We will be switching to the new UniProt website soon. Please explore and share your feedback.
Take me to the new website.
UniProtKB - Q01770 (HCP_DESDA)
(max 400 entries)
Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
>sp|Q01770|HCP_DESDA Hydroxylamine reductase OS=Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB) OX=525146 GN=hcp PE=1 SV=2 MSNAMFCYQCQETVGNKGCTQVGVCGKKPETAALQDALIYVTKGLGQIATRLRAEGKAVD HRIDRLVTGNLFATITNANFDDDILAERVRMTCAAKKELAASLTDKSGLSDAALWEASEK SAMLAKAGTVGVMATTDDDVRSLRWLITFGLKGMAAYAKHADVLGKHENSLDAFMQEALA KTLDDSLSVADLVALTLETGKFGVSAMALLDAANTGTYGHPEITKVNIGVGSNPGILISG HDLRDLEMLLKQTEGTGVDVYTHSEMLPAHYYPAFKKYAHFKGNYGNAWWKQKEEFESFN GPVLLTTNCLVPPKDSYKDRVYTTGIVGFTGCKHIPGEIGEHKDFSAIIAHAKTCPAPTE IESGEIIGGFAHNQVLALADKVIDAVKSGAIKKFVVMAGCDGRAKSRSYYTDFAEGLPKD TVILTAGCAKYRYNKLNLGDIGGIPRVLDAGQCNDSYSLAVIALKLKEVFGLEDVNDLPI VYNIAWYEQKAVIVLLALLSLGVKNIHLGPTLPAFLSPNVAKVLVEQFNIGGITSPQDDL KAFFGCommunity curation ()Add a publicationFeedback
Protein
Hydroxylamine reductase
Gene
hcp
Organism
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB)
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
Catalyzes the reduction of hydroxylamine to form NH3 and H2O.
UniRule annotation<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
Caution
Was originally thought to contain a 6Fe-6S cluster as indicated.1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.3"Direct spectroscopic evidence for the presence of a 6Fe cluster in an iron-sulfur protein isolated from Desulfovibrio desulfuricans (ATCC 27774)."
Moura I., Tavares P., Moura J.J.G., Ravi N., Huynh B.H., Liu M.Y., le Gall J.
J. Biol. Chem. 267:4489-4496(1992) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-37, COFACTOR, SUBUNIT.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- AEC:1.7.99.1
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion according to rulesi
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
Manual assertion according to rulesi
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
A- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
+H2O- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
+NH4+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
=AH2- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
+H+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
+hydroxylamine- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
<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
Protein has several cofactor binding sites:- [4Fe-4S] cluster
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
<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"Direct spectroscopic evidence for the presence of a 6Fe cluster in an iron-sulfur protein isolated from Desulfovibrio desulfuricans (ATCC 27774)."
Moura I., Tavares P., Moura J.J.G., Ravi N., Huynh B.H., Liu M.Y., le Gall J.
J. Biol. Chem. 267:4489-4496(1992) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-37, COFACTOR, SUBUNIT. - Ref.4"Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A resolution using synchrotron radiation."
Macedo S., Mitchell E.P., Romao C.V., Cooper S.J., Coelho R., Liu M.Y., Xavier A.V., LeGall J., Bailey S., Garner C.D., Hagen W.R., Teixeira M., Carrondo M.A., Lindley P.
J. Biol. Inorg. Chem. 7:514-525(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SULFHYDRATION AT CYS-400, SUBUNIT. - Ref.5"Structure of the hybrid cluster protein (HCP) from Desulfovibrio desulfuricans ATCC 27774 containing molecules in the oxidized and reduced states."
Macedo S., Aragao D., Mitchell E.P., Lindley P.
Acta Crystallogr. D 59:2065-2071(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR. - Ref.6"Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at high resolution using synchrotron radiation."
