UniProtKB - Q59109 (DSRA_ARCFU)
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>sp|Q59109|DSRA_ARCFU Sulfite reductase, dissimilatory-type subunit alpha OS=Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) OX=224325 GN=dsrA PE=1 SV=2 MSETPLLDELEKGPWPSFVKEIKKTAELMEKAAAEGKDVKMPKGARGLLKQLEISYKDKK THWKHGGIVSVVGYGGGVIGRYSDLGEQIPEVEHFHTMRINQPSGWFYSTKALRGLCDVW EKWGSGLTNFHGSTGDIIFLGTRSEYLQPCFEDLGNLEIPFDIGGSGSDLRTPSACMGPA LCEFACYDTLELCYDLTMTYQDELHRPMWPYKFKIKCAGCPNDCVASKARSDFAIIGTWK DDIKVDQEAVKEYASWMDIENEVVKLCPTGAIKWDGKELTIDNRECVRCMHCINKMPKAL KPGDERGATILIGGKAPFVEGAVIGWVAVPFVEVEKPYDEIKEILEAIWDWWDEEGKFRE RIGELIWRKGMREFLKVIGREADVRMVKAPRNNPFMFFEKDELKPSAYTEELKKRGMWCommunity curation ()Add a publicationFeedback
Protein
Sulfite reductase, dissimilatory-type subunit alpha
Gene
dsrA
Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
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 sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration.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
- Ref.1"Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes."
Dahl C., Kredich N.M., Deutzmann R., Trueper H.G.
J. Gen. Microbiol. 139:1817-1828(1993) [PubMed] [Europe PMC] [Abstract]
<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
- [DsrC protein]-disulfideEC:1.8.99.5
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Manual assertion based on experiment ini
- Ref.1"Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes."
Dahl C., Kredich N.M., Deutzmann R., Trueper H.G.
J. Gen. Microbiol. 139:1817-1828(1993) [PubMed] [Europe PMC] [Abstract] - Ref.4"Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus."
Parey K., Warkentin E., Kroneck P.M., Ermler U.
Biochemistry 49:8912-8921(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S); SIROHEME AND HYDROGENSULFITE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, REACTION MECHANISM.
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Manual assertion based on experiment ini
- Ref.1"Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes."
Dahl C., Kredich N.M., Deutzmann R., Trueper H.G.
J. Gen. Microbiol. 139:1817-1828(1993) [PubMed] [Europe PMC] [Abstract] - Ref.4"Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus."
Parey K., Warkentin E., Kroneck P.M., Ermler U.
Biochemistry 49:8912-8921(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S); SIROHEME AND HYDROGENSULFITE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, REACTION MECHANISM.
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[DsrC protein]-disulfide- Search proteins in UniProtKB for this molecule.
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=[DsrC protein]-dithiol- Search proteins in UniProtKB for this molecule.
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- [DsrC protein]-S-sulfanyl-L-cysteine/L-cysteineEC:1.8.99.5
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Manual assertion based on experiment ini
- Ref.1"Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes."
Dahl C., Kredich N.M., Deutzmann R., Trueper H.G.
J. Gen. Microbiol. 139:1817-1828(1993) [PubMed] [Europe PMC] [Abstract] - Ref.4"Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus."
Parey K., Warkentin E., Kroneck P.M., Ermler U.
Biochemistry 49:8912-8921(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S); SIROHEME AND HYDROGENSULFITE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, REACTION MECHANISM.
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Manual assertion based on experiment ini
- Ref.1"Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes."
Dahl C., Kredich N.M., Deutzmann R., Trueper H.G.
J. Gen. Microbiol. 139:1817-1828(1993) [PubMed] [Europe PMC] [Abstract] - Ref.4"Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus."
Parey K., Warkentin E., Kroneck P.M., Ermler U.
Biochemistry 49:8912-8921(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S); SIROHEME AND HYDROGENSULFITE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, REACTION MECHANISM.
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=[DsrC protein]-disulfide- Search proteins in UniProtKB for this molecule.
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L-cystine residuezoom- Search proteins in UniProtKB for this molecule.
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<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
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Manual assertion based on experiment ini
- Ref.3"Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus."
Schiffer A., Parey K., Warkentin E., Diederichs K., Huber H., Stetter K.O., Kroneck P.M.H., Ermler U.
J. Mol. Biol. 379:1063-1074(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S) AND SIROHEME, COFACTOR, SUBUNIT, REACTION MECHANISM. - Ref.4"Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus."
Parey K., Warkentin E., Kroneck P.M., Ermler U.
Biochemistry 49:8912-8921(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S); SIROHEME AND HYDROGENSULFITE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, REACTION MECHANISM.
Manual assertion based on experiment ini
- Ref.3"Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus."
Schiffer A., Parey K., Warkentin E., Diederichs K., Huber H., Stetter K.O., Kroneck P.M.H., Ermler U.
J. Mol. Biol. 379:1063-1074(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S) AND SIROHEME, COFACTOR, SUBUNIT, REACTION MECHANISM. - Ref.4"Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus."
