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Q58673

- LEUD_METJA

UniProt

Q58673 - LEUD_METJA

Protein

Isopropylmalate/citramalate isomerase small subunit

Gene

leuD

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate.1 Publication

    Catalytic activityi

    (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate.1 Publication
    (R)-2-methylmalate = 2-methylmaleate + H2O.1 Publication
    2-methylmaleate + H2O = (2R,3S)-3-methylmalate.1 Publication
    (R)-malate = maleate + H2O.1 Publication

    Kineticsi

    1. KM=80 µM for 2-methylmaleate1 Publication
    2. KM=810 µM for (R)-2-methylmalate1 Publication
    3. KM=1900 µM for racemic 2-isopropylmalate1 Publication
    4. KM=39 µM for racemic 3-isopropylmalate1 Publication
    5. KM=400 µM for maleate1 Publication

    Vmax=15 µmol/min/mg enzyme for 2-methylmaleate hydration reaction1 Publication

    Vmax=1.5 µmol/min/mg enzyme for (R)-2-methylmalate dehydration reaction1 Publication

    Vmax=4.2 µmol/min/mg enzyme for 2-isopropylmalate dehydration reaction1 Publication

    Vmax=1.8 µmol/min/mg enzyme for 3-isopropylmalate dehydration reaction1 Publication

    Vmax=34 µmol/min/mg enzyme for maleate hydration reaction1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. (R)-2-methylmalate dehydratase activity Source: UniProtKB-EC
    2. 3-isopropylmalate dehydratase activity Source: UniProtKB-HAMAP
    3. maleate hydratase activity Source: UniProtKB-EC

    GO - Biological processi

    1. isoleucine biosynthetic process Source: UniProtKB-UniPathway
    2. leucine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Isoleucine biosynthesis, Leucine biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13648.
    SABIO-RKQ58673.
    UniPathwayiUPA00047; UER00067.
    UPA00048; UER00071.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isopropylmalate/citramalate isomerase small subunit (EC:4.2.1.33, EC:4.2.1.35)
    Alternative name(s):
    (R)-2-methylmalate dehydratase
    (R)-citramalate dehydratase
    3-isopropylmalate dehydratase
    Alpha-isopropylmalate dehydratase
    Citraconate hydratase
    Isopropylmalate isomerase
    Short name:
    IPMI
    Maleate hydratase (EC:4.2.1.31)
    Short name:
    Malease
    Gene namesi
    Name:leuD
    Ordered Locus Names:MJ1277
    OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
    Taxonomic identifieri243232 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
    ProteomesiUP000000805: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. 3-isopropylmalate dehydratase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 168168Isopropylmalate/citramalate isomerase small subunitPRO_0000141937Add
    BLAST

    Interactioni

    Subunit structurei

    Heterotetramer of 2 LeuC and 2 LeuD. The heterotetramer that can be formed in vitro between HacA and LeuD is inactive.1 Publication

    Protein-protein interaction databases

    STRINGi243232.MJ1277.

    Structurei

    Secondary structure

    1
    168
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 119
    Helixi18 – 214
    Helixi24 – 263
    Helixi32 – 354
    Helixi36 – 383
    Turni39 – 435
    Helixi47 – 504
    Beta strandi56 – 594
    Beta strandi65 – 673
    Helixi71 – 788
    Beta strandi83 – 875
    Helixi91 – 999
    Beta strandi104 – 1063
    Helixi110 – 1134
    Beta strandi119 – 1235
    Turni124 – 1263
    Beta strandi128 – 1314
    Turni132 – 1343
    Beta strandi137 – 1393
    Helixi145 – 1539
    Helixi156 – 16510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VBAX-ray2.00A/B/C/D/E/F1-168[»]
    ProteinModelPortaliQ58673.
    SMRiQ58673. Positions 4-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LeuD family.Curated

    Phylogenomic databases

    eggNOGiCOG0066.
    KOiK01704.
    OMAiCMEDIDL.
    PhylomeDBiQ58673.

    Family and domain databases

    Gene3Di3.20.19.10. 1 hit.
    HAMAPiMF_01032. LeuD_type2.
    InterProiIPR015937. Acoase/IPM_deHydtase.
    IPR015928. Aconitase/3IPM_dehydase_swvl.
    IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
    IPR011827. IsopropMal_deHydtase_ssu.
    [Graphical view]
    PANTHERiPTHR11670. PTHR11670. 1 hit.
    PfamiPF00694. Aconitase_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF52016. SSF52016. 1 hit.
    TIGRFAMsiTIGR02087. LEUD_arch. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q58673-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRSIIKGRVW KFGNNVDTDA ILPARYLVYT KPEELAQFVM TGADPDFPKK    50
    VKPGDIIVGG KNFGCGSSRE HAPLGLKGAG ISCVIAESFA RIFYRNAINV 100
    GLPLIECKGI SEKVNEGDEL EVNLETGEIK NLTTGEVLKG QKLPEFMMEI 150
    LEAGGLMPYL KKKMAESQ 168
    Length:168
    Mass (Da):18,377
    Last modified:November 1, 1996 - v1
    Checksum:iA53C2CA883B6CCD7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77117 Genomic DNA. Translation: AAB99283.1.
    PIRiD64459.
    RefSeqiNP_248273.1. NC_000909.1.
    WP_010870790.1. NC_000909.1.

    Genome annotation databases

    EnsemblBacteriaiAAB99283; AAB99283; MJ_1277.
    GeneIDi1452175.
    KEGGimja:MJ_1277.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77117 Genomic DNA. Translation: AAB99283.1 .
    PIRi D64459.
    RefSeqi NP_248273.1. NC_000909.1.
    WP_010870790.1. NC_000909.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VBA X-ray 2.00 A/B/C/D/E/F 1-168 [» ]
    ProteinModelPortali Q58673.
    SMRi Q58673. Positions 4-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243232.MJ1277.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB99283 ; AAB99283 ; MJ_1277 .
    GeneIDi 1452175.
    KEGGi mja:MJ_1277.

    Phylogenomic databases

    eggNOGi COG0066.
    KOi K01704.
    OMAi CMEDIDL.
    PhylomeDBi Q58673.

    Enzyme and pathway databases

    UniPathwayi UPA00047 ; UER00067 .
    UPA00048 ; UER00071 .
    BioCyci MetaCyc:MONOMER-13648.
    SABIO-RK Q58673.

    Family and domain databases

    Gene3Di 3.20.19.10. 1 hit.
    HAMAPi MF_01032. LeuD_type2.
    InterProi IPR015937. Acoase/IPM_deHydtase.
    IPR015928. Aconitase/3IPM_dehydase_swvl.
    IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
    IPR011827. IsopropMal_deHydtase_ssu.
    [Graphical view ]
    PANTHERi PTHR11670. PTHR11670. 1 hit.
    Pfami PF00694. Aconitase_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52016. SSF52016. 1 hit.
    TIGRFAMsi TIGR02087. LEUD_arch. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
    2. "Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in Methanocaldococcus jannaschii."
      Drevland R.M., Waheed A., Graham D.E.
      J. Bacteriol. 189:4391-4400(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
    3. "Crystal structure of LeuD from Methanococcus jannaschii."
      Lee E.H., Cho Y.W., Hwang K.Y.
      Biochem. Biophys. Res. Commun. 419:160-164(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiLEUD_METJA
    AccessioniPrimary (citable) accession number: Q58673
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Methanococcus jannaschii
      Methanococcus jannaschii: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3