Aragao D., Macedo S., Mitchell E.P., Romao C.V., Liu M.Y., Frazao C., Saraiva L.M., Xavier A.V., LeGall J., van Dongen W.M.A.M., Hagen W.R., Teixeira M., Carrondo M.A., Lindley P.
J. Biol. Inorg. Chem. 8:540-548(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SUBUNIT.
Manual assertion based on experiment ini
- Ref.3"Direct spectroscopic evidence for the presence of a 6Fe cluster in an iron-sulfur protein isolated from Desulfovibrio desulfuricans (ATCC 27774)."
Moura I., Tavares P., Moura J.J.G., Ravi N., Huynh B.H., Liu M.Y., le Gall J.
J. Biol. Chem. 267:4489-4496(1992) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-37, COFACTOR, SUBUNIT. - Ref.4"Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A resolution using synchrotron radiation."
Macedo S., Mitchell E.P., Romao C.V., Cooper S.J., Coelho R., Liu M.Y., Xavier A.V., LeGall J., Bailey S., Garner C.D., Hagen W.R., Teixeira M., Carrondo M.A., Lindley P.
J. Biol. Inorg. Chem. 7:514-525(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SULFHYDRATION AT CYS-400, SUBUNIT. - Ref.5"Structure of the hybrid cluster protein (HCP) from Desulfovibrio desulfuricans ATCC 27774 containing molecules in the oxidized and reduced states."
Macedo S., Aragao D., Mitchell E.P., Lindley P.
Acta Crystallogr. D 59:2065-2071(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR. - Ref.6"Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at high resolution using synchrotron radiation."
Aragao D., Macedo S., Mitchell E.P., Romao C.V., Liu M.Y., Frazao C., Saraiva L.M., Xavier A.V., LeGall J., van Dongen W.M.A.M., Hagen W.R., Teixeira M., Carrondo M.A., Lindley P.
J. Biol. Inorg. Chem. 8:540-548(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SUBUNIT.
- hybrid [4Fe-2O-2S] cluster
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.4"Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A resolution using synchrotron radiation."
Macedo S., Mitchell E.P., Romao C.V., Cooper S.J., Coelho R., Liu M.Y., Xavier A.V., LeGall J., Bailey S., Garner C.D., Hagen W.R., Teixeira M., Carrondo M.A., Lindley P.
J. Biol. Inorg. Chem. 7:514-525(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SULFHYDRATION AT CYS-400, SUBUNIT. - Ref.5"Structure of the hybrid cluster protein (HCP) from Desulfovibrio desulfuricans ATCC 27774 containing molecules in the oxidized and reduced states."
Macedo S., Aragao D., Mitchell E.P., Lindley P.
Acta Crystallogr. D 59:2065-2071(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR. - Ref.6"Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at high resolution using synchrotron radiation."
Aragao D., Macedo S., Mitchell E.P., Romao C.V., Liu M.Y., Frazao C., Saraiva L.M., Xavier A.V., LeGall J., van Dongen W.M.A.M., Hagen W.R., Teixeira M., Carrondo M.A., Lindley P.
J. Biol. Inorg. Chem. 8:540-548(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SUBUNIT.
Manual assertion based on experiment ini
- Ref.4"Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A resolution using synchrotron radiation."
Macedo S., Mitchell E.P., Romao C.V., Cooper S.J., Coelho R., Liu M.Y., Xavier A.V., LeGall J., Bailey S., Garner C.D., Hagen W.R., Teixeira M., Carrondo M.A., Lindley P.
J. Biol. Inorg. Chem. 7:514-525(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SULFHYDRATION AT CYS-400, SUBUNIT. - Ref.5"Structure of the hybrid cluster protein (HCP) from Desulfovibrio desulfuricans ATCC 27774 containing molecules in the oxidized and reduced states."
Macedo S., Aragao D., Mitchell E.P., Lindley P.
Acta Crystallogr. D 59:2065-2071(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR. - Ref.6"Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at high resolution using synchrotron radiation."
