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Protein

3-methylitaconate isomerase

Gene

mii

Organism
Eubacterium barkeri (Clostridium barkeri)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible isomerization of (R)-3-methylitaconate to 2,3-dimethylmaleate. Has very low isomerase activity with itaconate.1 Publication

Catalytic activityi

Methylitaconate = 2,3-dimethylmaleate.3 Publications

Enzyme regulationi

Inhibited by oxidized glutathione, p-chloromercuriphenylsulfonic acid and iodoacetic acid. Not inhibited by the chelating agent alpha,alpha-dipyridyl. Activity is slightly increased by EDTA. Not activated by Fe2+, Mg2+, Mn2+ or Ca2+. Unaffected by K+, Na+, NH4+, Rb+ or Li+.1 Publication

Kineticsi

  1. KM=7 mM for (R,S)-3-methylitaconate2 Publications
  2. KM=60 mM for itaconate2 Publications

    pH dependencei

    Optimum pH is 6.8-8.2.2 Publications

    Pathwayi: nicotinate degradation

    This protein is involved in step 6 of the subpathway that synthesizes propanoate and pyruvate from 6-hydroxynicotinate.1 Publication
    Proteins known to be involved in the 8 steps of the subpathway in this organism are:
    1. 6-hydroxynicotinate reductase (Hnr)
    2. Enamidase (Ena)
    3. 2-(hydroxymethyl)glutarate dehydrogenase (Hgd)
    4. no protein annotated in this organism
    5. 2-methyleneglutarate mutase (mgm)
    6. 3-methylitaconate isomerase (mii)
    7. 2,3-dimethylmalate dehydratase small subunit (DmdB), 2,3-dimethylmalate dehydratase large subunit (dmdA)
    8. 2,3-dimethylmalate lyase (Dml)
    This subpathway is part of the pathway nicotinate degradation, which is itself part of Cofactor degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes propanoate and pyruvate from 6-hydroxynicotinate, the pathway nicotinate degradation and in Cofactor degradation.

    GO - Molecular functioni

    • methylitaconate delta-isomerase activity Source: UniProtKB

    GO - Biological processi

    • cofactor catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-11717.
    BRENDAi5.3.3.6. 1459.
    UniPathwayiUPA01010; UER01017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-methylitaconate isomerase (EC:5.3.3.6)
    Alternative name(s):
    (R)-3-methylitaconate isomerase1 Publication
    3-methylitaconate delta-isomerase
    Gene namesi
    Name:mii
    OrganismiEubacterium barkeri (Clostridium barkeri)
    Taxonomic identifieri1528 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeEubacterium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004040921 – 3803-methylitaconate isomeraseAdd BLAST380

    Proteomic databases

    PRIDEiQ0QLE6.

    Expressioni

    Inductioni

    By nicotinate.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Structurei

    Secondary structure

    1380
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 14Combined sources11
    Beta strandi17 – 23Combined sources7
    Helixi24 – 26Combined sources3
    Helixi31 – 42Combined sources12
    Beta strandi52 – 54Combined sources3
    Helixi58 – 60Combined sources3
    Beta strandi61 – 68Combined sources8
    Beta strandi75 – 83Combined sources9
    Beta strandi85 – 88Combined sources4
    Helixi97 – 109Combined sources13
    Beta strandi117 – 126Combined sources10
    Turni127 – 129Combined sources3
    Beta strandi132 – 140Combined sources9
    Beta strandi155 – 157Combined sources3
    Beta strandi162 – 165Combined sources4
    Helixi167 – 169Combined sources3
    Turni171 – 174Combined sources4
    Beta strandi175 – 178Combined sources4
    Beta strandi185 – 187Combined sources3
    Beta strandi194 – 210Combined sources17
    Helixi211 – 213Combined sources3
    Helixi221 – 225Combined sources5
    Helixi228 – 244Combined sources17
    Helixi251 – 257Combined sources7
    Beta strandi259 – 269Combined sources11
    Turni276 – 278Combined sources3
    Beta strandi288 – 294Combined sources7
    Beta strandi296 – 299Combined sources4
    Helixi305 – 316Combined sources12
    Helixi321 – 325Combined sources5
    Beta strandi334 – 339Combined sources6
    Beta strandi342 – 351Combined sources10
    Beta strandi354 – 362Combined sources9
    Beta strandi364 – 375Combined sources12
    Helixi376 – 378Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3G7KX-ray2.70A/B/C/D1-380[»]
    ProteinModelPortaliQ0QLE6.
    SMRiQ0QLE6.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ0QLE6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PrpF family.Curated

    Phylogenomic databases

    KOiK20451.

    Family and domain databases

    InterProiIPR007400. PrpF_protein.
    [Graphical view]
    PfamiPF04303. PrpF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q0QLE6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSDQMRIPCV IMRAGTSKGI FLKGNDLPAD QELRDKVILR IFGSPDVRQI
    60 70 80 90 100
    DGLAGADPLT SKLAIIGPST HPDADVDYTF AQVSITDAVV DYNGNCGNIS
    110 120 130 140 150
    AGVGPFAIDE SFVKAVEPMT RVCIHNTNTG KLLYAEVEVE DGKAKVSGDC
    160 170 180 190 200
    KIDGVPGTNA PELMDFSDTA GAATGKVLPT GNVVDVLSTS KGDIDVSIVD
    210 220 230 240 250
    VANPCIFVHA KDVNMTGTET PDVINGNADL LAYLEEIRAK CCVKIGMAAT
    260 270 280 290 300
    EKEASEKSPA FPMIAFVTKP EDYVDFSTGN TISGDDVDLV SRLMFMQVLH
    310 320 330 340 350
    KTYAGTATAC TGSAARIPGT IVNQVLRDTG DEDTVRIGHP AGVIPVVSIV
    360 370 380
    KDGKVEKAAL IRTARRIMEG YVYVEKAKLV
    Length:380
    Mass (Da):40,273
    Last modified:September 5, 2006 - v1
    Checksum:i6D37CCBC1CD128D9
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DQ310789 Genomic DNA. Translation: ABC88404.1.

    Genome annotation databases

    KEGGiag:ABC88404.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DQ310789 Genomic DNA. Translation: ABC88404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3G7KX-ray2.70A/B/C/D1-380[»]
    ProteinModelPortaliQ0QLE6.
    SMRiQ0QLE6.
    ModBaseiSearch...
    MobiDBiSearch...

    Proteomic databases

    PRIDEiQ0QLE6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:ABC88404.

    Phylogenomic databases

    KOiK20451.

    Enzyme and pathway databases

    UniPathwayiUPA01010; UER01017.
    BioCyciMetaCyc:MONOMER-11717.
    BRENDAi5.3.3.6. 1459.

    Miscellaneous databases

    EvolutionaryTraceiQ0QLE6.

    Family and domain databases

    InterProiIPR007400. PrpF_protein.
    [Graphical view]
    PfamiPF04303. PrpF. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMII_EUBBA
    AccessioniPrimary (citable) accession number: Q0QLE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 8, 2011
    Last sequence update: September 5, 2006
    Last modified: November 2, 2016
    This is version 35 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

    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

    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.