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Q9KX40

- ESTB_BURGA

UniProt

Q9KX40 - ESTB_BURGA

Protein

Esterase EstB

Gene

estB

Organism
Burkholderia gladioli (Pseudomonas marginata) (Phytomonas marginata)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Acts on short-chain (C4-C6) fatty acid esters and triglycerides, including tertiary alcohol esters. Activity on p-nitrophenyl esters is generally higher than on o-nitrophenyl esters. Lacks beta-lactamase activity; it hydrolyzes the ester bond of cephalosporin substrates but there is no opening of the beta-lactam ring observed.

    Enzyme regulationi

    Strongly inhibited by eserin, NaF, HgCl2, SDS and Triton X-100.

    Kineticsi

    Esterase, not beta-lactamase activity of the enzyme.

    1. KM=1.3 mM for cephalosporin C
    2. KM=1.0 mM for 7-amino cephalosporinic acid

    Vmax=79 µmol/min/mg enzyme for cephalosporin C

    Vmax=77 µmol/min/mg enzyme for 7-amino cephalosporinic acid

    pH dependencei

    Optimum pH is 7.0.

    Temperature dependencei

    Optimum temperature is 43 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei75 – 751Acyl-ester intermediate

    GO - Molecular functioni

    1. hydrolase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Protein family/group databases

    MEROPSiS12.950.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Esterase EstB (EC:3.1.1.-)
    Gene namesi
    Name:estB
    OrganismiBurkholderia gladioli (Pseudomonas marginata) (Phytomonas marginata)
    Taxonomic identifieri28095 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Biotechnological usei

    Directed evolutionary mutagenesis has created an enzyme with 40-fold higher stability in organic solvents. It contains the following changes: Leu-8, Ser-132, Arg-134, Cys-155, Gly-251, Val-311 and Lys-316 and could have applications in antibiotic synthesis (PubMed:17137667).1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi75 – 751S → A: Complete loss of esterase activity. 1 Publication
    Mutagenesisi149 – 1491S → A: Retains 30% esterase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 392392Esterase EstBPRO_0000370699Add
    BLAST

    Structurei

    Secondary structure

    1
    392
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 3116
    Beta strandi36 – 449
    Beta strandi47 – 5812
    Turni59 – 624
    Beta strandi70 – 723
    Helixi74 – 763
    Helixi77 – 9014
    Helixi100 – 1023
    Helixi121 – 1255
    Helixi134 – 1374
    Helixi142 – 1465
    Beta strandi151 – 1533
    Helixi159 – 16810
    Helixi184 – 19613
    Helixi200 – 2078
    Helixi209 – 2124
    Helixi224 – 2263
    Beta strandi235 – 2373
    Beta strandi245 – 2484
    Beta strandi255 – 2595
    Helixi261 – 2655
    Turni273 – 2753
    Helixi281 – 29313
    Beta strandi295 – 2984
    Helixi300 – 3078
    Helixi313 – 3153
    Beta strandi322 – 3243
    Beta strandi326 – 3327
    Helixi334 – 3374
    Beta strandi346 – 3505
    Turni351 – 3533
    Beta strandi354 – 3596
    Helixi360 – 3623
    Beta strandi364 – 37310
    Helixi375 – 3784
    Helixi380 – 38910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CI8X-ray2.00A/B1-392[»]
    1CI9X-ray1.80A/B1-392[»]
    ProteinModelPortaliQ9KX40.
    SMRiQ9KX40. Positions 15-391.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9KX40.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the class-A beta-lactamase family.Curated

    Family and domain databases

    Gene3Di3.40.710.10. 1 hit.
    InterProiIPR001466. Beta-lactam-related.
    IPR012338. Beta-lactam/transpept-like.
    IPR023650. Beta-lactam_class-A_AS.
    [Graphical view]
    PfamiPF00144. Beta-lactamase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56601. SSF56601. 1 hit.
    PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9KX40-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAASLDPTA FSLDAASLAA RLDAVFDQAL RERRLVGAVA IVARHGEILY    50
    RRAQGLADRE AGRPMREDTL FRLASVTKPI VALAVLRLVA RGELALDAPV 100
    TRWLPEFRPR LADGSEPLVT IHHLLTHTSG LGYWLLEGAG SVYDRLGISD 150
    GIDLRDFDLD ENLRRLASAP LSFAPGSGWQ YSLALDVLGA VVERATGQPL 200
    AAAVDALVAQ PLGMRDCGFV SAEPERFAVP YHDGQPEPVR MRDGIEVPLP 250
    EGHGAAVRFA PSRVFEPGAY PSGGAGMYGS ADDVLRALEA IRANPGFLPE 300
    TLADAARRDQ AGVGAETRGP GWGFGYLSAV LDDPAAAGTP QHAGTLQWGG 350
    VYGHSWFVDR ALGLSVLLLT NTAYEGMSGP LTIALRDAVY AR 392
    Length:392
    Mass (Da):41,707
    Last modified:October 1, 2000 - v1
    Checksum:i60EC4764C3C499B7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33634 Genomic DNA. Translation: AAF59826.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33634 Genomic DNA. Translation: AAF59826.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CI8 X-ray 2.00 A/B 1-392 [» ]
    1CI9 X-ray 1.80 A/B 1-392 [» ]
    ProteinModelPortali Q9KX40.
    SMRi Q9KX40. Positions 15-391.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S12.950.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q9KX40.

    Family and domain databases

    Gene3Di 3.40.710.10. 1 hit.
    InterProi IPR001466. Beta-lactam-related.
    IPR012338. Beta-lactam/transpept-like.
    IPR023650. Beta-lactam_class-A_AS.
    [Graphical view ]
    Pfami PF00144. Beta-lactamase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56601. SSF56601. 1 hit.
    PROSITEi PS00146. BETA_LACTAMASE_A. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel esterase from Burkholderia gladioli which shows high deacetylation activity on cephalosporins is related to beta-lactamases and DD-peptidases."
      Petersen E.I., Valinger G., Soelkner B., Stubenrauch G., Schwab H.
      J. Biotechnol. 89:11-25(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION AS AN ESTERASE, MUTAGENESIS OF SER-75 AND SER-149, ABSENCE OF BETA-LACTAMASE ACTIVITY, PROBABLE SUBCELLULAR LOCATION.
      Strain: ATCC 10248 / NCPPB 1891.
    2. "Stability and activity improvement of cephalosporin esterase EstB from Burkholderia gladioli by directed evolution and structural interpretation of muteins."
      Valinger G., Hermann M., Wagner U.G., Schwab H.
      J. Biotechnol. 129:98-108(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: RANDOM MUTAGENESIS TO CREATE MORE STABLE ORGANIC SOLVENT-RESISTANT ENZYME.
      Strain: ATCC 10248 / NCPPB 1891.
    3. "Inverting enantioselectivity of Burkholderia gladioli esterase EstB by directed and designed evolution."
      Ivancic M., Valinger G., Gruber K., Schwab H.
      J. Biotechnol. 129:109-122(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: RANDOM MUTAGENESIS TO ALTER ENANTIOSELECTIVITY.
      Strain: ATCC 10248 / NCPPB 1891.
    4. "EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity."
      Wagner U.G., Petersen E.I., Schwab H., Kratky C.
      Protein Sci. 11:467-478(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) WITH AND WITHOUT THE INHIBITOR DIISOPROPYL-FLUOROPHOSPHATE.
      Strain: ATCC 10248 / NCPPB 1891.

    Entry informationi

    Entry nameiESTB_BURGA
    AccessioniPrimary (citable) accession number: Q9KX40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 5, 2009
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 53 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3