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O31156

- PHNX_BACCE

UniProt

O31156 - PHNX_BACCE

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Protein

Phosphonoacetaldehyde hydrolase

Gene

phnX

Organism
Bacillus cereus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in phosphonate degradation.

Catalytic activityi

Phosphonoacetaldehyde + H2O = acetaldehyde + phosphate.

Cofactori

Mg2+Note: Binds 1 Mg(2+) ion per subunit.

Kineticsi

  1. KM=33 µM for phosphonoacetaldehyde (at pH 7.0, 25 degrees Celsius)

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei9 – 91Nucleophile
Metal bindingi9 – 91Magnesium
Metal bindingi11 – 111Magnesium; via carbonyl oxygen
Active sitei50 – 501Schiff-base intermediate with substrate
Metal bindingi183 – 1831Magnesium

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. phosphonoacetaldehyde hydrolase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. organic phosphonate catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Schiff base

Enzyme and pathway databases

SABIO-RKO31156.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphonoacetaldehyde hydrolase (EC:3.11.1.1)
Short name:
Phosphonatase
Alternative name(s):
Phosphonoacetaldehyde phosphonohydrolase
Gene namesi
Name:phnX
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91D → A: Loss of enzymatic activity. 2 Publications
Mutagenesisi9 – 91D → E: Kcat/KM decreases 30000-fold. 2 Publications
Mutagenesisi19 – 191C → A or S: Kcat/KM decreases 10-100-fold. 1 Publication
Mutagenesisi46 – 461M → L: Kcat/KM decreases 17000-fold. 1 Publication
Mutagenesisi47 – 471G → A: Kcat/KM decreases 10000-fold. 1 Publication
Mutagenesisi47 – 471G → P or V: Loss of enzymatic activity. 1 Publication
Mutagenesisi50 – 501K → R: Loss of enzymatic activity. 1 Publication
Mutagenesisi53 – 531H → A: Kcat/KM decreases 1000-fold. 2 Publications
Mutagenesisi53 – 531H → Q: Kcat/KM decreases 250-fold. 2 Publications
Mutagenesisi125 – 1251Y → A: Kcat/KM decreases 230-fold. 1 Publication
Mutagenesisi125 – 1251Y → F: Kcat/KM decreases 10-fold. 1 Publication
Mutagenesisi183 – 1831D → A: Loss of enzymatic activity. 1 Publication
Mutagenesisi187 – 1871D → A: Kcat/KM decreases 10000-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Phosphonoacetaldehyde hydrolasePRO_0000284575Add
BLAST

Interactioni

Subunit structurei

Homodimer.4 Publications

Structurei

Secondary structure

1
264
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Turni11 – 133Combined sources
Beta strandi14 – 163Combined sources
Helixi23 – 319Combined sources
Turni32 – 343Combined sources
Helixi39 – 435Combined sources
Turni44 – 474Combined sources
Helixi50 – 5910Combined sources
Helixi61 – 7111Combined sources
Helixi77 – 9418Combined sources
Helixi95 – 984Combined sources
Helixi105 – 11410Combined sources
Beta strandi118 – 1225Combined sources
Helixi127 – 13913Combined sources
Beta strandi145 – 1473Combined sources
Helixi150 – 1523Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi157 – 1604Combined sources
Helixi161 – 17010Combined sources
Helixi175 – 1773Combined sources
Beta strandi178 – 1847Combined sources
Helixi185 – 1939Combined sources
Beta strandi196 – 2016Combined sources
Turni206 – 2083Combined sources
Helixi212 – 2176Combined sources
Helixi220 – 23617Combined sources
Beta strandi240 – 2456Combined sources
Helixi246 – 2483Combined sources
Helixi249 – 2568Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliO31156.
SMRiO31156. Positions 2-257.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO31156.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 2 hits.
HAMAPiMF_01375. PhnX.
InterProiIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR023198. PGP_dom2.
IPR006323. Phosphonoacetald_hydro.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01549. HAD-SF-IA-v1. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR01422. phosphonatase. 1 hit.

Sequencei

Sequence statusi: Complete.

O31156-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIEAVIFDW AGTTVDYGCF APLEVFMEIF HKRGVAITAE EARKPMGLLK
60 70 80 90 100
IDHVRALTEM PRIASEWNRV FRQLPTEADI QEMYEEFEEI LFAILPRYAS
110 120 130 140 150
PINGVKEVIA SLRERGIKIG STTGYTREMM DIVAKEAALQ GYKPDFLVTP
160 170 180 190 200
DDVPAGRPYP WMCYKNAMEL GVYPMNHMIK VGDTVSDMKE GRNAGMWTVG
210 220 230 240 250
VILGSSELGL TEEEVENMDS VELREKIEVV RNRFVENGAH FTIETMQELE
260
SVMEHIEKQE LIIS
Length:264
Mass (Da):30,060
Last modified:April 17, 2007 - v3
Checksum:i59A99D2BBED760AD
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030979 Genomic DNA. Translation: AAB86434.2. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030979 Genomic DNA. Translation: AAB86434.2 . Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FEZ X-ray 3.00 A/B/C/D 2-257 [» ]
1RDF X-ray 2.80 A/B/C/D/E/F 1-264 [» ]
1RQL X-ray 2.40 A/B 1-264 [» ]
1RQN X-ray 2.80 A/B 1-264 [» ]
1SWV X-ray 2.30 A/B 1-264 [» ]
1SWW X-ray 2.30 A/B 1-264 [» ]
2IOF X-ray 2.50 A/K 1-264 [» ]
2IOH X-ray 2.90 A/B/C/D 1-264 [» ]
ProteinModelPortali O31156.
SMRi O31156. Positions 2-257.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK O31156.

Miscellaneous databases

EvolutionaryTracei O31156.

Family and domain databases

Gene3Di 1.10.150.240. 1 hit.
3.40.50.1000. 2 hits.
HAMAPi MF_01375. PhnX.
InterProi IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR023198. PGP_dom2.
IPR006323. Phosphonoacetald_hydro.
[Graphical view ]
Pfami PF13419. HAD_2. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01549. HAD-SF-IA-v1. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR01422. phosphonatase. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPHNX_BACCE
AccessioniPrimary (citable) accession number: O31156
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: November 26, 2014
This is version 70 of the entry and version 3 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
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3