P22862 (ESTE_PSEFL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Arylesterase EC=3.1.1.2 Alternative name(s): Aryl-ester hydrolase PFE Putative bromoperoxidase EC=1.-.-.-
Organism	Pseudomonas fluorescens
Taxonomic identifier	294 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	272 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional enzyme, capable of both ester hydrolysis and halogenation. Has a low bromoperoxidase activity. Acts on many phenolic esters.
Catalytic activity	A phenyl acetate + H2O = a phenol + acetate.
Subunit structure	Homodimer.
Sequence caution	The sequence BAA02052.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Molecular function	Hydrolase Oxidoreductase Peroxidase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	arylesterase activity Inferred from electronic annotation. Source: EC peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 272

271

Arylesterase

PRO_0000207059

Sites

Active site

95

1

Active site

223

1

Active site

252

1

Secondary structure

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272

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Beta strand

11 – 26

16

Helix

33 – 36

4

Helix

37 – 44

8

Turn

45 – 47

3

Beta strand

49 – 53

5

Helix

70 – 84

15

Beta strand

88 – 94

7

Helix

97 – 108

12

Beta strand

113 – 120

8

Helix

138 – 164

27

Helix

166 – 168

3

Helix

174 – 186

13

Helix

189 – 201

13

Helix

205 – 210

6

Beta strand

215 – 220

6

Beta strand

224 – 226

3

Helix

228 – 230

3

Helix

232 – 238

7

Beta strand

243 – 247

5

Helix

254 – 257

4

Helix

259 – 270

12

Sequences

	Sequence		Length	Mass (Da)
	P22862 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 92E3D1ADBDBE0135	FASTA	272	30,092
	10 20 30 40 50 60 MSTFVAKDGT QIYFKDWGSG KPVLFSHGWL LDADMWEYQM EYLSSRGYRT IAFDRRGFGR 70 80 90 100 110 120 SDQPWTGNDY DTFADDIAQL IEHLDLKEVT LVGFSMGGGD VARYIARHGS ARVAGLVLLG 130 140 150 160 170 180 AVTPLFGQKP DYPQGVPLDV FARFKTELLK DRAQFISDFN APFYGINKGQ VVSQGVQTQT 190 200 210 220 230 240 LQIALLASLK ATVDCVTAFA ETDFRPDMAK IDVPTLVIHG DGDQIVPFET TGKVAAELIK 250 260 270 GAELKVYKDA PHGFAVTHAQ QLNEDLLAFL KR

References

[1]	"Cloning and nucleotide sequence of an esterase gene from Pseudomonas fluorescens and expression of the gene in Escherichia coli." Choi K.D., Jeohn G.H., Rhee J.S., Yoo O.J. Agric. Biol. Chem. 54:2039-2045(1990) [PubMed: 1368608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18. Strain: SIK WI.
[2]	"A bacterial esterase is homologous with non-haem haloperoxidases and displays brominating activity." Pelletier I., Altenbuchner J. Microbiology 141:459-468(1995) [PubMed: 7704276] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SIK WI.
[3]	"Structure of an aryl esterase from Pseudomonas fluorescens." Cheeseman J.D., Tocilj A., Park S., Schrag J.D., Kazlauskas R.J. Acta Crystallogr. D 60:1237-1243(2004) [PubMed: 15213385] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D12484 Genomic DNA. Translation: BAA02052.1. Frameshift.
U12537 Genomic DNA. Translation: AAB60168.1.

PIR

JQ0606.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VA4	X-ray	1.80	A/B/C/D/E/F	2-272	[»]
3HEA	X-ray	1.90	A/B/C/D/E/F	2-272	[»]
3HI4	X-ray	2.25	A/B/C/D/E/F	2-272	[»]
3IA2	X-ray	1.65	A/B/C/D/E/F	2-272	[»]

ProteinModelPortal

P22862.

SMR

P22862. Positions 2-272.

ModBase

Search...

Protein family/group databases

PeroxiBase

5910. PfHalNPrx03_SIKWI.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]

PRINTS

PR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.

ProtoNet

Search...

Entry information

Entry name

ESTE_PSEFL

Accession

Primary (citable) accession number: P22862

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	January 23, 2007
Last modified:	July 27, 2011
This is version 73 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program