loiseau L., Ollagnier-de-Choudens S., Nachin L., Fontecave M., Barras F.
J. Biol. Chem. 278:38352-38359(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH SUFE AND SUFBCD COMPLEX. - Ref.11"The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli."
Outten F.W., Wood M.J., Munoz F.M., Storz G.
J. Biol. Chem. 278:45713-45719(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH SUFE AND SUFBCD COMPLEX. - Ref.12"Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for sulfur transfer from SufS to SufE."
Ollagnier-de-Choudens S., Lascoux D., Loiseau L., Barras F., Forest E., Fontecave M.
FEBS Lett. 555:263-267(2003) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION, INTERACTION WITH SUFE.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: iron-sulfur cluster biosynthesis
This protein is involved in the pathway iron-sulfur cluster biosynthesis, which is part of Cofactor biosynthesis.View all proteins of this organism that are known to be involved in the pathway iron-sulfur cluster biosynthesis and in Cofactor biosynthesis.
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 | 364 | Cysteine persulfide intermediate | 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
- cysteine desulfurase activity Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- pyridoxal phosphate binding Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- selenocysteine lyase activity Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<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
- cysteine metabolic process Source: InterPro
- iron-sulfur cluster assembly Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- selenium compound metabolic process Source: EcoCyc <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- sulfur compound metabolic process Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- sulfur incorporation into metallo-sulfur cluster Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<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 | Lyase, Transferase |
| Ligand | Pyridoxal phosphate |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:G6906-MONOMER MetaCyc:G6906-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.8.1.7 2026 4.4.1.16 2026 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00266 |
<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 | |
| <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:sufS Synonyms:csdB, ynhB Ordered Locus Names:b1680, JW1670 |
| <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 | Escherichia coli (strain K12) |
| <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 | 83333 [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 › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Escherichia coli strain K12 genome database More...EcoGenei | EG13962 sufS |
<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
- Cytoplasm By similarity
<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 - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
<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 - Cellular componenti
Cytoplasm<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 | 55 | H → A: No effect. 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 | 123 | H → A: Loss of function; possibly due to destabilization of PLP in the active site. 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 | 364 | C → A: Abolishes activity towards L-cysteine but not towards selenocysteine. 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 | 379 | R → A: Loss of function. 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
Drug and drug target database More...DrugBanki | DB04217 L-2-amino-3-butynoic acid DB02761 S-Mercaptocysteine DB03049 S-Selanyl Cysteine DB02345 Selenocysteine |
<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_0000150329 | 1 – 406 | Cysteine desulfuraseAdd BLAST | 406 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 226 | N6-(pyridoxal phosphate)lysine | 1 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P77444 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P77444 |
PRoteomics IDEntifications database More...PRIDEi | P77444 |
<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.10"Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase."
Loiseau L., Ollagnier-de-Choudens S., Nachin L., Fontecave M., Barras F.
J. Biol. Chem. 278:38352-38359(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH SUFE AND SUFBCD COMPLEX. - Ref.11"The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli."
Outten F.W., Wood M.J., Munoz F.M., Storz G.
J. Biol. Chem. 278:45713-45719(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH SUFE AND SUFBCD COMPLEX. - Ref.12"Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for sulfur transfer from SufS to SufE."
Ollagnier-de-Choudens S., Lascoux D., Loiseau L., Barras F., Forest E., Fontecave M.
FEBS Lett. 555:263-267(2003) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION, INTERACTION WITH SUFE. - Ref.15"Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formation."
Lima C.D.
