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O31156 (PHNX_BACCE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphonoacetaldehyde hydrolase

Short name=Phosphonatase
EC=3.11.1.1
Alternative name(s):
Phosphonoacetaldehyde phosphonohydrolase
Gene names
Name:phnX
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in phosphonate degradation. HAMAP-Rule MF_01375

Catalytic activity

Phosphonoacetaldehyde + H2O = acetaldehyde + phosphate. HAMAP-Rule MF_01375

Cofactor

Binds 1 Mg2+ ion per subunit.

Subunit structure

Homodimer. Ref.3

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. PhnX family.

Biophysicochemical properties

Kinetic parameters:

KM=33 µM for phosphonoacetaldehyde (at pH 7.0, 25 degrees Celsius) HAMAP-Rule MF_01375

Sequence caution

The sequence AAB86434.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Phosphonoacetaldehyde hydrolase HAMAP-Rule MF_01375
PRO_0000284575

Sites

Active site91Nucleophile
Active site501Schiff-base intermediate with substrate
Metal binding91Magnesium
Metal binding111Magnesium; via carbonyl oxygen
Metal binding1831Magnesium

Experimental info

Mutagenesis91D → A: Loss of enzymatic activity. Ref.4 Ref.7
Mutagenesis91D → E: Kcat/KM decreases 30000-fold. Ref.4 Ref.7
Mutagenesis191C → A or S: Kcat/KM decreases 10-100-fold. Ref.5
Mutagenesis461M → L: Kcat/KM decreases 17000-fold. Ref.5
Mutagenesis471G → A: Kcat/KM decreases 10000-fold. Ref.6
Mutagenesis471G → P or V: Loss of enzymatic activity. Ref.6
Mutagenesis501K → R: Loss of enzymatic activity. Ref.6
Mutagenesis531H → A: Kcat/KM decreases 1000-fold. Ref.5 Ref.8
Mutagenesis531H → Q: Kcat/KM decreases 250-fold. Ref.5 Ref.8
Mutagenesis1251Y → A: Kcat/KM decreases 230-fold. Ref.5
Mutagenesis1251Y → F: Kcat/KM decreases 10-fold. Ref.5
Mutagenesis1831D → A: Loss of enzymatic activity. Ref.7
Mutagenesis1871D → A: Kcat/KM decreases 10000-fold. Ref.7

Secondary structure

................................................. 264
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O31156 [UniParc].

Last modified April 17, 2007. Version 3.
Checksum: 59A99D2BBED760AD

FASTA26430,060
        10         20         30         40         50         60 
MKIEAVIFDW AGTTVDYGCF APLEVFMEIF HKRGVAITAE EARKPMGLLK IDHVRALTEM 

        70         80         90        100        110        120 
PRIASEWNRV FRQLPTEADI QEMYEEFEEI LFAILPRYAS PINGVKEVIA SLRERGIKIG 

       130        140        150        160        170        180 
STTGYTREMM DIVAKEAALQ GYKPDFLVTP DDVPAGRPYP WMCYKNAMEL GVYPMNHMIK 

       190        200        210        220        230        240 
VGDTVSDMKE GRNAGMWTVG VILGSSELGL TEEEVENMDS VELREKIEVV RNRFVENGAH 

