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Q9KX40

- ESTB_BURGA

UniProt

Q9KX40 - ESTB_BURGA

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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 – 3116Combined sources
Beta strandi36 – 449Combined sources
Beta strandi47 – 5812Combined sources
Turni59 – 624Combined sources
Beta strandi70 – 723Combined sources
Helixi74 – 763Combined sources
Helixi77 – 9014Combined sources
Helixi100 – 1023Combined sources
Helixi121 – 1255Combined sources
Helixi134 – 1374Combined sources
Helixi142 – 1465Combined sources
Beta strandi151 – 1533Combined sources
Helixi159 – 16810Combined sources
Helixi184 – 19613Combined sources
Helixi200 – 2078Combined sources
Helixi209 – 2124Combined sources
Helixi224 – 2263Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi245 – 2484Combined sources
Beta strandi255 – 2595Combined sources
Helixi261 – 2655Combined sources
Turni273 – 2753Combined sources
Helixi281 – 29313Combined sources
Beta strandi295 – 2984Combined sources
Helixi300 – 3078Combined sources
Helixi313 – 3153Combined sources
Beta strandi322 – 3243Combined sources
Beta strandi326 – 3327Combined sources
Helixi334 – 3374Combined sources
Beta strandi346 – 3505Combined sources
Turni351 – 3533Combined sources
Beta strandi354 – 3596Combined sources
Helixi360 – 3623Combined sources
Beta strandi364 – 37310Combined sources
Helixi375 – 3784Combined sources
Helixi380 – 38910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MTAASLDPTA FSLDAASLAA RLDAVFDQAL RERRLVGAVA IVARHGEILY
60 70 80 90 100
RRAQGLADRE AGRPMREDTL FRLASVTKPI VALAVLRLVA RGELALDAPV
110 120 130 140 150
TRWLPEFRPR LADGSEPLVT IHHLLTHTSG LGYWLLEGAG SVYDRLGISD
160 170 180 190 200
GIDLRDFDLD ENLRRLASAP LSFAPGSGWQ YSLALDVLGA VVERATGQPL
210 220 230 240 250
AAAVDALVAQ PLGMRDCGFV SAEPERFAVP YHDGQPEPVR MRDGIEVPLP
260 270 280 290 300
EGHGAAVRFA PSRVFEPGAY PSGGAGMYGS ADDVLRALEA IRANPGFLPE
310 320 330 340 350
TLADAARRDQ AGVGAETRGP GWGFGYLSAV LDDPAAAGTP QHAGTLQWGG
360 370 380 390
VYGHSWFVDR ALGLSVLLLT NTAYEGMSGP LTIALRDAVY AR
Length:392
Mass (Da):41,707
Last modified:October 1, 2000 - v1
Checksum:i60EC4764C3C499B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33634 Genomic DNA. Translation: AAF59826.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33634 Genomic DNA. Translation: AAF59826.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 55 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