Parey K., Warkentin E., Kroneck P.M., Ermler U.
Biochemistry 49:8912-8921(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S); SIROHEME AND HYDROGENSULFITE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, REACTION MECHANISM.
- siroheme
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Manual assertion based on experiment ini
- Ref.3"Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus."
Schiffer A., Parey K., Warkentin E., Diederichs K., Huber H., Stetter K.O., Kroneck P.M.H., Ermler U.
J. Mol. Biol. 379:1063-1074(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S) AND SIROHEME, COFACTOR, SUBUNIT, REACTION MECHANISM. - Ref.4"Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus."
Parey K., Warkentin E., Kroneck P.M., Ermler U.
Biochemistry 49:8912-8921(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S); SIROHEME AND HYDROGENSULFITE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, REACTION MECHANISM.
Manual assertion based on experiment ini
- Ref.3"Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus."
Schiffer A., Parey K., Warkentin E., Diederichs K., Huber H., Stetter K.O., Kroneck P.M.H., Ermler U.
J. Mol. Biol. 379:1063-1074(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S) AND SIROHEME, COFACTOR, SUBUNIT, REACTION MECHANISM. - Ref.4"Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus."
Parey K., Warkentin E., Kroneck P.M., Ermler U.
Biochemistry 49:8912-8921(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S); SIROHEME AND HYDROGENSULFITE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, REACTION MECHANISM.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Temperature dependencei
Highly thermostable. Inactive towards methylviologen below 55 degrees Celsius.
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 | 176 | Iron-sulfur 1 (4Fe-4S)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 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 182 | Iron-sulfur 1 (4Fe-4S)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 220 | Iron-sulfur 1 (4Fe-4S)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 224 | Iron (siroheme axial ligand)2 Publications <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
| 1 | |
| Metal bindingi | 224 | Iron-sulfur 1 (4Fe-4S)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 267 | Iron-sulfur 2 (4Fe-4S)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 286 | Iron-sulfur 2 (4Fe-4S)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 289 | Iron-sulfur 2 (4Fe-4S)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 292 | Iron-sulfur 2 (4Fe-4S)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual 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
- heme binding Source: InterPro
- hydrogensulfite reductase activity Source: InterPro
- 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, Heme, Iron, Iron-sulfur, Metal-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:MONOMER-12500 |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.8.99.1, 414 1.8.99.3, 414 |
<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: Sulfite reductase, dissimilatory-type subunit alpha (EC:1.8.99.5
Manual assertion based on experiment ini
Alternative name(s): Dissimilatory sulfite reductase subunit alpha Hydrogensulfite reductase subunit alpha |
| <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:dsrA Ordered Locus Names:AF_0423 |
| <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 | Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) |
| <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 | 224325 [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 › Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus › Archaeoglobus fulgidus |
| <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 |
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<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
- Membrane Note: Although the protein complex is found in the soluble fraction it may be membrane-associated in vivo.
GO - Cellular componenti
- membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Membrane<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_0000080025 | 2 – 418 | Sulfite reductase, dissimilatory-type subunit alphaAdd BLAST | 417 |
<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
Heterotetramer of two alpha and two beta subunits.
2 PublicationsManual assertion based on experiment ini
- Ref.3"Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus."
Schiffer A., Parey K., Warkentin E., Diederichs K., Huber H., Stetter K.O., Kroneck P.M.H., Ermler U.
J. Mol. Biol. 379:1063-1074(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S) AND SIROHEME, COFACTOR, SUBUNIT, REACTION MECHANISM. - Ref.4"Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus."
Parey K., Warkentin E., Kroneck P.M., Ermler U.
Biochemistry 49:8912-8921(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S); SIROHEME AND HYDROGENSULFITE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, REACTION MECHANISM.
Protein-protein interaction databases
STRING: functional protein association networks More...STRINGi | 224325.AF_0423 |
<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 | 5 – 8 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 9 – 11 | Combined sources Manual 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 | 12 – 15 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 18 – 34 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| Helixi | 44 – 58 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| Beta strandi | 75 – 79 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <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 | 84 – 88 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 90 – 92 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 96 – 100 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 104 – 106 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 107 – 109 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 110 – 123 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| Beta strandi | 126 – 130 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 133 – 135 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 137 – 142 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 144 – 146 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 147 – 156 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 157 – 159 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 167 – 170 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 178 – 180 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 189 – 199 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 201 – 205 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 209 – 211 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 215 – 220 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 227 – 230 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 232 – 241 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 247 – 254 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 259 – 262 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 264 – 266 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 272 – 274 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 279 – 281 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 283 – 285 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 291 – 295 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 297 – 299 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 304 – 312 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Turni | 318 – 320 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 326 – 332 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 339 – 355 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| Helixi | 362 – 369 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 371 – 377 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 384 – 386 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 387 – 389 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 400 – 402 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 407 – 415 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q59109 |
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 | Q59109 |
<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
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 277 – 305 | 4Fe-4S ferredoxin-typePROSITE-ProRule 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 Add BLAST | 29 |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | arCOG02057, Archaea |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_660112_0_0_2 |
Identification of Orthologs from Complete Genome Data More...OMAi | MHCINVM |
Database of Orthologous Groups More...OrthoDBi | 58856at2157 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR017896, 4Fe4S_Fe-S-bd IPR011806, DsrA IPR005117, NiRdtase/SiRdtase_haem-b_fer IPR036136, Nit/Sulf_reduc_fer-like_dom_sf IPR006067, NO2/SO3_Rdtase_4Fe4S_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF01077, NIR_SIR, 1 hit PF03460, NIR_SIR_ferr, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF55124, SSF55124, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR02064, dsrA, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51379, 4FE4S_FER_2, 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.