       250        260 
FTIETMQELE SVMEHIEKQE LIIS 

« Hide

References

[1]"Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis."
Baker A.S., Ciocci M.J., Metcalf W.W., Kim J., Babbitt P.C., Wanner B.L., Martin B.M., Dunaway-Mariano D.
Biochemistry 37:9305-9315(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17 AND 35-55, REACTION MECHANISM, BIOPHYSICAL CHARACTERIZATION.
Strain: ATCC 43881 / AI-2.
[2]"Investigation of the substrate binding and catalytic groups of the P-C bond cleaving enzyme, phosphonoacetaldehyde hydrolase."
Olsen D.B., Hepburn T.W., Lee S.-L., Martin B.M., Mariano P.S., Dunaway-Mariano D.
Arch. Biochem. Biophys. 296:144-151(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 34-55, SCHIFF BASE, REACTION MECHANISM.
Strain: ATCC 43881 / AI-2.
[3]"Crystallization and preliminary crystallographic analysis of phosphonoacetaldehyde hydrolase."
Morais M.C., Baker A.S., Dunaway-Mariano D., Allen K.N.
Acta Crystallogr. D 56:206-209(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, PRELIMINARY CRYSTALLOGRAPHY.
Strain: ATCC 43881 / AI-2.
[4]"The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily."
Morais M.C., Zhang W., Baker A.S., Zhang G., Dunaway-Mariano D., Allen K.N.
Biochemistry 39:10385-10396(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-260 IN COMPLEX WITH THE PHOSPHATE ANALOG TUNGSTATE, BINDING OF MAGNESIUM, MUTAGENESIS OF ASP-9.
Strain: ATCC 43881 / AI-2.
[5]"X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis."
Morais M.C., Zhang G., Zhang W., Olsen D.B., Dunaway-Mariano D., Allen K.N.
J. Biol. Chem. 279:9353-9361(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH MG(2+) AND WITH MG(2+) PLUS VINYLSULFONATE, MUTAGENESIS OF CYS-19; MET-46; HIS-53 AND TYR-125.
Strain: ATCC 43881 / AI-2.
[6]"Analysis of the substrate specificity loop of the HAD superfamily cap domain."
Lahiri S.D., Zhang G., Dai J., Dunaway-Mariano D., Allen K.N.
Biochemistry 43:2812-2820(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT PRO-47, MUTAGENESIS OF GLY-47 AND LYS-50.
Strain: ATCC 43881 / AI-2.
[7]"Investigation of metal ion binding in phosphonoacetaldehyde hydrolase identifies sequence markers for metal-activated enzymes of the HAD enzyme superfamily."
Zhang G., Morais M.C., Dai J., Zhang W., Dunaway-Mariano D., Allen K.N.
Biochemistry 43:4990-4997(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-9 IN COMPLEX WITH MG(2+) AND WITH MG(2+) PLUS PHOSPHONOACETALDEHYDE, MUTAGENESIS OF ASP-9; ASP-183 AND ASP-187.
Strain: ATCC 43881 / AI-2.
[8]"Diversification of function in the haloacid dehalogenase enzyme superfamily: the role of the cap domain in hydrolytic phosphorus--carbon bond cleavage."
Lahiri S.D., Zhang G., Dunaway-Mariano D., Allen K.N.
Bioorg. Chem. 34:394-409(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF MUTANT ARG-50, MUTAGENESIS OF HIS-53.
Strain: ATCC 43881 / AI-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF030979 Genomic DNA. Translation: AAB86434.2. Different initiation.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FEZX-ray3.00A/B/C/D2-257[»]
1RDFX-ray2.80A/B/C/D/E/F1-264[»]
1RQLX-ray2.40A/B1-264[»]
1RQNX-ray2.80A/B1-264[»]
1SWVX-ray2.30A/B1-264[»]
1SWWX-ray2.30A/B1-264[»]
2IOFX-ray2.50A/K1-264[»]
2IOHX-ray2.90A/B/C/D1-264[»]
ProteinModelPortalO31156.
SMRO31156. Positions 2-257.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKO31156.

Family and domain databases

Gene3D1.10.150.240. 1 hit.
3.40.50.1000. 2 hits.
HAMAPMF_01375. PhnX.
InterProIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR023198. PGP_dom2.
IPR006323. Phosphonoacetald_hydro.
[Graphical view]
PfamPF13419. HAD_2. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01549. HAD-SF-IA-v1. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR01422. phosphonatase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO31156.

Entry information

Entry namePHNX_BACCE
AccessionPrimary (citable) accession number: O31156
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: February 19, 2014
This is version 68 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references