Aragao D., Macedo S., Mitchell E.P., Romao C.V., Liu M.Y., Frazao C., Saraiva L.M., Xavier A.V., LeGall J., van Dongen W.M.A.M., Hagen W.R., Teixeira M., Carrondo M.A., Lindley P.
J. Biol. Inorg. Chem. 8:540-548(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SUBUNIT.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 7 | Iron-sulfur (4Fe-4S)3 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 10 | Iron-sulfur (4Fe-4S)3 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 19 | Iron-sulfur (4Fe-4S)3 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 25 | Iron-sulfur (4Fe-4S)3 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 241 | Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen3 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 265 | Iron-oxo-sulfur (4Fe-2O-2S)3 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 309 | Iron-oxo-sulfur (4Fe-2O-2S)3 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 400 | Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group2 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 428 | Iron-oxo-sulfur (4Fe-2O-2S)3 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 453 | Iron-oxo-sulfur (4Fe-2O-2S)3 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 488 | Iron-oxo-sulfur (4Fe-2O-2S)2 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 490 | Iron-oxo-sulfur (4Fe-2O-2S)2 Publications 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
- 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
- hydroxylamine reductase activity Source: UniProtKB-UniRule
- metal ion 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 | 4Fe-4S, Iron, Iron-sulfur, Metal-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | DDES525146:G1GUN-1926-MONOMER |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Hydroxylamine reductaseUniRule annotationManual assertion according to rulesi (EC:1.7.99.1
Manual assertion according to rulesi )Alternative name(s): Hybrid-cluster proteinUniRule annotation Manual assertion according to rulesi Short name: HCPUniRule annotation Manual assertion according to rulesi Prismane proteinUniRule annotation Manual assertion according to rulesi |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:hcpUniRule annotation Manual assertion according to rulesi Ordered Locus Names:Ddes_1829 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 525146 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio › Desulfovibrio desulfuricans |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 |
|
<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 and Cytosol
- Cytoplasm UniRule annotation
Manual assertion according to rulesi
- Cytoplasm UniRule annotation
Other locations
- cytoplasm Source: UniProtKB-SubCell
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
Chemistry databases
Drug and drug target database More...DrugBanki | DB03814, 2-(N-morpholino)ethanesulfonic acid DB02761, S-Mercaptocysteine |
<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication Manual assertion based on experiment ini
| |||
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000151666 | 2 – 545 | Hydroxylamine reductaseAdd BLAST | 544 |
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 | 400 | Cysteine persulfide; in oxidized form1 Publication Manual assertion based on experiment ini
| 1 |
Proteomic databases
PRoteomics IDEntifications database More...PRIDEi | Q01770 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Monomer.
3 PublicationsManual assertion based on experiment ini
- Ref.3"Direct spectroscopic evidence for the presence of a 6Fe cluster in an iron-sulfur protein isolated from Desulfovibrio desulfuricans (ATCC 27774)."
Moura I., Tavares P., Moura J.J.G., Ravi N., Huynh B.H., Liu M.Y., le Gall J.
J. Biol. Chem. 267:4489-4496(1992) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-37, COFACTOR, SUBUNIT. - Ref.4"Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A resolution using synchrotron radiation."
Macedo S., Mitchell E.P., Romao C.V., Cooper S.J., Coelho R., Liu M.Y., Xavier A.V., LeGall J., Bailey S., Garner C.D., Hagen W.R., Teixeira M., Carrondo M.A., Lindley P.
J. Biol. Inorg. Chem. 7:514-525(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SULFHYDRATION AT CYS-400, SUBUNIT. - Ref.6"Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at high resolution using synchrotron radiation."
Aragao D., Macedo S., Mitchell E.P., Romao C.V., Liu M.Y., Frazao C., Saraiva L.M., Xavier A.V., LeGall J., van Dongen W.M.A.M., Hagen W.R., Teixeira M., Carrondo M.A., Lindley P.
J. Biol. Inorg. Chem. 8:540-548(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-545 IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SUBUNIT.
