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P55250

- FUMH_RHIOR

UniProt

P55250 - FUMH_RHIOR

Protein

Fumarate hydratase, mitochondrial

Gene

FUMR

Organism
Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate = fumarate + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei130 – 1301SubstrateBy similarity

    GO - Molecular functioni

    1. fumarate hydratase activity Source: UniProtKB-EC

    GO - Biological processi

    1. fumarate metabolic process Source: InterPro
    2. tricarboxylic acid cycle Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase, mitochondrial (EC:4.2.1.2)
    Short name:
    Fumarase
    Gene namesi
    Name:FUMR
    OrganismiRhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
    Taxonomic identifieri64495 [NCBI]
    Taxonomic lineageiEukaryotaFungiFungi incertae sedisEarly diverging fungal lineagesMucoromycotinaMucoralesMucorineaeRhizopodaceaeRhizopus

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. tricarboxylic acid cycle enzyme complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1515MitochondrionSequence AnalysisAdd
    BLAST
    Chaini16 – 494479Fumarate hydratase, mitochondrialPRO_0000010331Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP55250.
    SMRiP55250. Positions 33-493.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni159 – 1624B siteBy similarity
    Regioni169 – 1713Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    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.

    P55250-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRASATRFL SQAKNMNNSP RLFSSASAAL QKFRAERDTF GDLQVPADRY    50
    WGAQTQRSLQ NFDIGGPTER MPEPLIRAFG VLKKAAATVN MTYGLDPKVG 100
    EAIQKAADEV IDGSLIDHFP LVVWQTGSGT QTKMNVNEVI SNRAIELLGG 150
    ELGSKAPVHP NDHVNMSQSS NDTFPTAMHV AAVVEIHGRL IPALTTLRDA 200
    LQAKSAEFEH IIKIGRTHLQ DATPLTLGQE FSGYTQQLTY GIARVQGTLE 250
    RLYNLAQGGT AVGTGLNTRK GFDAKVAEAI ASITGLPFKT APNKFEALAA 300
    HDALVEAHGA LNTVACSLMK IANDIRYLGS GPRCGLGELS LPENEPGSSI 350
    MPGKVNPTQC EAMTMVCAQV MGNNTAISVA GSNGQFELNV FKPVMIKNLI 400
    QSIRLISDAS ISFTKNCVVG IEANEKKISS IMNESLMLVT ALNPHIGYDK 450
    AAKCAKKAHK EGTTLKEAAL SLGYLTSEEF DQWVRPEDMI SAKD 494
    Length:494
    Mass (Da):53,157
    Last modified:October 1, 1996 - v1
    Checksum:i8FDB9D323A9146EE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78576 Genomic DNA. Translation: CAA55314.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78576 Genomic DNA. Translation: CAA55314.1 .

    3D structure databases

    ProteinModelPortali P55250.
    SMRi P55250. Positions 33-493.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .

    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. "The fumR gene encoding fumarase in the filamentous fungus Rhizopus oryzae: cloning, structure and expression."
      Friedberg D., Peleg Y., Monsonego A., Maissi S., Battat E., Rokem J.S., Goldberg I.
      Gene 163:139-144(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 10260 / CBS 329.47 / DSM 905 / NRRL 1526.

    Entry informationi

    Entry nameiFUMH_RHIOR
    AccessioniPrimary (citable) accession number: P55250
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    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

    Documents

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

    External Data

    Dasty 3