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UniProtKB - P84469 (FERB_PARDE)
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>sp|P84469|FERB_PARDE Ferric reductase B (Fragment) OS=Paracoccus denitrificans OX=266 GN=ferB PE=1 SV=1 MVKTVAVMVGSLRKDSLAHKLMKVLQKCommunity curation ()Add a publicationFeedback
Protein
Ferric reductase B
Gene
ferB
Organism
Paracoccus denitrificans
Status
Reviewed-Annotation score:
Annotation score:3 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
Reductase activity that acts on Fe3+-chelates and uses both NADH and NADPH as electron donors. May play a role in iron uptake.
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"Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans."
Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.
Eur. J. Biochem. 271:553-562(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MASS SPECTROMETRY.
<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
- 2 a Fe(II)-siderophoreEC:1.16.1.7
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- Search chemical reactions in Rhea for this molecule.
- 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.
- 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.1"Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans."
Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.
Eur. J. Biochem. 271:553-562(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MASS SPECTROMETRY.
- 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 based on experiment ini
- Ref.1"Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans."
Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.
Eur. J. Biochem. 271:553-562(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MASS SPECTROMETRY.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
2a Fe(II)-siderophore- Search proteins in UniProtKB for this molecule.
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Fe2+zoom- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
+H+- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
+NAD+- Search proteins in UniProtKB for this molecule.
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=2a Fe(III)-siderophore- Search proteins in UniProtKB for this molecule.
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Fe3+zoom- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
+NADH- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
<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
FAD
- 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.1"Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans."
Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.
Eur. J. Biochem. 271:553-562(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MASS SPECTROMETRY.
Manual assertion based on experiment ini
- Ref.1"Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans."
Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.
Eur. J. Biochem. 271:553-562(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MASS SPECTROMETRY.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=0.4 mM for Fe3+EGTA and NADH1 Publication
Manual assertion based on experiment ini
- Ref.1"Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans."
Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.
Eur. J. Biochem. 271:553-562(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MASS SPECTROMETRY.
- KM=1.6 mM for Fe3+EDTA and NADH1 Publication
Manual assertion based on experiment ini
- Ref.1"Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans."
Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.
Eur. J. Biochem. 271:553-562(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MASS SPECTROMETRY.
- KM=0.4 mM for Fe3+citrate and NADH1 Publication
Manual assertion based on experiment ini
- Ref.1"Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans."
Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.
Eur. J. Biochem. 271:553-562(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MASS SPECTROMETRY.
- KM=0.4 mM for Fe3+chloride and NADH1 Publication
Manual assertion based on experiment ini
- Ref.1"Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans."
Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.
Eur. J. Biochem. 271:553-562(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MASS SPECTROMETRY.
<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
- ferric-chelate reductase (NADH) activity Source: UniProtKB-EC
<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 |
| Biological process | Electron transport, Transport |
| Ligand | FAD, Flavoprotein, NAD, NADP |
Enzyme and pathway databases
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P84469 |
<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: Ferric reductase B (EC:1.16.1.7
|
| <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:ferB |
| <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 | Paracoccus denitrificans |
| <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 | 266 [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 › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus |
<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000087228 | 1 – ›27 | Ferric reductase BAdd BLAST | ›27 |
<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
By Fe3+ ion deprivation.1 Publication
Manual assertion based on experiment ini
- Ref.1"Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans."
Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.
Eur. J. Biochem. 271:553-562(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MASS SPECTROMETRY.
<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
Homodimer.
1 PublicationManual assertion based on experiment ini
- Ref.1"Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans."
Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.
Eur. J. Biochem. 271:553-562(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MASS SPECTROMETRY.
<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
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P84469 |
Database of comparative protein structure models More...ModBasei | Search... |
<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: Fragment.
P84469-1 [UniParc]FASTAAdd to basketAdded to basket
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MVKTVAVMVG SLRKDSLAHK LMKVLQK
Length:27
Mass (Da):3,012
Last modified:March 29, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i10D878742BCD3F4B
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei | 27 | 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 |
<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi
Molecular mass is 20196 Da. Determined by MALDI. 1 Publication
Manual assertion based on experiment ini
- Ref.1"Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans."
Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.
Eur. J. Biochem. 271:553-562(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MASS SPECTROMETRY.
<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
3D structure databases
| SMRi | P84469 |
| ModBasei | Search... |
Enzyme and pathway databases
| SABIO-RKi | P84469 |
Family and domain databases
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 | FERB_PARDE | |
| <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 | P84469Primary (citable) accession number: P84469 | |
| <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: | March 29, 2005 |
| Last sequence update: | March 29, 2005 | |
| Last modified: | September 29, 2021 | |
| This is version 34 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 | |