Protein-protein interaction databases
STRING: functional protein association networks More...STRINGi | 525146.Ddes_1829 |
<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%5Fsection">'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 | 14 – 16 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'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 | 19 – 22 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 29 – 54 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 26 | |
| Helixi | 61 – 73 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'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 | 76 – 78 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 82 – 100 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 19 | |
| Helixi | 111 – 114 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 120 – 127 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Turni | 128 – 130 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 132 – 134 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 138 – 163 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 26 | |
| Helixi | 169 – 181 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
| Helixi | 189 – 218 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 30 | |
| Beta strandi | 224 – 227 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 235 – 241 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 243 – 253 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Turni | 254 – 257 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 259 – 262 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 264 – 271 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 273 – 277 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 281 – 284 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 286 – 288 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 289 – 291 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 292 – 299 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 303 – 308 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 315 – 318 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 321 – 324 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 332 – 335 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 338 – 340 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 346 – 353 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 364 – 368 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 372 – 377 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 379 – 387 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 393 – 396 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 405 – 407 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 408 – 416 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 421 – 425 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 428 – 432 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 433 – 435 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 444 – 449 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 453 – 455 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 456 – 470 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 15 | |
| Helixi | 475 – 477 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 478 – 485 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 489 – 500 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
| Beta strandi | 507 – 511 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 518 – 528 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 536 – 542 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q01770 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q01770 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the HCP family.UniRule annotation
Manual assertion according to rulesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG1151, Bacteria |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_038344_2_0_7 |
Identification of Orthologs from Complete Genome Data More...OMAi | DINIYTH |
Database of Orthologous Groups More...OrthoDBi | 337713at2 |
Family and domain databases
Conserved Domains Database More...CDDi | cd01914, HCP, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.1270.20, 2 hits 3.40.50.2030, 2 hits |
HAMAP database of protein families More...HAMAPi | MF_00069, Hydroxylam_reduct, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR004137, HCP/CODH IPR010048, Hydroxylam_reduct IPR016099, Prismane-like_a/b-sand IPR011254, Prismane-like_sf IPR016100, Prismane_a-bundle |