J. Mol. Biol. 315:1199-1208(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH L-CYSTEINE AND L-SELENOCYSTEINE, PYRIDOXAL PHOSPHATE AT LYS-226.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| sufE | P76194 | 3 | EBI-1124981,EBI-1124973 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 4260281, 100 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-2124 SufS complex |
Database of interacting proteins More...DIPi | DIP-9324N |
Protein interaction database and analysis system More...IntActi | P77444, 14 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_1814 |
<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 | 5 – 10 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 13 – 16 | 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 | 4 | |
| <p>This subsection of the ‘Structure’ 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 | 29 – 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 | 3 | |
| <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 | 37 – 49 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 60 – 79 | 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 | 20 | |
| <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 | 85 – 87 | 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 | 88 – 93 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 94 – 109 | 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 | 16 | |
| <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 | 115 – 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 | 5 | |
| <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 | 124 – 126 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 128 – 137 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 140 – 144 | 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 | 5 | |
| <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 | 154 – 156 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 157 – 160 | 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 | 4 | |
| <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 | 165 – 173 | 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 | 9 | |
| <p>This subsection of the ‘Structure’ 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 | 175 – 177 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 183 – 192 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 196 – 200 | 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 | 5 | |
| <p>This subsection of the ‘Structure’ 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 | 202 – 207 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 212 – 215 | 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 | 4 | |
| <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 | 218 – 223 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 224 – 226 | 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 | 234 – 238 | 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 | 5 | |
| <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 | 240 – 243 | 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 | 4 | |
| <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 | 252 – 258 | 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 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 | 261 – 263 | 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 | 264 – 267 | 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 | 4 | |
| <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 | 272 – 274 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 281 – 297 | 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 | 299 – 317 | 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 | 19 | |
| <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 | 323 – 327 | 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 | 5 | |
| <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 | 333 – 339 | 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 | 344 – 353 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 359 – 361 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 366 – 371 | 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 | 377 – 381 | 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 | 5 | |
| <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 | 388 – 405 | 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 | 18 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P77444 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P77444 |
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 | P77444 |
<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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105C9B Bacteria COG0520 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000017511 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P77444 |
KEGG Orthology (KO) More...KOi | K11717 |
Identification of Orthologs from Complete Genome Data More...OMAi | SGHKMCA |
Database for complete collections of gene phylogenies More...PhylomeDBi | P77444 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 2 hits |
HAMAP database of protein families More...HAMAPi | MF_01831 SufS_aminotrans_5, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000192 Aminotrans_V_dom IPR020578 Aminotrans_V_PyrdxlP_BS IPR010970 Cys_dSase_SufS IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major |
Pfam protein domain database More...Pfami | View protein in Pfam PF00266 Aminotran_5, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53383 SSF53383, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01979 sufS, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00595 AA_TRANSFER_CLASS_5, 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
MIFSVDKVRA DFPVLSREVN GLPLAYLDSA ASAQKPSQVI DAEAEFYRHG
60 70 80 90 100