Q59109-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MSETPLLDEL EKGPWPSFVK EIKKTAELME KAAAEGKDVK MPKGARGLLK
60 70 80 90 100
QLEISYKDKK THWKHGGIVS VVGYGGGVIG RYSDLGEQIP EVEHFHTMRI
110 120 130 140 150
NQPSGWFYST KALRGLCDVW EKWGSGLTNF HGSTGDIIFL GTRSEYLQPC
160 170 180 190 200
FEDLGNLEIP FDIGGSGSDL RTPSACMGPA LCEFACYDTL ELCYDLTMTY
210 220 230 240 250
QDELHRPMWP YKFKIKCAGC PNDCVASKAR SDFAIIGTWK DDIKVDQEAV
260 270 280 290 300
KEYASWMDIE NEVVKLCPTG AIKWDGKELT IDNRECVRCM HCINKMPKAL
310 320 330 340 350
KPGDERGATI LIGGKAPFVE GAVIGWVAVP FVEVEKPYDE IKEILEAIWD
360 370 380 390 400
WWDEEGKFRE RIGELIWRKG MREFLKVIGR EADVRMVKAP RNNPFMFFEK
410
DELKPSAYTE ELKKRGMW
Length:418
Mass (Da):47,525
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:iAC12A7BFDF27EEEF
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 | M95624 Genomic DNA Translation: AAB17213.1 AE000782 Genomic DNA Translation: AAB90812.1 |
Protein sequence database of the Protein Information Resource More...PIRi | G69302 |
NCBI Reference Sequences More...RefSeqi | WP_010877930.1, NC_000917.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAB90812; AAB90812; AF_0423 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 24793961 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | afu:AF_0423 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M95624 Genomic DNA Translation: AAB17213.1 AE000782 Genomic DNA Translation: AAB90812.1 |
| PIRi | G69302 |
| RefSeqi | WP_010877930.1, NC_000917.1 |
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 |
| 3MM5 | X-ray | 1.80 | A/D | 1-418 | [»] | |
| 3MM6 | X-ray | 1.90 | A/D | 1-418 | [»] | |
| 3MM7 | X-ray | 1.90 | A/D | 1-418 | [»] | |
| 3MM8 | X-ray | 2.28 | A/D | 1-418 | [»] | |
| 3MM9 | X-ray | 2.10 | A/D | 1-418 | [»] | |
| 3MMA | X-ray | 2.30 | A/D | 1-418 | [»] | |
| 3MMB | X-ray | 2.30 | A/D | 1-418 | [»] | |
| 3MMC | X-ray | 2.04 | A/D | 1-418 | [»] | |
| SMRi | Q59109 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| STRINGi | 224325.AF_0423 |
Genome annotation databases
| EnsemblBacteriai | AAB90812; AAB90812; AF_0423 |
| GeneIDi | 24793961 |
| KEGGi | afu:AF_0423 |
Phylogenomic databases
| eggNOGi | arCOG02057, Archaea |
| HOGENOMi | CLU_660112_0_0_2 |
| OMAi | MHCINVM |
| OrthoDBi | 58856at2157 |
Enzyme and pathway databases
| BioCyci | MetaCyc:MONOMER-12500 |
| BRENDAi | 1.8.99.1, 414 1.8.99.3, 414 |
Miscellaneous databases
| EvolutionaryTracei | Q59109 |
Family and domain databases
| InterProi | View protein in InterPro IPR017896, 4Fe4S_Fe-S-bd IPR011806, DsrA IPR005117, NiRdtase/SiRdtase_haem-b_fer IPR036136, Nit/Sulf_reduc_fer-like_dom_sf IPR006067, NO2/SO3_Rdtase_4Fe4S_dom |
| Pfami | View protein in Pfam PF01077, NIR_SIR, 1 hit PF03460, NIR_SIR_ferr, 1 hit |
| SUPFAMi | SSF55124, SSF55124, 1 hit |
| TIGRFAMsi | TIGR02064, dsrA, 1 hit |
| PROSITEi | View protein in PROSITE PS51379, 4FE4S_FER_2, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | DSRA_ARCFU | |
| <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 | Q59109Primary (citable) accession number: Q59109 | |
| <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 15, 1998 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | December 2, 2020 | |
| This is version 122 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
