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Entry version 94 (11 Dec 2019)
Sequence version 2 (24 Jul 2013)
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Protein

(S)-mandelate dehydrogenase, mitochondrial

Gene
N/A
Organism
Rhodotorula graminis (Yeast)
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

Involved in the reduction of (S)-mandelate to benzoylformate and enables utilization of mandelate as substrate for growth.2 Publications

<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

  1. KM=0.47 mM for D,L-mandelate (with ferricyanide as electron acceptor)1 Publication
  2. KM=0.53 mM for 2-deuterated D,L-mandelate (with ferricyanide as electron acceptor)1 Publication
  3. KM=0.78 mM for D,L-mandelate (with cytochrome c as electron acceptor)1 Publication
  4. KM=1.33 mM for 2-deuterated D,L-mandelate (with cytochrome c as electron acceptor)1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: (R)-mandelate degradation

    This protein is involved in step 2 of the subpathway that synthesizes benzoate from (R)-mandelate.
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. (S)-mandelate dehydrogenase, mitochondrial
    3. no protein annotated in this organism
    4. no protein annotated in this organism
    This subpathway is part of the pathway (R)-mandelate degradation, which is itself part of Aromatic compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes benzoate from (R)-mandelate, the pathway (R)-mandelate degradation and in Aromatic compound metabolism.

    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 bindingi121Iron (heme axial ligand)PROSITE-ProRule annotation1
    Metal bindingi144Iron (heme axial ligand)PROSITE-ProRule annotation1
    <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 sitei215SubstratePROSITE-ProRule annotation1
    Binding sitei297FMNPROSITE-ProRule annotation1
    Binding sitei320FMNPROSITE-ProRule annotation1
    Binding sitei322SubstratePROSITE-ProRule annotation1
    Binding sitei348FMNPROSITE-ProRule annotation1
    Binding sitei357SubstratePROSITE-ProRule annotation1
    Binding sitei427FMNPROSITE-ProRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei451Proton acceptorPROSITE-ProRule annotation1
    Binding sitei454SubstratePROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi485 – 509FMNPROSITE-ProRule annotationAdd BLAST25

    <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

    GO - Biological processi

    <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
    Biological processAromatic hydrocarbons catabolism, Electron transport, Mandelate pathway, Respiratory chain, Transport
    LigandFlavoprotein, FMN, Heme, Iron, Metal-binding

    Enzyme and pathway databases

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00873;UER00853

    <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:
    (S)-mandelate dehydrogenase, mitochondrial (EC:1.1.99.31)
    Alternative name(s):
    Flavocytochrome b
    L(+)-mandelate dehydrogenase
    Short name:
    L-MDH
    <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>OrganismiRhodotorula graminis (Yeast)
    <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 identifieri29898 [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 lineageiEukaryotaFungiDikaryaBasidiomycotaPucciniomycotinaMicrobotryomycetesSporidiobolalesSporidiobolaceaeRhodotorula

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Mitochondrion

    <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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 54MitochondrionSequence analysisAdd BLAST54
    <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_000020632855 – 565(S)-mandelate dehydrogenase, mitochondrialAdd BLAST511

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P32953

    <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

    Homotetramer.

    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
    P32953

    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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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>Domaini86 – 163Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST78
    Domaini189 – 559FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd BLAST371

    <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 FMN-dependent alpha-hydroxy acid dehydrogenase family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd02922, FCB2_FMN, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.10.120.10, 1 hit
    3.20.20.70, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR013785, Aldolase_TIM
    IPR001199, Cyt_B5-like_heme/steroid-bd
    IPR036400, Cyt_B5-like_heme/steroid_sf
    IPR018506, Cyt_B5_heme-BS
    IPR000262, FMN-dep_DH
    IPR037396, FMN_HAD
    IPR037458, L-MDH/L-LDH_FMN-bd

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00173, Cyt-b5, 1 hit
    PF01070, FMN_dh, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01117, Cyt-b5, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF55856, SSF55856, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00191, CYTOCHROME_B5_1, 1 hit
    PS50255, CYTOCHROME_B5_2, 1 hit
    PS51349, FMN_HYDROXY_ACID_DH_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.

    P32953-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSFARVRTAL RCQRAAASPA PPKVQARRFA NKAAPHASAS SAGSRAFHLG
    60 70 80 90 100
    LAAGAALAVG GAGLYLFSRS PVLLDAQLPV KQRGRARSIS AAEVAKHNSR
    110 120 130 140 150
    DSMWVCIDDE VWDITNFVEL HPGGAKVLEQ NAGKDVTKVF KSIHPPKTLE
    160 170 180 190 200
    KFLTDDNFVG RIDVDEVTKI GGGKNAEDLR IEQARKELRN VETVVCLDEF
    210 220 230 240 250
    EEISQKILSE MAMAYYGTGA ETEQTLRDER EAWQRVRFRP RVLRKMRHID
    260 270 280 290 300
    TNTTFLGIPT PLPIFVAPAG LARLGHPDGE QNIVRGVAKH DILQVVSSGA
    310 320 330 340 350
    SCSIDEIFEV KEPDQNLAWQ FYVHSDKKIA EEKLKRALAL GAKAIFVTVD
    360 370 380 390 400
    VPVLGKRERD LKLKARSQNY EHPIAAQWKA AGSKVEETIA KRGVSDIPDT
    410 420 430 440 450
    AHIDANLNWD DIAWIKERAP GVPIVIKGVG CVEDVELAKQ YGADGVVLST
    460 470 480 490 500
    HGARQLDGAR APLDVLIEVR RKNPALLKEI EVYVDGQARR GTDVLKALCL
    510 520 530 540 550
    GARGVGFGRG FLYAQSAYGA DGVDKAIRIL ENEIQNAMRL LGANTLADLK
    560
    PEMVECSFPE RWVPE
    Length:565
    Mass (Da):61,974
    Last modified:July 24, 2013 - 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:iA16F5BB4CFE418F1
    GO

    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
    AJ001430 Genomic DNA Translation: CAA04758.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S35053

    <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
    AJ001430 Genomic DNA Translation: CAA04758.1
    PIRiS35053

    3D structure databases

    SMRiP32953
    ModBaseiSearch...

    Proteomic databases

    PRIDEiP32953

    Enzyme and pathway databases

    UniPathwayiUPA00873;UER00853

    Family and domain databases

    CDDicd02922, FCB2_FMN, 1 hit
    Gene3Di3.10.120.10, 1 hit
    3.20.20.70, 1 hit
    InterProiView protein in InterPro
    IPR013785, Aldolase_TIM
    IPR001199, Cyt_B5-like_heme/steroid-bd
    IPR036400, Cyt_B5-like_heme/steroid_sf
    IPR018506, Cyt_B5_heme-BS
    IPR000262, FMN-dep_DH
    IPR037396, FMN_HAD
    IPR037458, L-MDH/L-LDH_FMN-bd
    PfamiView protein in Pfam
    PF00173, Cyt-b5, 1 hit
    PF01070, FMN_dh, 1 hit
    SMARTiView protein in SMART
    SM01117, Cyt-b5, 1 hit
    SUPFAMiSSF55856, SSF55856, 1 hit
    PROSITEiView protein in PROSITE
    PS00191, CYTOCHROME_B5_1, 1 hit
    PS50255, CYTOCHROME_B5_2, 1 hit
    PS51349, FMN_HYDROXY_ACID_DH_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 nameiCYBL_RHOGR
    <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: P32953
    Secondary accession number(s): O13510
    <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 1, 1993
    Last sequence update: July 24, 2013
    Last modified: December 11, 2019
    This is version 94 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 statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal 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

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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