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Protein

Fumarate reductase 1

Gene

FRD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Irreversibly catalyzes the reduction of fumarate to succinate. Together with the second isozyme of soluble fumarate reductase (OSM1), essential for anaerobic growth. Involved in maintaining redox balance. Reduction of fumarate is the main source of succinate during fermentation, and under anaerobic conditions, the formation of succinate is strictly required for the reoxidation of FADH2.4 Publications

Catalytic activityi

Succinate + NAD+ = fumarate + NADH.1 Publication

Cofactori

FAD2 PublicationsNote: Binds 1 FAD per monomer.2 Publications

Kineticsi

  1. KM=0.2 mM for fumarate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei249 – 2491By similarity
    Active sitei272 – 2721By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi6 – 2015FADSequence analysisAdd
    BLAST

    GO - Molecular functioni

    • fumarate reductase (NADH) activity Source: SGD
    • succinate dehydrogenase activity Source: InterPro

    GO - Biological processi

    • cellular response to anoxia Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NAD

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30165-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate reductase 1 (EC:1.3.1.6)
    Short name:
    FRDS1
    Alternative name(s):
    FAD-dependent oxidoreductase
    NADH-dependent fumarate reductase
    Soluble fumarate reductase, cytoplasmic isozyme
    Gene namesi
    Name:FRD1
    Synonyms:FRDS, FRDS1
    Ordered Locus Names:YEL047C
    ORF Names:SYGP-ORF35
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome V

    Organism-specific databases

    EuPathDBiFungiDB:YEL047C.
    SGDiS000000773. FRD1.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 470470Fumarate reductase 1PRO_0000158669Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei66 – 661PhosphoserineCombined sources

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32614.

    PTM databases

    iPTMnetiP32614.

    Expressioni

    Inductioni

    During anaerobic growth.1 Publication

    Interactioni

    Protein-protein interaction databases

    BioGridi36683. 28 interactions.
    DIPiDIP-5287N.
    IntActiP32614. 4 interactions.
    MINTiMINT-534771.

    Structurei

    3D structure databases

    ProteinModelPortaliP32614.
    SMRiP32614. Positions 3-466.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00650000094148.
    HOGENOMiHOG000227327.
    InParanoidiP32614.
    KOiK18561.
    OMAiNTIMALP.
    OrthoDBiEOG7T1RMD.

    Family and domain databases

    Gene3Di3.50.50.60. 2 hits.
    3.90.700.10. 1 hit.
    InterProiIPR003953. FAD-binding_2.
    IPR023753. FAD/NAD-binding_dom.
    IPR010960. Flavocytochrome_c.
    IPR027477. Succ_DH/fumarate_Rdtase_cat.
    [Graphical view]
    PfamiPF00890. FAD_binding_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.
    SSF56425. SSF56425. 1 hit.
    TIGRFAMsiTIGR01813. flavo_cyto_c. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P32614-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSLSPVVVIG TGLAGLAAAN ELVNKYNIPV TILEKASSIG GNSIKASSGI
    60 70 80 90 100
    NGACTETQRH FHIEDSPRLF EDDTIKSAKG KGVQELMAKL ANDSPLAIEW
    110 120 130 140 150
    LKNEFDLKLD LLAQLGGHSV ARTHRSSGKL PPGFEIVSAL SNNLKKLAET
    160 170 180 190 200
    KPELVKINLD SKVVDIHEKD GSISAVVYED KNGEKHMVSA NDVVFCSGGF
    210 220 230 240 250
    GFSKEMLKEY APELVNLPTT NGQQTTGDGQ RLLQKLGADL IDMDQIQVHP
    260 270 280 290 300
    TGFIDPNDRS SSWKFLAAES LRGLGGILLN PITGRRFVNE LTTRDVVTAA
    310 320 330 340 350
    IQKVCPQEDN RALLVMGEKM YTDLKNNLDF YMFKKLVQKL TLSQVVSEYN
    360 370 380 390 400
    LPITVAQLCE ELQTYSSFTT KADPLGRTVI LNEFGSDVTP ETVVFIGEVT
    410 420 430 440 450
    PVVHFTMGGA RINVKAQVIG KNDERLLKGL YAAGEVSGGV HGANRLGGSS
    460 470
    LLECVVFGRT AAESIANDRK
    Length:470
    Mass (Da):50,844
    Last modified:October 1, 1993 - v1
    Checksum:i63C30B39252DC935
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti285 – 2851R → K AA sequence (PubMed:8946166).Curated
    Sequence conflicti440 – 4401V → L AA sequence (PubMed:8946166).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U18779 Genomic DNA. Translation: AAB64995.1.
    BK006939 Genomic DNA. Translation: DAA07607.1.
    PIRiS30830.
    RefSeqiNP_010867.3. NM_001178862.3.

