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Protein

Esterase EstB

Gene

estB

Organism
Burkholderia gladioli (Pseudomonas marginata) (Phytomonas marginata)
Status
Reviewed-Annotation score: 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
  1. Vmax=79 µmol/min/mg enzyme for cephalosporin C
  2. 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)DescriptionActionsGraphical viewLength
Active sitei75Acyl-ester intermediate1

GO - Molecular functioni

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

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Mutagenesisi75S → A: Complete loss of esterase activity. 1 Publication1
Mutagenesisi149S → A: Retains 30% esterase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003706991 – 392Esterase EstBAdd BLAST392

Interactioni

Protein-protein interaction databases

STRINGi999541.bgla_2g14490.

Structurei

Secondary structure

1392
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 31Combined sources16
Beta strandi36 – 44Combined sources9
Beta strandi47 – 58Combined sources12
Turni59 – 62Combined sources4
Beta strandi70 – 72Combined sources3
Helixi74 – 76Combined sources3
Helixi77 – 90Combined sources14
Helixi100 – 102Combined sources3
Helixi121 – 125Combined sources5
Helixi134 – 137Combined sources4
Helixi142 – 146Combined sources5
Beta strandi151 – 153Combined sources3
Helixi159 – 168Combined sources10
Helixi184 – 196Combined sources13
Helixi200 – 207Combined sources8
Helixi209 – 212Combined sources4
Helixi224 – 226Combined sources3
Beta strandi235 – 237Combined sources3
Beta strandi245 – 248Combined sources4
Beta strandi255 – 259Combined sources5
Helixi261 – 265Combined sources5
Turni273 – 275Combined sources3
Helixi281 – 293Combined sources13
Beta strandi295 – 298Combined sources4
Helixi300 – 307Combined sources8
Helixi313 – 315Combined sources3
Beta strandi322 – 324Combined sources3
Beta strandi326 – 332Combined sources7
Helixi334 – 337Combined sources4
Beta strandi346 – 350Combined sources5
Turni351 – 353Combined sources3
Beta strandi354 – 359Combined sources6
Helixi360 – 362Combined sources3
Beta strandi364 – 373Combined sources10
Helixi375 – 378Combined sources4
Helixi380 – 389Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CI8X-ray2.00A/B1-392[»]
1CI9X-ray1.80A/B1-392[»]
ProteinModelPortaliQ9KX40.
SMRiQ9KX40.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9KX40.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107S1E. Bacteria.
COG1680. LUCA.

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.
RefSeqiWP_036056391.1. NZ_KN150850.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33634 Genomic DNA. Translation: AAF59826.1.
RefSeqiWP_036056391.1. NZ_KN150850.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CI8X-ray2.00A/B1-392[»]
1CI9X-ray1.80A/B1-392[»]
ProteinModelPortaliQ9KX40.
SMRiQ9KX40.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi999541.bgla_2g14490.

Protein family/group databases

MEROPSiS12.950.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107S1E. Bacteria.
COG1680. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ9KX40.

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]
ProtoNetiSearch...

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 2, 2016
This is version 63 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

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.