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Protein

Hydrophobic dipeptide epimerase

Gene

EF_1511

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the epimerization of L-Ile-L-Tyr to L-Ile-D-Tyr (in vitro). Catalyzes the epimerization of dipeptides, with a preference for substrates with a hydrophobic or basic amino acid in the first position, followed by an aromatic residue in the second position. Has epimerase activity with L-Ile-L-Tyr, L-Val-L-Tyr and L-Arg-L-Tyr (in vitro).1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Kineticsi

kcat is 9.2 sec(-1) for epimerization of L-Ile-L-Tyr. kcat is 8.7 sec(-1) for epimerization of L-Val-L-Tyr. kcat is 15 sec(-1) for epimerization of L-Arg-L-Tyr.

  1. KM=0.7 mM for L-Val-L-Tyr1 Publication
  2. KM=1.4 mM for L-Arg-L-Tyr1 Publication
  3. KM=0.77 mM for L-Ile-L-Tyr1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei134 – 1341Substrate
    Binding sitei159 – 1591Substrate
    Metal bindingi189 – 1891Magnesium
    Binding sitei191 – 1911Substrate
    Metal bindingi215 – 2151Magnesium
    Metal bindingi240 – 2401Magnesium
    Binding sitei264 – 2641Substrate

    GO - Molecular functioni

    • magnesium ion binding Source: UniProtKB
    • racemase and epimerase activity Source: UniProtKB

    GO - Biological processi

    • cellular amino acid catabolic process Source: InterPro
    • peptide metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEFAE226185:GHI1-1500-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hydrophobic dipeptide epimerase (EC:5.1.1.-)
    Gene namesi
    Ordered Locus Names:EF_1511
    ORF Names:I574_01909, OO5_01959
    OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
    Taxonomic identifieri226185 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
    Proteomesi
    • UP000001415 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 354354Hydrophobic dipeptide epimerasePRO_0000429653Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi226185.EF1511.

    Structurei

    Secondary structure

    1
    354
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 2119Combined sources
    Beta strandi24 – 3815Combined sources
    Beta strandi43 – 486Combined sources
    Turni52 – 543Combined sources
    Helixi59 – 7012Combined sources
    Turni73 – 753Combined sources
    Helixi81 – 9111Combined sources
    Helixi96 – 11419Combined sources
    Helixi118 – 1214Combined sources
    Beta strandi127 – 1304Combined sources
    Beta strandi133 – 1353Combined sources
    Helixi140 – 15213Combined sources
    Beta strandi156 – 1616Combined sources
    Helixi166 – 18015Combined sources
    Beta strandi184 – 1896Combined sources
    Helixi196 – 20510Combined sources
    Turni206 – 2083Combined sources
    Beta strandi211 – 2155Combined sources
    Helixi223 – 23210Combined sources
    Beta strandi234 – 2407Combined sources
    Helixi246 – 25510Combined sources
    Beta strandi259 – 2635Combined sources
    Helixi265 – 2684Combined sources
    Helixi271 – 28313Combined sources
    Beta strandi287 – 2904Combined sources
    Helixi298 – 31013Combined sources
    Beta strandi314 – 3174Combined sources
    Helixi321 – 3244Combined sources
    Beta strandi325 – 3273Combined sources
    Beta strandi329 – 3346Combined sources
    Beta strandi340 – 3434Combined sources
    Beta strandi346 – 3494Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3JVAX-ray1.70A/B/C/D/E/F/G/H1-354[»]
    3JW7X-ray1.80A/B/C/D/E/F/G/H1-354[»]
    3JZUX-ray2.00A/B/C/D/E/F/G/H1-354[»]
    3K1GX-ray2.00A/B/C/D/E/F/G/H1-354[»]
    3KUMX-ray1.90A/B/C/D/E/F/G/H1-354[»]
    ProteinModelPortaliQ834W6.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ834W6.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni159 – 1613Substrate binding
    Regioni292 – 2954Substrate binding
    Regioni318 – 3203Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105DTQ. Bacteria.
    COG4948. LUCA.
    KOiK19802.
    OMAiDFDAPLM.
    OrthoDBiEOG6S52NQ.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    InterProiIPR029065. Enolase_C-like.
    IPR029017. Enolase_N-like.
    IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
    IPR013342. Mandelate_racemase_C.
    IPR013341. Mandelate_racemase_N_dom.
    IPR001354. MR/MLE/MAL.
    [Graphical view]
    PANTHERiPTHR13794. PTHR13794. 1 hit.
    PfamiPF13378. MR_MLE_C. 1 hit.
    PF02746. MR_MLE_N. 1 hit.
    [Graphical view]
    SMARTiSM00922. MR_MLE. 1 hit.
    [Graphical view]
    SUPFAMiSSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    PROSITEiPS00909. MR_MLE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q834W6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKIKQVHVRA SKIKLKETFT IALGTIESAD SAIVEIETEE GLVGYGEGGP
    60 70 80 90 100
    GIFITGETLA GTLETIELFG QAIIGLNPFN IEKIHEVMDK ISAFAPAAKA
    110 120 130 140 150
    AIDIACYDLM GQKAQLPLYQ LLGGYDNQVI TDITLGIDEP NVMAQKAVEK
    160 170 180 190 200
    VKLGFDTLKI KVGTGIEADI ARVKAIREAV GFDIKLRLDA NQAWTPKDAV
    210 220 230 240 250
    KAIQALADYQ IELVEQPVKR RDLEGLKYVT SQVNTTIMAD ESCFDAQDAL
    260 270 280 290 300
    ELVKKGTVDV INIKLMKCGG IHEALKINQI CETAGIECMI GCMAEETTIG
    310 320 330 340 350
    ITAAAHLAAA QKNITRADLD ATFGLETAPV TGGVSLEAKP LLELGEAAGL

