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P93033

- FUM1_ARATH

UniProt

P93033 - FUM1_ARATH

Protein

Fumarate hydratase 1, mitochondrial

Gene

FUM1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (15 Dec 2003)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate = fumarate + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei129 – 1291SubstrateBy similarity

    GO - Molecular functioni

    1. fumarate hydratase activity Source: UniProtKB-EC
    2. protein binding Source: TAIR

    GO - Biological processi

    1. fumarate metabolic process Source: InterPro
    2. pollen tube development Source: TAIR
    3. response to oxidative stress Source: TAIR
    4. response to salt stress Source: TAIR
    5. tricarboxylic acid cycle Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciARA:GQT-1578-MONOMER.
    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase 1, mitochondrial (EC:4.2.1.2)
    Short name:
    Fumarase 1
    Gene namesi
    Name:FUM1
    Ordered Locus Names:At2g47510
    ORF Names:T30B22.19
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G47510.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: TAIR
    2. tricarboxylic acid cycle enzyme complex Source: InterPro

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2828MitochondrionSequence AnalysisAdd
    BLAST
    Chaini29 – 492464Fumarate hydratase 1, mitochondrialPRO_0000010329Add
    BLAST

    Proteomic databases

    PaxDbiP93033.
    PRIDEiP93033.

    Expressioni

    Gene expression databases

    GenevestigatoriP93033.

    Interactioni

    Protein-protein interaction databases

    BioGridi4699. 1 interaction.
    IntActiP93033. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP93033.
    SMRiP93033. Positions 31-490.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni157 – 1604B siteBy similarity
    Regioni167 – 1693Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    InParanoidiP93033.
    KOiK01679.
    OMAiNAHPEYH.
    PhylomeDBiP93033.

    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.

    P93033-1 [UniParc]FASTAAdd to Basket

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    MSIYVASRRL SGGTTVTALR YATSLRSYST SFREERDTFG PIQVPSDKLW    50
    GAQTQRSLQN FEIGGERERM PEPIVRAFGV LKKCAAKVNM EYGLDPTIGK 100
    AIMQAAQEVA EGKLNDHFPL VVWQTGSGTQ SNMNANEVIA NRAAEILGRK 150
    RGEKCVHPND HVNRSQSSND TFPTVMHIAA ATEINSRLIP SLKTLHSTLE 200
    SKSFEFKDIV KIGRTHTQDA TPLTLGQEFG GYATQVKYGL NRVTCTLPRL 250
    YQLAQGGTAV GTGLNTKKGF DVKIAAAVAE ETNLPFVTAE NKFEALAAHD 300
    ACVETSGSLN TIATSLMKIA NDIRFLGSGP RCGLGELVLP ENEPGSSIMP 350
    GKVNPTQCEA LTMVCAQVMG NHVAVTVGGS NGHFELNVFK PVIASALLHS 400
    VRLIADASAS FEKNCVRGIE ANRERISKLL HESLMLVTSL NPKIGYDNAA 450
    AVAKKAHKEG CTLKEAALNL GVLTAEEFDT LVVPEKMIGP SD 492
    Length:492
    Mass (Da):53,000
    Last modified:December 15, 2003 - v2
    Checksum:iDF07D2D393966B3E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 92RR → A in AAB39989. 1 PublicationCurated
    Sequence conflicti197 – 1971S → R in AAB39989. 1 PublicationCurated
    Sequence conflicti393 – 3942IA → TS in AAB39989. 1 PublicationCurated
    Sequence conflicti442 – 4421P → R in AAB39989. 1 PublicationCurated
    Sequence conflicti446 – 4461Y → C in AAB39989. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82202 mRNA. Translation: AAB39989.1.
    AC002535 Genomic DNA. Translation: AAC62859.1.
    CP002685 Genomic DNA. Translation: AEC10852.1.
    CP002685 Genomic DNA. Translation: AEC10853.1.
    AF020303 Genomic DNA. Translation: AAB71399.1.
    AY054252 mRNA. Translation: AAL06911.1.
    AY062460 mRNA. Translation: AAL32538.1.
    BT003361 mRNA. Translation: AAO29979.1.
    PIRiT00433.
    RefSeqiNP_001078075.1. NM_001084606.1.
    NP_182273.1. NM_130319.3.
    UniGeneiAt.10398.

    Genome annotation databases

    EnsemblPlantsiAT2G47510.1; AT2G47510.1; AT2G47510.
    AT2G47510.2; AT2G47510.2; AT2G47510.
    GeneIDi819364.
    KEGGiath:AT2G47510.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82202 mRNA. Translation: AAB39989.1 .
    AC002535 Genomic DNA. Translation: AAC62859.1 .
    CP002685 Genomic DNA. Translation: AEC10852.1 .
    CP002685 Genomic DNA. Translation: AEC10853.1 .
    AF020303 Genomic DNA. Translation: AAB71399.1 .
    AY054252 mRNA. Translation: AAL06911.1 .
    AY062460 mRNA. Translation: AAL32538.1 .
    BT003361 mRNA. Translation: AAO29979.1 .
    PIRi T00433.
    RefSeqi NP_001078075.1. NM_001084606.1.
    NP_182273.1. NM_130319.3.
    UniGenei At.10398.

    3D structure databases

    ProteinModelPortali P93033.
    SMRi P93033. Positions 31-490.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 4699. 1 interaction.
    IntActi P93033. 1 interaction.

    Proteomic databases

    PaxDbi P93033.
    PRIDEi P93033.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G47510.1 ; AT2G47510.1 ; AT2G47510 .
    AT2G47510.2 ; AT2G47510.2 ; AT2G47510 .
    GeneIDi 819364.
    KEGGi ath:AT2G47510.

    Organism-specific databases

    GeneFarmi 4370. 440.
    TAIRi AT2G47510.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061736.
    InParanoidi P93033.
    KOi K01679.
    OMAi NAHPEYH.
    PhylomeDBi P93033.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci ARA:GQT-1578-MONOMER.

    Gene expression databases

    Genevestigatori P93033.

    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. Behal R.H., Oliver D.J.
      Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
      Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
      Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: cv. Landsberg erecta.

    Entry informationi

    Entry nameiFUM1_ARATH
    AccessioniPrimary (citable) accession number: P93033
    Secondary accession number(s): O24649
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3