Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

C0RFF1

- LEUC_BRUMB

UniProt

C0RFF1 - LEUC_BRUMB

Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Brucella melitensis biotype 2 (strain ATCC 23457)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 39 (01 Oct 2014)
      Sequence version 1 (05 May 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.UniRule annotation

    Catalytic activityi

    (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate.UniRule annotation

    Cofactori

    Binds 1 4Fe-4S cluster per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi350 – 3501Iron-sulfur (4Fe-4S)UniRule annotation
    Metal bindingi410 – 4101Iron-sulfur (4Fe-4S)UniRule annotation
    Metal bindingi413 – 4131Iron-sulfur (4Fe-4S)UniRule annotation

    GO - Molecular functioni

    1. 3-isopropylmalate dehydratase activity Source: UniProtKB-HAMAP
    2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. leucine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

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

    Keywords - Ligandi

    4Fe-4S, Iron, Iron-sulfur, Metal-binding

    Enzyme and pathway databases

    BioCyciBMEL546272:GJOX-1909-MONOMER.
    UniPathwayiUPA00048; UER00071.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-isopropylmalate dehydratase large subunitUniRule annotation (EC:4.2.1.33UniRule annotation)
    Alternative name(s):
    Alpha-IPM isomeraseUniRule annotation
    Short name:
    IPMIUniRule annotation
    Isopropylmalate isomeraseUniRule annotation
    Gene namesi
    Name:leuCUniRule annotation
    Ordered Locus Names:BMEA_A1961
    OrganismiBrucella melitensis biotype 2 (strain ATCC 23457)
    Taxonomic identifieri546272 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
    ProteomesiUP000001748: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4694693-isopropylmalate dehydratase large subunitPRO_1000149356Add
    BLAST

    Interactioni

    Subunit structurei

    Heterodimer of LeuC and LeuD.UniRule annotation

    Protein-protein interaction databases

    STRINGi546272.BMEA_A1961.

    Structurei

    3D structure databases

    ProteinModelPortaliC0RFF1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0065.
    HOGENOMiHOG000226972.
    KOiK01703.
    OMAiQARAKTM.
    OrthoDBiEOG600DP5.

    Family and domain databases

    Gene3Di3.30.499.10. 3 hits.
    3.40.1060.10. 1 hit.
    HAMAPiMF_01026. LeuC_type1.
    InterProiIPR004430. 3-IsopropMal_deHydase_lsu.
    IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
    IPR015937. Acoase/IPM_deHydtase.
    IPR001030. Acoase/IPM_deHydtase_lsu_aba.
    IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
    IPR018136. Aconitase_4Fe-4S_BS.
    [Graphical view]
    PANTHERiPTHR11670. PTHR11670. 1 hit.
    PfamiPF00330. Aconitase. 1 hit.
    [Graphical view]
    PRINTSiPR00415. ACONITASE.
    SUPFAMiSSF53732. SSF53732. 1 hit.
    TIGRFAMsiTIGR00170. leuC. 1 hit.
    PROSITEiPS00450. ACONITASE_1. 1 hit.
    PS01244. ACONITASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    C0RFF1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAPRTLYDK IWDDHVVDQQ EDGTCLLYID RHLVHEVTSP QAFEGLHMAG    50
    RPVRHPEKTL AVVDHNVPTS PDRINGIQNE ESRIQVEALA RNAADFGVEY 100
    YSERDKRQGI VHIVGPEQGF TLPGMTIVCG DSHTSTHGAF GALAHGIGTS 150
    EVEHVLATQT LIQKKAKNML VRVDGKLPAG VTAKDIVLAI IGEIGTAGGT 200
    GYVIEYAGEA IRSLSMEGRM TICNMSIEGG ARAGLIAPDE TTFEYIKGRP 250
    RAPQGETLEQ AINYWKTLHS DEGAHFDKIV TLDAGSLPPI VSWGSSPEDV 300
    VSVTGVVPNP DDIADETKRA SKWRALDYMG LKPGTKITDI AVDRVFIGSC 350
    TNGRIEDLRA AAKVVEGKKV APTVNAMIVP GSGLVKEQAE AEGLHKIFIE 400
    AGFDWREPGC SMCLAMNDDR LKPGERCAST SNRNFEGRQG FKGRTHLVSP 450
    AMAAAAAIAG HFVDIRAWK 469
    Length:469
    Mass (Da):50,692
    Last modified:May 5, 2009 - v1
    Checksum:i14442D949C40BCDF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001488 Genomic DNA. Translation: ACO01623.1.
    RefSeqiYP_002733577.1. NC_012441.1.

    Genome annotation databases

    EnsemblBacteriaiACO01623; ACO01623; BMEA_A1961.
    GeneIDi7677608.
    KEGGibmi:BMEA_A1961.
    PATRICi17839718. VBIBruMel14466_1976.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001488 Genomic DNA. Translation: ACO01623.1 .
    RefSeqi YP_002733577.1. NC_012441.1.

    3D structure databases

    ProteinModelPortali C0RFF1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 546272.BMEA_A1961.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACO01623 ; ACO01623 ; BMEA_A1961 .
    GeneIDi 7677608.
    KEGGi bmi:BMEA_A1961.
    PATRICi 17839718. VBIBruMel14466_1976.

    Phylogenomic databases

    eggNOGi COG0065.
    HOGENOMi HOG000226972.
    KOi K01703.
    OMAi QARAKTM.
    OrthoDBi EOG600DP5.

    Enzyme and pathway databases

    UniPathwayi UPA00048 ; UER00071 .
    BioCyci BMEL546272:GJOX-1909-MONOMER.

    Miscellaneous databases

    PROi C0RFF1.

    Family and domain databases

    Gene3Di 3.30.499.10. 3 hits.
    3.40.1060.10. 1 hit.
    HAMAPi MF_01026. LeuC_type1.
    InterProi IPR004430. 3-IsopropMal_deHydase_lsu.
    IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
    IPR015937. Acoase/IPM_deHydtase.
    IPR001030. Acoase/IPM_deHydtase_lsu_aba.
    IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
    IPR018136. Aconitase_4Fe-4S_BS.
    [Graphical view ]
    PANTHERi PTHR11670. PTHR11670. 1 hit.
    Pfami PF00330. Aconitase. 1 hit.
    [Graphical view ]
    PRINTSi PR00415. ACONITASE.
    SUPFAMi SSF53732. SSF53732. 1 hit.
    TIGRFAMsi TIGR00170. leuC. 1 hit.
    PROSITEi PS00450. ACONITASE_1. 1 hit.
    PS01244. ACONITASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project."
      Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C.
      , Tapia R., Han C., Detter J.C., Bruce D., Brettin T.S.
      Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 23457.

    Entry informationi

    Entry nameiLEUC_BRUMB
    AccessioniPrimary (citable) accession number: C0RFF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 39 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

    Complete proteome

    Documents

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

    External Data

    Dasty 3