    Genome annotation databases

    EnsemblFungiiYEL047C; YEL047C; YEL047C.
    GeneIDi856664.
    KEGGisce:YEL047C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U18779 Genomic DNA. Translation: AAB64995.1.
    BK006939 Genomic DNA. Translation: DAA07607.1.
    PIRiS30830.
    RefSeqiNP_010867.3. NM_001178862.3.

    3D structure databases

    ProteinModelPortaliP32614.
    SMRiP32614. Positions 3-466.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi36683. 28 interactions.
    DIPiDIP-5287N.
    IntActiP32614. 4 interactions.
    MINTiMINT-534771.

    PTM databases

    iPTMnetiP32614.

    Proteomic databases

    MaxQBiP32614.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYEL047C; YEL047C; YEL047C.
    GeneIDi856664.
    KEGGisce:YEL047C.

    Organism-specific databases

    EuPathDBiFungiDB:YEL047C.
    SGDiS000000773. FRD1.

    Phylogenomic databases

    GeneTreeiENSGT00650000094148.
    HOGENOMiHOG000227327.
    InParanoidiP32614.
    KOiK18561.
    OMAiNTIMALP.
    OrthoDBiEOG7T1RMD.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30165-MONOMER.

    Miscellaneous databases

    PROiP32614.

    Family and domain databases

    Gene3Di3.50.50.60. 2 hits.
    3.90.700.10. 1 hit.
    InterProiIPR003953. FAD-binding_2.
    IPR023753. FAD/NAD-binding_dom.
    IPR010960. Flavocytochrome_c.
    IPR027477. Succ_DH/fumarate_Rdtase_cat.
    [Graphical view]
    PfamiPF00890. FAD_binding_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.
    SSF56425. SSF56425. 1 hit.
    TIGRFAMsiTIGR01813. flavo_cyto_c. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and sequencing of the gene encoding the soluble fumarate reductase from Saccharomyces cerevisiae."
      Enomoto K., Ohki R., Muratsubaki H.
      DNA Res. 3:263-267(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 89-106; 245-253; 322-327 AND 409-423, COFACTOR, SUBCELLULAR LOCATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Purification and properties of fumarate reductase from baker's yeast."
      Muratsubaki H., Katsume T.
      Agric. Biol. Chem. 40:2902-2917(1982)
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    5. "One of the fumarate reductase isoenzymes from Saccharomyces cerevisiae is encoded by the OSM1 gene."
      Muratsubaki H., Enomoto K.
      Arch. Biochem. Biophys. 352:175-181(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    6. "Soluble fumarate reductase isoenzymes from Saccharomyces cerevisiae are required for anaerobic growth."
      Arikawa Y., Enomoto K., Muratsubaki H., Okazaki M.
      FEMS Microbiol. Lett. 165:111-116(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Investigation by 13C-NMR and tricarboxylic acid (TCA) deletion mutant analysis of pathways for succinate formation in Saccharomyces cerevisiae during anaerobic fermentation."
      Camarasa C., Grivet J.P., Dequin S.
      Microbiology 149:2669-2678(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    10. "Role in anaerobiosis of the isoenzymes for Saccharomyces cerevisiae fumarate reductase encoded by OSM1 and FRDS1."
      Camarasa C., Faucet V., Dequin S.
      Yeast 24:391-401(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.

    Entry informationi

    Entry nameiFRDS_YEAST
    AccessioniPrimary (citable) accession number: P32614
    Secondary accession number(s): D3DLK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: July 6, 2016
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 7620 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.