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P08417

- FUMH_YEAST

UniProt

P08417 - FUMH_YEAST

Protein

Fumarate hydratase, mitochondrial

Gene

FUM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate = fumarate + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei126 – 1261SubstrateBy similarity

    GO - Molecular functioni

    1. fumarate hydratase activity Source: SGD

    GO - Biological processi

    1. fumarate metabolic process Source: SGD
    2. tricarboxylic acid cycle Source: SGD

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciYEAST:YPL262W-MONOMER.
    BRENDAi4.2.1.2. 984.
    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase, mitochondrial (EC:4.2.1.2)
    Short name:
    Fumarase
    Gene namesi
    Name:FUM1
    Ordered Locus Names:YPL262W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    CYGDiYPL262w.
    SGDiS000006183. FUM1.

    Subcellular locationi

    Mitochondrion matrix 1 Publication. Cytoplasm 1 Publication
    Note: Both fumarases are encoded by a single nuclear gene.

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. mitochondrial matrix Source: SGD
    3. mitochondrion Source: SGD
    4. tricarboxylic acid cycle enzyme complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 488Fumarate hydratase, mitochondrialPRO_0000010333
    Transit peptidei1 – ?Mitochondrion

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei428 – 4281Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP08417.
    PaxDbiP08417.
    PeptideAtlasiP08417.

    Expressioni

    Gene expression databases

    GenevestigatoriP08417.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi35951. 152 interactions.
    DIPiDIP-6451N.
    IntActiP08417. 3 interactions.
    MINTiMINT-606236.
    STRINGi4932.YPL262W.

    Structurei

    Secondary structure

    1
    488
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 314
    Beta strandi33 – 353
    Beta strandi38 – 436
    Helixi48 – 547
    Helixi61 – 644
    Helixi68 – 8720
    Helixi93 – 10715
    Helixi112 – 1143
    Beta strandi118 – 1214
    Helixi126 – 14217
    Helixi155 – 1595
    Turni160 – 1623
    Helixi165 – 18218
    Helixi185 – 20218
    Turni203 – 2053
    Beta strandi207 – 2126
    Beta strandi215 – 2217
    Helixi222 – 24726
    Turni255 – 2573
    Helixi267 – 27913
    Helixi289 – 2946
    Helixi297 – 32327
    Beta strandi327 – 3304
    Helixi353 – 37725
    Helixi387 – 41125
    Helixi413 – 4153
    Helixi420 – 42910
    Helixi432 – 4343
    Turni435 – 4373
    Helixi438 – 4403
    Helixi443 – 45614
    Helixi460 – 4667
    Helixi472 – 4787
    Helixi481 – 4833

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YFMX-ray2.60A1-488[»]
    ProteinModelPortaliP08417.
    SMRiP08417. Positions 27-485.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08417.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni164 – 1663Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0114.
    GeneTreeiENSGT00390000002779.
    HOGENOMiHOG000061736.
    KOiK01679.
    OMAiAITNCEL.
    OrthoDBiEOG73NGC9.

