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P45548 (PHP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphotriesterase homology protein
Gene names
Name:php
Synonyms:yhfV
Ordered Locus Names:b3379, JW3342
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Its real enzymatic activity is not yet known. It was tested for general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities with the following substrates: P-nitrophenyl acetate, L-alanine nitroanilide, P-nitrophenyl sulfate, bis(P-nitrophenyl) phosphate, paraoxon, and P-nitrophenyl phosphate. No enzymatic activity was detected with any of these nonspecific substrates.

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Monomer.

Sequence similarities

Belongs to the phosphotriesterase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

groLP0A6F51EBI-1123441,EBI-543750

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 292292Phosphotriesterase homology protein
PRO_0000205362

Sites

Metal binding121Zinc 1
Metal binding141Zinc 1
Metal binding1251Zinc 1
Metal binding1251Zinc 2
Metal binding1581Zinc 2
Metal binding1861Zinc 2
Metal binding2431Zinc 1

Secondary structure

............................................................. 292
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P45548 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 1480C6858E5E8230

FASTA29232,915
        10         20         30         40         50         60 
MSFDPTGYTL AHEHLHIDLS GFKNNVDCRL DQYAFICQEM NDLMTRGVRN VIEMTNRYMG 

        70         80         90        100        110        120 
RNAQFMLDVM RETGINVVAC TGYYQDAFFP EHVATRSVQE LAQEMVDEIE QGIDGTELKA 

       130        140        150        160        170        180 
GIIAEIGTSE GKITPLEEKV FIAAALAHNQ TGRPISTHTS FSTMGLEQLA LLQAHGVDLS 

       190        200        210        220        230        240 
RVTVGHCDLK DNLDNILKMI DLGAYVQFDT IGKNSYYPDE KRIAMLHALR DRGLLNRVML 

       250        260        270        280        290 
SMDITRRSHL KANGGYGYDY LLTTFIPQLR QSGFSQADVD VMLRENPSQF FQ 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family."
Buchbinder J.L., Stephenson R.C., Dresser M.J., Pitera J.W., Scanlan T.S., Fletterick R.J.
Biochemistry 37:5096-5106(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), PARTIAL PROTEIN SEQUENCE.
[4]Erratum
Buchbinder J.L., Stephenson R.C., Dresser M.J., Pitera J.W., Scanlan T.S., Fletterick R.J.
Biochemistry 37:10860-10860(1998) [PubMed] [Europe PMC] [Abstract]

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18997 Genomic DNA. Translation: AAA58176.1.
U00096 Genomic DNA. Translation: AAC76404.1.
AP009048 Genomic DNA. Translation: BAE77912.1.
PIRF65132.
RefSeqNP_417838.1. NC_000913.2.
YP_492053.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BF6X-ray1.70A/B2-292[»]
ProteinModelPortalP45548.
SMRP45548. Positions 2-292.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10504N.
IntActP45548. 2 interactions.
STRING511145.b3379.

Proteomic databases

PaxDbP45548.
PRIDEP45548.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76404; AAC76404; b3379.
BAE77912; BAE77912; BAE77912.
GeneID12931770.
947891.
KEGGecj:Y75_p3797.
eco:b3379.
PATRIC32122190. VBIEscCol129921_3472.

Organism-specific databases

EchoBASEEB2753.
EcoGeneEG12917. php.

Phylogenomic databases

eggNOGCOG1735.
HOGENOMHOG000081700.
KOK07048.
OMAVIGHCDL.
ProtClustDBPRK09875.

Enzyme and pathway databases

BioCycEcoCyc:G7731-MONOMER.
ECOL316407:JW3342-MONOMER.

Gene expression databases

GenevestigatorP45548.

Family and domain databases

InterProIPR017947. AryldialkylPase_Zn-BS.
IPR001559. Aryldialkylphosphatase.
IPR027280. Php.
[Graphical view]
PANTHERPTHR10819. PTHR10819. 1 hit.
PfamPF02126. PTE. 1 hit.
[Graphical view]
PIRSFPIRSF016839. PhP. 1 hit.
PROSITEPS01322. PHOSPHOTRIESTERASE_1. 1 hit.
PS51347. PHOSPHOTRIESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP45548.

Entry information

Entry namePHP_ECOLI
AccessionPrimary (citable) accession number: P45548
Secondary accession number(s): Q2M744
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families