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Protein

Protein BMEI1586

Gene

BMEI1586

Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

In vitro, catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp) and that of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp), albeit with very low efficiency. The physiological substrate may be different (PubMed:24980702). Displays neither proline racemase activity nor t3LHyp dehydratase activity (PubMed:17849014, PubMed:24980702).1 Publication2 Publications

Catalytic activityi

Trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline.1 Publication

Kineticsi

kcat is 0.082 sec(-1) for t4LHyp epimerization. kcat is 0.085 sec(-1) for t3LHyp epimerization.1 Publication

  1. KM=4.5 mM for trans-4-hydroxy-L-proline1 Publication
  2. KM=2.6 mM for trans-3-hydroxy-L-proline1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei90 – 901Proton acceptorBy similarity
    Binding sitei251 – 2511SubstrateBy similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein BMEI1586 (EC:5.1.1.81 Publication)
    Gene namesi
    Ordered Locus Names:BMEI1586
    OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
    Taxonomic identifieri224914 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
    Proteomesi
    • UP000000419 Componenti: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 342342Protein BMEI1586PRO_0000354042Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi224914.BAWG_0638.

    Structurei

    Secondary structure

    1
    342
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 148Combined sources
    Beta strandi20 – 256Combined sources
    Beta strandi30 – 334Combined sources
    Helixi34 – 4411Combined sources
    Helixi46 – 527Combined sources
    Turni54 – 563Combined sources
    Beta strandi63 – 675Combined sources
    Beta strandi71 – 733Combined sources
    Beta strandi75 – 795Combined sources
    Helixi91 – 10313Combined sources
    Beta strandi111 – 1199Combined sources
    Beta strandi124 – 1318Combined sources
    Beta strandi133 – 14210Combined sources
    Beta strandi146 – 1483Combined sources
    Beta strandi152 – 1565Combined sources
    Beta strandi158 – 17821Combined sources
    Helixi179 – 1813Combined sources
    Helixi188 – 20215Combined sources
    Beta strandi223 – 2275Combined sources
    Beta strandi231 – 2399Combined sources
    Helixi256 – 26813Combined sources
    Beta strandi277 – 2804Combined sources
    Beta strandi288 – 29811Combined sources
    Beta strandi301 – 31010Combined sources
    Beta strandi312 – 3209Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TM0X-ray2.80A/B1-342[»]
    ProteinModelPortaliQ8YFD6.
    SMRiQ8YFD6. Positions 1-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8YFD6.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni91 – 922Substrate bindingBy similarity
    Regioni256 – 2572Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the proline racemase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CTU. Bacteria.
    COG3938. LUCA.
    HOGENOMiHOG000084336.
    KOiK01777.
    OMAiWITGIHQ.
    OrthoDBiEOG6SNDV3.

    Family and domain databases

    InterProiIPR008794. Pro_racemase_fam.
    [Graphical view]
    PfamiPF05544. Pro_racemase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF029792. Pro_racemase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8YFD6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRSTKVIHIV GCHAEGEVGD VIVGGVAPPP GETVWEQSRF IANDETLRNF
    60 70 80 90 100
    VLNKPRGGVF RHVNLLVPPK DPRAQMGFII MEPADTPPMS GSNSICVSTV
    110 120 130 140 150
    LLDSGIIAMQ EPVTHMVLEA PGGIIEVEAE CRNGKAERIS VRNVPSFADR
    160 170 180 190 200
    LDAPLDVTGL GTIMVDTAYG GDSFVIVDAA QIGMKIEPGQ ARELAEIGVK
    210 220 230 240 250
    ITKAANEQLG FRHPERDWRH ISFCQITEPV TREGDVLTGV NTVAIRPAKF
    260 270 280 290 300
    DRSPTGTGCS ARMAVLHAKG QMKAGERFIG KSVLGTEFHC RLDKVLELGG
    310 320 330 340
    KPAISPIISG RAWVTGTSQL MLDPSDPFPH GYRLSDTWPR DE
    Length:342
    Mass (Da):36,974
    Last modified:March 1, 2002 - v1
    Checksum:iFB6E5E9208EF98DC
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE008917 Genomic DNA. Translation: AAL52767.1.
    PIRiAD3450.
    RefSeqiWP_004682925.1. NZ_GG703778.1.

    Genome annotation databases

    EnsemblBacteriaiAAL52767; AAL52767; BMEI1586.
    KEGGibme:BMEI1586.
    PATRICi17796763. VBIBruMel146950_0201.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE008917 Genomic DNA. Translation: AAL52767.1.
    PIRiAD3450.
    RefSeqiWP_004682925.1. NZ_GG703778.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TM0X-ray2.80A/B1-342[»]
    ProteinModelPortaliQ8YFD6.
    SMRiQ8YFD6. Positions 1-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224914.BAWG_0638.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL52767; AAL52767; BMEI1586.
    KEGGibme:BMEI1586.
    PATRICi17796763. VBIBruMel146950_0201.

    Phylogenomic databases

    eggNOGiENOG4105CTU. Bacteria.
    COG3938. LUCA.
    HOGENOMiHOG000084336.
    KOiK01777.
    OMAiWITGIHQ.
    OrthoDBiEOG6SNDV3.

    Miscellaneous databases

    EvolutionaryTraceiQ8YFD6.

    Family and domain databases

    InterProiIPR008794. Pro_racemase_fam.
    [Graphical view]
    PfamiPF05544. Pro_racemase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF029792. Pro_racemase. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 16M / ATCC 23456 / NCTC 10094.
    2. "Molecular and structural discrimination of proline racemase and hydroxyproline-2-epimerase from nosocomial and bacterial pathogens."
      Goytia M., Chamond N., Cosson A., Coatnoan N., Hermant D., Berneman A., Minoprio P.
      PLoS ONE 2:E885-E885(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: LACK OF ENZYMATIC ACTIVITY AS PROLINE RACEMASE AND HYDROXYPROLINE 2-EPIMERASE.
      Strain: 16M / ATCC 23456 / NCTC 10094.
    3. "Prediction and characterization of enzymatic activities guided by sequence similarity and genome neighborhood networks."
      Zhao S., Sakai A., Zhang X., Vetting M.W., Kumar R., Hillerich B., San Francisco B., Solbiati J., Steves A., Brown S., Akiva E., Barber A., Seidel R.D., Babbitt P.C., Almo S.C., Gerlt J.A., Jacobson M.P.
      Elife 3:0-0(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

    Entry informationi

    Entry nameiY1586_BRUME
    AccessioniPrimary (citable) accession number: Q8YFD6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 25, 2008
    Last sequence update: March 1, 2002
    Last modified: May 11, 2016
    This is version 78 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

    Documents

    1. Brucella melitensis
      Brucella melitensis (strain 16M): entries and gene names
    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.