    GISH
    Length:354
    Mass (Da):37,807
    Last modified:June 1, 2003 - v1
    Checksum:iD94FBCE053A4D531
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE016830 Genomic DNA. Translation: AAO81302.1.
    AHYN01000009 Genomic DNA. Translation: EOT50195.1.
    ASWP01000006 Genomic DNA. Translation: EOT84729.1.
    RefSeqiNP_815232.1. NC_004668.1.
    WP_002382304.1. NZ_KE136528.1.

    Genome annotation databases

    EnsemblBacteriaiAAO81302; AAO81302; EF_1511.
    EOT50195; EOT50195; OO5_01959.
    EOT84729; EOT84729; I574_01909.
    GeneIDi1200414.
    KEGGiefa:EF1511.
    PATRICi21853388. VBIEntFae7065_1420.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE016830 Genomic DNA. Translation: AAO81302.1.
    AHYN01000009 Genomic DNA. Translation: EOT50195.1.
    ASWP01000006 Genomic DNA. Translation: EOT84729.1.
    RefSeqiNP_815232.1. NC_004668.1.
    WP_002382304.1. NZ_KE136528.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3JVAX-ray1.70A/B/C/D/E/F/G/H1-354[»]
    3JW7X-ray1.80A/B/C/D/E/F/G/H1-354[»]
    3JZUX-ray2.00A/B/C/D/E/F/G/H1-354[»]
    3K1GX-ray2.00A/B/C/D/E/F/G/H1-354[»]
    3KUMX-ray1.90A/B/C/D/E/F/G/H1-354[»]
    ProteinModelPortaliQ834W6.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi226185.EF1511.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAO81302; AAO81302; EF_1511.
    EOT50195; EOT50195; OO5_01959.
    EOT84729; EOT84729; I574_01909.
    GeneIDi1200414.
    KEGGiefa:EF1511.
    PATRICi21853388. VBIEntFae7065_1420.

    Phylogenomic databases

    eggNOGiENOG4105DTQ. Bacteria.
    COG4948. LUCA.
    KOiK19802.
    OMAiDFDAPLM.
    OrthoDBiEOG6S52NQ.

    Enzyme and pathway databases

    BioCyciEFAE226185:GHI1-1500-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiQ834W6.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    InterProiIPR029065. Enolase_C-like.
    IPR029017. Enolase_N-like.
    IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
    IPR013342. Mandelate_racemase_C.
    IPR013341. Mandelate_racemase_N_dom.
    IPR001354. MR/MLE/MAL.
    [Graphical view]
    PANTHERiPTHR13794. PTHR13794. 1 hit.
    PfamiPF13378. MR_MLE_C. 1 hit.
    PF02746. MR_MLE_N. 1 hit.
    [Graphical view]
    SMARTiSM00922. MR_MLE. 1 hit.
    [Graphical view]
    SUPFAMiSSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    PROSITEiPS00909. MR_MLE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700802 / V583.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700802 / V583.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700802 / V583.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEXES WITH DIPEPTIDE AND MAGNESIUM, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 700802 / V583.

    Entry informationi

    Entry nameiHYEP_ENTFA
    AccessioniPrimary (citable) accession number: Q834W6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 9, 2014
    Last sequence update: June 1, 2003
    Last modified: April 13, 2016
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Part of a large, functionally divergent protein family. Protein modeling and substrate docking was used to predict the substrate specificity, prior to biochemical analysis.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.