    Family and domain databases

    Gene3Di1.10.275.10. 1 hit.
    HAMAPiMF_00743. FumaraseC.
    InterProiIPR005677. Fum_hydII.
    IPR024083. Fumarase/histidase_N.
    IPR018951. Fumarase_C_C.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    [Graphical view]
    PANTHERiPTHR11444. PTHR11444. 1 hit.
    PfamiPF10415. FumaraseC_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view]
    PRINTSiPR00149. FUMRATELYASE.
    SUPFAMiSSF48557. SSF48557. 1 hit.
    TIGRFAMsiTIGR00979. fumC_II. 1 hit.
    PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08417-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRFTNCSCK TFVKSSYKLN IRRMNSSFRT ETDAFGEIHV PADKYWGAQT    50
    QRSFQNFKIG GARERMPLPL VHAFGVLKKS AAIVNESLGG LDPKISKAIQ 100
    QAADEVASGK LDDHFPLVVF QTGSGTQSNM NANEVISNRA IEILGGKIGS 150
    KQVHPNNHCN QSQSSNDTFP TVMHIAASLQ IQNELIPELT NLKNALEAKS 200
    KEFDHIVKIG RTHLQDATPL TLGQEFSGYV QQVENGIQRV AHSLKTLSFL 250
    AQGGTAVGTG LNTKPGFDVK IAEQISKETG LKFQTAPNKF EALAAHDAIV 300
    ECSGALNTLA CSLFKIAQDI RYLGSGPRCG YHELMLPENE PGSSIMPGKV 350
    NPTQNEALTQ VCVQVMGNNA AITFAGSQGQ FELNVFKPVM IANLLNSIRL 400
    ITDAAYSFRV HCVEGIKANE PRIHELLTKS LMLVTALNPK IGYDAASKVA 450
    KNAHKKGITL KESALELGVL TEKEFDEWVV PEHMLGPK 488
    Length:488
    Mass (Da):53,152
    Last modified:November 1, 1997 - v2
    Checksum:iC099A02409A210E6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti173 – 1731M → V in AAA66909. (PubMed:3040736)Curated
    Sequence conflicti289 – 2891K → R in AAA66909. (PubMed:3040736)Curated
    Sequence conflicti392 – 3921A → V in AAA66909. (PubMed:3040736)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02802 Genomic DNA. Translation: AAA66909.1.
    Z73618 Genomic DNA. Translation: CAA97997.1.
    BK006949 Genomic DNA. Translation: DAA11174.1.
    PIRiS65295. UFBYM.
    RefSeqiNP_015061.1. NM_001184076.1.

    Genome annotation databases

    EnsemblFungiiYPL262W; YPL262W; YPL262W.
    GeneIDi855866.
    KEGGisce:YPL262W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02802 Genomic DNA. Translation: AAA66909.1 .
    Z73618 Genomic DNA. Translation: CAA97997.1 .
    BK006949 Genomic DNA. Translation: DAA11174.1 .
    PIRi S65295. UFBYM.
    RefSeqi NP_015061.1. NM_001184076.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YFM X-ray 2.60 A 1-488 [» ]
    ProteinModelPortali P08417.
    SMRi P08417. Positions 27-485.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35951. 152 interactions.
    DIPi DIP-6451N.
    IntActi P08417. 3 interactions.
    MINTi MINT-606236.
    STRINGi 4932.YPL262W.

    Proteomic databases

    MaxQBi P08417.
    PaxDbi P08417.
    PeptideAtlasi P08417.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPL262W ; YPL262W ; YPL262W .
    GeneIDi 855866.
    KEGGi sce:YPL262W.

    Organism-specific databases

    CYGDi YPL262w.
    SGDi S000006183. FUM1.

    Phylogenomic databases

    eggNOGi COG0114.
    GeneTreei ENSGT00390000002779.
    HOGENOMi HOG000061736.
    KOi K01679.
    OMAi AITNCEL.
    OrthoDBi EOG73NGC9.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci YEAST:YPL262W-MONOMER.
    BRENDAi 4.2.1.2. 984.

    Miscellaneous databases

    EvolutionaryTracei P08417.
    NextBioi 980493.
    PROi P08417.

    Gene expression databases

    Genevestigatori P08417.

    Family and domain databases

    Gene3Di 1.10.275.10. 1 hit.
    HAMAPi MF_00743. FumaraseC.
    InterProi IPR005677. Fum_hydII.
    IPR024083. Fumarase/histidase_N.
    IPR018951. Fumarase_C_C.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    [Graphical view ]
    PANTHERi PTHR11444. PTHR11444. 1 hit.
    Pfami PF10415. FumaraseC_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00149. FUMRATELYASE.
    SUPFAMi SSF48557. SSF48557. 1 hit.
    TIGRFAMsi TIGR00979. fumC_II. 1 hit.
    PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mitochondrial and cytoplasmic fumarases in Saccharomyces cerevisiae are encoded by a single nuclear gene FUM1."
      Wu M., Tzagoloff A.
      J. Biol. Chem. 262:12275-12282(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
      , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
      Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
      Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
      Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 44-52, SUBCELLULAR LOCATION.
      Strain: ATCC 201238 / W303-1B.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
      Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
      Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    7. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiFUMH_YEAST
    AccessioniPrimary (citable) accession number: P08417
    Secondary accession number(s): D6W3A8, Q08978
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 151 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 6920 molecules/cell in log phase SD medium.1 Publication
    There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors By similarity.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    External Data

    Dasty 3