YAAVHRGIHT LSAQATEKME NVRKRASLFI NARSAEELVF VRGTTEGINL
110 120 130 140 150
VANSWGNSNV RAGDNIIISQ MEHHANIVPW QMLCARVGAE LRVIPLNPDG
160 170 180 190 200
TLQLETLPTL FDEKTRLLAI THVSNVLGTE NPLAEMITLA HQHGAKVLVD
210 220 230 240 250
GAQAVMHHPV DVQALDCDFY VFSGHKLYGP TGIGILYVKE ALLQEMPPWE
260 270 280 290 300
GGGSMIATVS LSEGTTWTKA PWRFEAGTPN TGGIIGLGAA LEYVSALGLN
310 320 330 340 350
NIAEYEQNLM HYALSQLESV PDLTLYGPQN RLGVIAFNLG KHHAYDVGSF
360 370 380 390 400
LDNYGIAVRT GHHCAMPLMA YYNVPAMCRA SLAMYNTHEE VDRLVTGLQR
IHRLLG
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 | AB055108 Genomic DNA Translation: BAB21542.1 U00096 Genomic DNA Translation: AAC74750.1 AP009048 Genomic DNA Translation: BAA15457.1 |
Protein sequence database of the Protein Information Resource More...PIRi | H64925 |
NCBI Reference Sequences More...RefSeqi | NP_416195.1, NC_000913.3 WP_000577988.1, NZ_LN832404.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC74750; AAC74750; b1680 BAA15457; BAA15457; BAA15457 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 946185 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW1670 eco:b1680 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.578 |
<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 | |
|---|---|---|---|---|---|
| P77444 | Cysteine desulfurase | 406 | |||
| Cysteine desulfurase | 406 | ||||
| Cysteine desulfurase | 406 | ||||
| Cysteine desulfurase | 406 | ||||
| Cysteine desulfurase | 406 | ||||
| +20 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P77444 | Cysteine desulfurase | 406 | |||
| Cysteine desulfurase | 406 | ||||
| Cysteine desulfurase | 406 | ||||
| Cysteine desulfurase | 406 | ||||
| Cysteine desulfurase | 275 | ||||
| +705 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P77444 | Cysteine desulfurase | 406 | |||
| Cysteine desulfurase | 406 | ||||
| Cysteine desulfurase | 406 | ||||
| Cysteine desulfurase | 406 | ||||
| Cysteine desulfurase | 275 | ||||
| +2248 | |||||
<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 | AB055108 Genomic DNA Translation: BAB21542.1 U00096 Genomic DNA Translation: AAC74750.1 AP009048 Genomic DNA Translation: BAA15457.1 |
Protein sequence database of the Protein Information Resource More...PIRi | H64925 |
NCBI Reference Sequences More...RefSeqi | NP_416195.1, NC_000913.3 WP_000577988.1, NZ_LN832404.1 |
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 |
| 1C0N | X-ray | 2.80 | A | 1-406 | [»] | |
| 1I29 | X-ray | 2.80 | A | 1-406 | [»] | |
| 1JF9 | X-ray | 2.00 | A | 1-406 | [»] | |
| 1KMJ | X-ray | 2.00 | A | 1-406 | [»] | |
| 1KMK | X-ray | 2.20 | A | 1-406 | [»] | |
| 5DB5 | X-ray | 2.75 | A/B | 1-406 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P77444 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P77444 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 4260281, 100 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-2124 SufS complex |
Database of interacting proteins More...DIPi | DIP-9324N |
Protein interaction database and analysis system More...IntActi | P77444, 14 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_1814 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB04217 L-2-amino-3-butynoic acid DB02761 S-Mercaptocysteine DB03049 S-Selanyl Cysteine DB02345 Selenocysteine |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P77444 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P77444 |
PRoteomics IDEntifications database More...PRIDEi | P77444 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC74750; AAC74750; b1680 BAA15457; BAA15457; BAA15457 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 946185 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW1670 eco:b1680 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.578 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB3720 |
Escherichia coli strain K12 genome database More...EcoGenei | EG13962 sufS |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105C9B Bacteria COG0520 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000017511 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P77444 |
KEGG Orthology (KO) More...KOi | K11717 |
Identification of Orthologs from Complete Genome Data More...OMAi | SGHKMCA |
Database for complete collections of gene phylogenies More...PhylomeDBi | P77444 |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00266 |
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:G6906-MONOMER MetaCyc:G6906-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.8.1.7 2026 4.4.1.16 2026 |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P77444 |
Protein Ontology More...PROi | PR:P77444 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 2 hits |
HAMAP database of protein families More...HAMAPi | MF_01831 SufS_aminotrans_5, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000192 Aminotrans_V_dom IPR020578 Aminotrans_V_PyrdxlP_BS IPR010970 Cys_dSase_SufS IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major |
Pfam protein domain database More...Pfami | View protein in Pfam PF00266 Aminotran_5, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53383 SSF53383, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01979 sufS, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00595 AA_TRANSFER_CLASS_5, 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 | SUFS_ECOLI | |
| <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 | P77444Primary (citable) accession number: P77444 | |
| <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 27, 2001 |
| Last sequence update: | February 1, 1997 | |
| Last modified: | June 20, 2018 | |
| This is version 158 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, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
