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Protein

L-Ala-D/L-Glu epimerase

Gene

BT_1313

Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and may play a role in the metabolism of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the epimerization of L-Ala-D-Asp, L-Ala-L-Glu, L-Ala-L-Ser, L-Ala-L-Pro, L-Ala-L-L-Val, L-Ala-L-Thr, L-Ala-L-Leu, L-Ala-L-Ile and L-Gly-L-Glu (in vitro).1 Publication

Catalytic activityi

L-alanyl-D-glutamate = L-alanyl-L-glutamate.

Cofactori

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

Kineticsi

kcat is 147 sec(-1) for epimerization of L-Ala-L-Glu. kcat is 59 sec(-1) for epimerization of L-Ala-D-Glu. kcat is 96 sec(-1) for epimerization of L-Val-L-Glu. kcat is 43 sec(-1) for epimerization of L-Val-D-Glu. kcat is 30 sec(-1) for epimerization of L-Ile-L-Glu.

  1. KM=2.0 mM for L-Ala-L-Glu1 Publication
  2. KM=6.0 mM for L-Ala-D-Glu1 Publication
  3. KM=1.7 mM for L-Val-L-Glu1 Publication
  4. KM=4.4 mM for L-Val-D-Glu1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei68 – 681Substrate
    Binding sitei94 – 941Substrate
    Metal bindingi224 – 2241Magnesium1 Publication
    Metal bindingi251 – 2511Magnesium1 Publication
    Metal bindingi276 – 2761Magnesium1 Publication
    Binding sitei298 – 2981Substrate

    GO - Molecular functioni

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

    GO - Biological processi

    • cell wall organization Source: UniProtKB-KW
    • peptide metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciBTHE226186:GJXV-1340-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-Ala-D/L-Glu epimerase (EC:5.1.1.20)
    Short name:
    AE epimerase
    Short name:
    AEE
    Gene namesi
    Ordered Locus Names:BT_1313
    OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
    Taxonomic identifieri226186 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
    Proteomesi
    • UP000001414 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 383383L-Ala-D/L-Glu epimerasePRO_0000429646Add
    BLAST

    Proteomic databases

    PaxDbiQ8A861.

    Interactioni

    Protein-protein interaction databases

    STRINGi226186.BT_1313.