The PANTHER Classification System More...PANTHERi | PTHR30109, PTHR30109, 1 hit PTHR30109:SF0, PTHR30109:SF0, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03063, Prismane, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000076, HCP, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF56821, SSF56821, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01703, hybrid_clust, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
Q01770-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MSNAMFCYQC QETVGNKGCT QVGVCGKKPE TAALQDALIY VTKGLGQIAT
60 70 80 90 100
RLRAEGKAVD HRIDRLVTGN LFATITNANF DDDILAERVR MTCAAKKELA
110 120 130 140 150
ASLTDKSGLS DAALWEASEK SAMLAKAGTV GVMATTDDDV RSLRWLITFG
160 170 180 190 200
LKGMAAYAKH ADVLGKHENS LDAFMQEALA KTLDDSLSVA DLVALTLETG
210 220 230 240 250
KFGVSAMALL DAANTGTYGH PEITKVNIGV GSNPGILISG HDLRDLEMLL
260 270 280 290 300
KQTEGTGVDV YTHSEMLPAH YYPAFKKYAH FKGNYGNAWW KQKEEFESFN
310 320 330 340 350
GPVLLTTNCL VPPKDSYKDR VYTTGIVGFT GCKHIPGEIG EHKDFSAIIA
360 370 380 390 400
HAKTCPAPTE IESGEIIGGF AHNQVLALAD KVIDAVKSGA IKKFVVMAGC
410 420 430 440 450
DGRAKSRSYY TDFAEGLPKD TVILTAGCAK YRYNKLNLGD IGGIPRVLDA
460 470 480 490 500
GQCNDSYSLA VIALKLKEVF GLEDVNDLPI VYNIAWYEQK AVIVLLALLS
510 520 530 540
LGVKNIHLGP TLPAFLSPNV AKVLVEQFNI GGITSPQDDL KAFFG
Length:545
Mass (Da):58,659
Last modified:January 23, 2007 - v2
<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:iFEFF010FF9FBE4AC
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 | Z11975 Genomic DNA Translation: CAA78029.1 CP001358 Genomic DNA Translation: ACL49726.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S24389 |
NCBI Reference Sequences More...RefSeqi | WP_012625450.1, NC_011883.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | ACL49726; ACL49726; Ddes_1829 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | dds:Ddes_1829 |
<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 | |
|---|---|---|---|---|---|---|
| Q01770 | Hydroxylamine reductase | 545 | UniRef100_Q01770 | |||
| +2 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q01770 | Hydroxylamine reductase | 545 | UniRef90_Q01770 | |||
| Hydroxylamine reductase | 545 | |||||
| Hydroxylamine reductase | 545 | |||||
| Hydroxylamine reductase | 545 | |||||
| Hydroxylamine reductase | 545 | |||||
| +4 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q01770 | Hydroxylamine reductase 2 | 567 | UniRef50_Q01770 | |||
| Hydroxylamine reductase | 552 | |||||
| Hydroxylamine reductase | 549 | |||||
| Hydroxylamine reductase | 549 | |||||
| Hydroxylamine reductase | 549 | |||||
| +2960 | ||||||
<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 | Z11975 Genomic DNA Translation: CAA78029.1 CP001358 Genomic DNA Translation: ACL49726.1 |
| PIRi | S24389 |
| RefSeqi | WP_012625450.1, NC_011883.1 |
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 |
| 1GN9 | X-ray | 2.60 | A/B | 2-545 | [»] | |
| 1GNL | X-ray | 1.25 | A/B | 2-545 | [»] | |
| 1OA0 | X-ray | 1.25 | A/B | 2-545 | [»] | |
| 1UPX | X-ray | 1.25 | A/B | 2-545 | [»] | |
| SMRi | Q01770 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| STRINGi | 525146.Ddes_1829 |
Chemistry databases
| DrugBanki | DB03814, 2-(N-morpholino)ethanesulfonic acid DB02761, S-Mercaptocysteine |
Proteomic databases
| PRIDEi | Q01770 |
Genome annotation databases
| EnsemblBacteriai | ACL49726; ACL49726; Ddes_1829 |
| KEGGi | dds:Ddes_1829 |
Phylogenomic databases
| eggNOGi | COG1151, Bacteria |
| HOGENOMi | CLU_038344_2_0_7 |
| OMAi | DINIYTH |
| OrthoDBi | 337713at2 |
Enzyme and pathway databases
| BioCyci | DDES525146:G1GUN-1926-MONOMER |
Miscellaneous databases
| EvolutionaryTracei | Q01770 |
Family and domain databases
| CDDi | cd01914, HCP, 1 hit |
| Gene3Di | 1.20.1270.20, 2 hits 3.40.50.2030, 2 hits |
| HAMAPi | MF_00069, Hydroxylam_reduct, 1 hit |
| InterProi | View protein in InterPro IPR004137, HCP/CODH IPR010048, Hydroxylam_reduct IPR016099, Prismane-like_a/b-sand IPR011254, Prismane-like_sf IPR016100, Prismane_a-bundle |
| PANTHERi | PTHR30109, PTHR30109, 1 hit PTHR30109:SF0, PTHR30109:SF0, 1 hit |
| Pfami | View protein in Pfam PF03063, Prismane, 1 hit |
| PIRSFi | PIRSF000076, HCP, 1 hit |
| SUPFAMi | SSF56821, SSF56821, 1 hit |
| TIGRFAMsi | TIGR01703, hybrid_clust, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | HCP_DESDA | |
| <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 | Q01770Primary (citable) accession number: Q01770 Secondary accession number(s): B8J267 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1993 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | February 23, 2022 | |
| This is version 142 of the entry and version 2 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
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
