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Protein

Arylesterase

Gene
N/A
Organism
Pseudomonas fluorescens
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional enzyme, capable of both ester hydrolysis and halogenation. Has a low bromoperoxidase activity. Acts on many phenolic esters.

Catalytic activityi

A phenyl acetate + H2O = a phenol + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei95 – 951
Active sitei223 – 2231
Active sitei252 – 2521

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase, Peroxidase

Protein family/group databases

ESTHERipsefl-este. Haloperoxidase.
PeroxiBasei5910. PfHalNPrx03_SIKWI.

Names & Taxonomyi

Protein namesi
Recommended name:
Arylesterase (EC:3.1.1.2)
Alternative name(s):
Aryl-ester hydrolase
PFE
Putative bromoperoxidase (EC:1.-.-.-)
OrganismiPseudomonas fluorescens
Taxonomic identifieri294 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 272271ArylesterasePRO_0000207059Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
272
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Beta strandi11 – 2616Combined sources
Helixi33 – 364Combined sources
Helixi37 – 448Combined sources
Turni45 – 473Combined sources
Beta strandi49 – 535Combined sources
Helixi70 – 8415Combined sources
Beta strandi88 – 947Combined sources
Helixi97 – 10812Combined sources
Beta strandi113 – 1208Combined sources
Helixi138 – 16427Combined sources
Helixi166 – 1683Combined sources
Helixi174 – 18613Combined sources
Helixi189 – 20113Combined sources
Helixi205 – 2084Combined sources
Beta strandi215 – 2206Combined sources
Beta strandi224 – 2263Combined sources
Helixi228 – 2303Combined sources
Helixi232 – 2387Combined sources
Beta strandi243 – 2475Combined sources
Helixi254 – 2574Combined sources
Helixi259 – 27012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VA4X-ray1.80A/B/C/D/E/F2-272[»]
3HEAX-ray1.90A/B/C/D/E/F2-272[»]
3HI4X-ray2.25A/B/C/D/E/F2-272[»]
3IA2X-ray1.65A/B/C/D/E/F2-272[»]
3T4UX-ray2.02A/B/C/D/E/F2-272[»]
3T52X-ray2.00A/B/C/D/E/F2-272[»]
ProteinModelPortaliP22862.
SMRiP22862. Positions 2-272.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22862.

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22862-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTFVAKDGT QIYFKDWGSG KPVLFSHGWL LDADMWEYQM EYLSSRGYRT
60 70 80 90 100
IAFDRRGFGR SDQPWTGNDY DTFADDIAQL IEHLDLKEVT LVGFSMGGGD
110 120 130 140 150
VARYIARHGS ARVAGLVLLG AVTPLFGQKP DYPQGVPLDV FARFKTELLK
160 170 180 190 200
DRAQFISDFN APFYGINKGQ VVSQGVQTQT LQIALLASLK ATVDCVTAFA
210 220 230 240 250
ETDFRPDMAK IDVPTLVIHG DGDQIVPFET TGKVAAELIK GAELKVYKDA
260 270
PHGFAVTHAQ QLNEDLLAFL KR
Length:272
Mass (Da):30,092
Last modified:January 23, 2007 - v4
Checksum:i92E3D1ADBDBE0135
GO

Sequence cautioni

The sequence BAA02052 differs from that shown. Reason: Frameshift at several positions. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12484 Genomic DNA. Translation: BAA02052.1. Frameshift.
U12537 Genomic DNA. Translation: AAB60168.1.
PIRiJQ0606.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12484 Genomic DNA. Translation: BAA02052.1. Frameshift.
U12537 Genomic DNA. Translation: AAB60168.1.
PIRiJQ0606.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VA4X-ray1.80A/B/C/D/E/F2-272[»]
3HEAX-ray1.90A/B/C/D/E/F2-272[»]
3HI4X-ray2.25A/B/C/D/E/F2-272[»]
3IA2X-ray1.65A/B/C/D/E/F2-272[»]
3T4UX-ray2.02A/B/C/D/E/F2-272[»]
3T52X-ray2.00A/B/C/D/E/F2-272[»]
ProteinModelPortaliP22862.
SMRiP22862. Positions 2-272.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERipsefl-este. Haloperoxidase.
PeroxiBasei5910. PfHalNPrx03_SIKWI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP22862.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiESTE_PSEFL
AccessioniPrimary (citable) accession number: P22862
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 87 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.