Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 24 (02 Dec 2020)
Sequence version 1 (24 Jun 2015)
Previous versions | rss
Add a publicationFeedback
Protein

2-oxoacid:ferredoxin oxidoreductase subunit beta

Gene

SSOP1_2914

Organism
Saccharolobus solfataricus (Sulfolobus solfataricus)
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>

<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 coenzyme A-dependent oxidative decarboxylation of different 2-oxoacids such as 2-oxoglutarate, pyruvate and 2-oxobutyrate to form their CoA derivatives.

1 Publication

<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

<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:

<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

Kcat is 452 min(-1) for 2-oxoglutarate as substrate. Kcat is 144 min(-1) for pyruvate as substrate. Kcat is 93 min(-1) for 2-oxobutyrate as substrate.
  1. KM=163 µM for 2-oxoglutarate1 Publication
  2. KM=275 µM for pyruvate1 Publication
  3. KM=516 µM for 2-oxobutyrate1 Publication

    pH dependencei

    Optimum pH is between 7-8.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bindingi12Iron-sulfur (4Fe-4S)By similarity1
    Metal bindingi15Iron-sulfur (4Fe-4S)By similarity1
    Metal bindingi46Iron-sulfur (4Fe-4S)By similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei65Thiamine pyrophosphateBy similarity1
    Metal bindingi90MagnesiumBy similarity1
    Metal bindingi118MagnesiumBy similarity1
    Metal bindingi120Magnesium; via carbonyl oxygenBy similarity1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei125Plays an important role in the binding of CoABy similarity1
    Metal bindingi197Iron-sulfur (4Fe-4S)By similarity1

    <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

    <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 functionOxidoreductase
    LigandIron, Iron-sulfur, Magnesium, Metal-binding, Thiamine pyrophosphate

    <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:
    2-oxoacid:ferredoxin oxidoreductase subunit beta1 Publication (EC:1.2.7.111 Publication)
    Short name:
    OFORCurated
    <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
    ORF Names:SSOP1_2914Imported, SULA_0624Imported, SULB_0626Imported, SULC_0624Imported
    <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>OrganismiSaccharolobus solfataricus (Sulfolobus solfataricus)
    <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 identifieri2287 [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 lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSaccharolobus
    <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
    • UP000033057 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000076770 Componenti: Chromosome i
    • UP000033085 Componenti: Chromosome
    • UP000033106 Componenti: Chromosome

    <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 keyPosition(s)DescriptionActionsGraphical viewLength
    <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_00004455281 – 3052-oxoacid:ferredoxin oxidoreductase subunit betaAdd BLAST305

    <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

    Heterodimer composed of an alpha and a beta subunit.

    1 Publication

    <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
    A0A0E3KBH3

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni44 – 47Thiamine pyrophosphate bindingBy similarity4
    Regioni91 – 92Thiamine pyrophosphate bindingBy similarity2
    Regioni122 – 123Thiamine pyrophosphate bindingBy similarity2

    Phylogenomic databases

    Database of Orthologous Groups

    More...
    OrthoDBi
    43666at2157

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR011896, OFOB
    IPR032686, PFO_beta_C
    IPR029061, THDP-binding
    IPR011766, TPP_enzyme-bd_C

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF12367, PFO_beta_C, 1 hit
    PF02775, TPP_enzyme_C, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52518, SSF52518, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR02177, PorB_KorB, 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.

    A0A0E3KBH3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAGLKVEWND WCPGCGNFGI LSAEQQAIQE LGLDPKKVVL VSGIGCSGKI
    60 70 80 90 100
    PHFIRLPASG VHTLHGRALT FAIGIKLANP SLEVIVNGGD GDQLGIGVGH
    110 120 130 140 150
    FVSAGRRNVD LTVIVHNNGV YGLTKGQASP TLKLGVKTKS LPKPNINSDI
    160 170 180 190 200
    NPIALAISSG YTFVARGYAY DVKHLKEIIK KAIKHKGLAM IDVLQPCPTY
    210 220 230 240 250
    NDIHTKEYYD KRVYKLDEDP SWDPIVKKPE EMDDKMSKAI LKSMEWGDRT
    260 270 280 290 300
    PIGIFYQNEL VSTYEQRIAE RSPSYLDNPP AHDVIEFEGK PTTDVEDILK

    ERRVT
    Length:305
    Mass (Da):33,616
    Last modified:June 24, 2015 - 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:i89FABF906E2611CA
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence SAI86468 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti250T → I in SAI86468 (Ref. 2) Curated1

    <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 33600 Da. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    CP011055 Genomic DNA Translation: AKA73018.1
    CP011056 Genomic DNA Translation: AKA75716.1
    CP011057 Genomic DNA Translation: AKA78408.1
    LT549890 Genomic DNA Translation: SAI86468.1 Different initiation.

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_048186280.1, NZ_CP033241.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AKA73018; AKA73018; SULB_0626
    AKA75716; AKA75716; SULC_0624
    AKA78408; AKA78408; SULA_0624

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    44128565

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ssoa:SULA_0624
    ssof:SULC_0624
    ssol:SULB_0626

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|2287.6.peg.650

    <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
    CP011055 Genomic DNA Translation: AKA73018.1
    CP011056 Genomic DNA Translation: AKA75716.1
    CP011057 Genomic DNA Translation: AKA78408.1
    LT549890 Genomic DNA Translation: SAI86468.1 Different initiation.
    RefSeqiWP_048186280.1, NZ_CP033241.1

    3D structure databases

    SMRiA0A0E3KBH3
    ModBaseiSearch...

    Genome annotation databases

    EnsemblBacteriaiAKA73018; AKA73018; SULB_0626
    AKA75716; AKA75716; SULC_0624
    AKA78408; AKA78408; SULA_0624
    GeneIDi44128565
    KEGGissoa:SULA_0624
    ssof:SULC_0624
    ssol:SULB_0626
    PATRICifig|2287.6.peg.650

    Phylogenomic databases

    OrthoDBi43666at2157

    Family and domain databases

    InterProiView protein in InterPro
    IPR011896, OFOB
    IPR032686, PFO_beta_C
    IPR029061, THDP-binding
    IPR011766, TPP_enzyme-bd_C
    PfamiView protein in Pfam
    PF12367, PFO_beta_C, 1 hit
    PF02775, TPP_enzyme_C, 1 hit
    SUPFAMiSSF52518, SSF52518, 1 hit
    TIGRFAMsiTIGR02177, PorB_KorB, 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 nameiOFOB_SACSO
    <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>AccessioniPrimary (citable) accession number: A0A0E3KBH3
    Secondary accession number(s): A0A157T6A7
    <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 historyiIntegrated into UniProtKB/Swiss-Prot: October 10, 2018
    Last sequence update: June 24, 2015
    Last modified: December 2, 2020
    This is version 24 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 statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again