    Structurei

    Secondary structure

    1
    383
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi48 – 525Combined sources
    Beta strandi55 – 639Combined sources
    Beta strandi66 – 716Combined sources
    Beta strandi73 – 808Combined sources
    Beta strandi83 – 908Combined sources
    Helixi93 – 953Combined sources
    Helixi99 – 1068Combined sources
    Helixi120 – 12910Combined sources
    Helixi135 – 15319Combined sources
    Helixi157 – 1604Combined sources
    Helixi165 – 1673Combined sources
    Helixi180 – 19112Combined sources
    Beta strandi195 – 2006Combined sources
    Beta strandi202 – 2043Combined sources
    Helixi206 – 2149Combined sources
    Beta strandi221 – 2244Combined sources
    Helixi232 – 24413Combined sources
    Beta strandi247 – 2515Combined sources
    Helixi256 – 2583Combined sources
    Helixi259 – 2679Combined sources
    Beta strandi273 – 2764Combined sources
    Helixi282 – 2843Combined sources
    Helixi286 – 2883Combined sources
    Turni289 – 2913Combined sources
    Beta strandi292 – 2976Combined sources
    Helixi299 – 3024Combined sources
    Helixi305 – 31713Combined sources
    Beta strandi321 – 3244Combined sources
    Helixi331 – 3388Combined sources
    Helixi339 – 3435Combined sources
    Beta strandi345 – 3473Combined sources
    Helixi351 – 3544Combined sources
    Beta strandi364 – 3663Combined sources
    Beta strandi369 – 3713Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IJIX-ray1.60A/B46-383[»]
    3IJLX-ray1.50A/B46-383[»]
    3IJQX-ray2.00A/B46-383[»]
    ProteinModelPortaliQ8A861.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni198 – 2003Substrate binding
    Regioni326 – 3283Substrate binding
    Regioni348 – 3503Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105DTQ. Bacteria.
    COG4948. LUCA.
    InParanoidiQ8A861.
    KOiK19802.
    OMAiANEAWSG.
    OrthoDBiEOG68WR4X.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    InterProiIPR029065. Enolase_C-like.
    IPR029017. Enolase_N-like.
    IPR013342. Mandelate_racemase_C.
    IPR013341. Mandelate_racemase_N_dom.
    IPR001354. MR/MLE/MAL.
    IPR006311. TAT_signal.
    IPR019546. TAT_signal_bac_arc.
    [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.
    TIGRFAMsiTIGR01409. TAT_signal_seq. 1 hit.
    PROSITEiPS51318. TAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8A861-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPNRRDFLKT AAFATLGSGI AVSQVLAGEC MPSAIHINKY GIGGKMKMTF
    60 70 80 90 100
    FPYELKLRHV FTVATYSRTT TPDVQVEIEY EGVTGYGEAS MPPYLGETVE
    110 120 130 140 150
    SVMNFLKKVN LEQFSDPFQL EDILSYVDSL SPKDTAAKAA VDIALHDLVG
    160 170 180 190 200
    KLLGAPWYKI WGLNKEKTPS TTFTIGIDTP DVVRAKTKEC AGLFNILKVK
    210 220 230 240 250
    LGRDNDKEMI ETIRSVTDLP IAVDANQGWK DRQYALDMIH WLKEKGIVMI
    260 270 280 290 300
    EQPMPKEQLD DIAWVTQQSP LPVFADESLQ RLGDVAALKG AFTGINIKLM
    310 320 330 340 350
    KCTGMREAWK MVTLAHALGM RVMVGCMTET SCAISAASQF SPAVDFADLD
    360 370 380
    GNLLISNDRF KGVEVVNGKI TLNDLPGIGV MKI
    Length:383
    Mass (Da):42,168
    Last modified:June 1, 2003 - v1
    Checksum:i1088235F1C0A356F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE015928 Genomic DNA. Translation: AAO76420.1.
    RefSeqiNP_810226.1. NC_004663.1.
    WP_011107704.1. NC_004663.1.

    Genome annotation databases

    EnsemblBacteriaiAAO76420; AAO76420; BT_1313.
    GeneIDi1073218.
    KEGGibth:BT_1313.
    PATRICi21057481. VBIBacThe70966_1342.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE015928 Genomic DNA. Translation: AAO76420.1.
    RefSeqiNP_810226.1. NC_004663.1.
    WP_011107704.1. NC_004663.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IJIX-ray1.60A/B46-383[»]
    3IJLX-ray1.50A/B46-383[»]
    3IJQX-ray2.00A/B46-383[»]
    ProteinModelPortaliQ8A861.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi226186.BT_1313.

    Proteomic databases

    PaxDbiQ8A861.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAO76420; AAO76420; BT_1313.
    GeneIDi1073218.
    KEGGibth:BT_1313.
    PATRICi21057481. VBIBacThe70966_1342.

    Phylogenomic databases

    eggNOGiENOG4105DTQ. Bacteria.
    COG4948. LUCA.
    InParanoidiQ8A861.
    KOiK19802.
    OMAiANEAWSG.
    OrthoDBiEOG68WR4X.

    Enzyme and pathway databases

    BioCyciBTHE226186:GJXV-1340-MONOMER.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    InterProiIPR029065. Enolase_C-like.
    IPR029017. Enolase_N-like.
    IPR013342. Mandelate_racemase_C.
    IPR013341. Mandelate_racemase_N_dom.
    IPR001354. MR/MLE/MAL.
    IPR006311. TAT_signal.
    IPR019546. TAT_signal_bac_arc.
    [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.
    TIGRFAMsiTIGR01409. TAT_signal_seq. 1 hit.
    PROSITEiPS51318. TAT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
      Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
      Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 46-383 IN COMPLEX WITH DIPEPTIDE AND MAGNESIUM, COFACTOR, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

    Entry informationi

    Entry nameiAEEP_BACTN
    AccessioniPrimary (citable) accession number: Q8A861
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 9, 2014
    Last sequence update: June 1, 2003
    Last modified: April 13, 2016
    This is version 84 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 were 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.