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Protein

Phosphonoacetate hydrolase

Gene

phnA

Organism
Pseudomonas fluorescens
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Specifically hydrolyzes phosphonoacetate. Does not have activity on other organophosphonates or acetates.1 Publication

Catalytic activityi

Phosphonoacetate + H2O = acetate + phosphate.3 Publications

Cofactori

Zn2+2 PublicationsNote: Binds 2 Zn2+ ions per subunit.2 Publications

Enzyme regulationi

Completely inhibited by EDTA and 1,10-phenanthroline. Moderately inhibited by the phosphonocarboxylic acids phosphonoformate and 3-phosphonopropionate and the phosphonate herbicide glyphosate. Partially inhibited by the reducing agents sodium sulfide and dithiotheitol and the chelating agent iminodiacetate. Nonphosphonate analogs of phosphonoacetate, such as arsonoacetate, sulfonoacetate and malonate are poor inhibitors. Inorganic phosphate, acetate and the known phosphonotase inhibitor phosphite have little effect on activity. Not inhibited by the alkylphosphonic acids methylphosphonate and ethylphosphonate, or the aminoalkylphosphonates 2-aminoethylphosphonate, 3-aminopropylphosphonate and 4-aminobutylphosphonate. Fe3+, Ca2+, Mg2+ and Cs+ have no effect on activity. Activity is slightly increased by the aminoalkylphosphonates 1-aminoethylphosphonate, 1-aminobutylphosphonate, 2-amino-4-butylphosphonate. Activity is increased by Zn2+, Mn2+ and Co2+, these 3 metal ions also allow recovery of activity after EDTA treatment.2 Publications

Kineticsi

  1. KM=1.25 mM for phosphonoacetate1 Publication
  1. Vmax=1.25 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is approximately 7.8.1 Publication

Temperature dependencei

Optimum temperature is 37 degrees Celsius. Activity is rapidly lost after incubation for 30 minutes above 40 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi25 – 251Zinc 11 Publication
Metal bindingi64 – 641Zinc 11 Publication
Binding sitei64 – 641Substrate1 Publication
Metal bindingi202 – 2021Zinc 21 Publication
Binding sitei202 – 2021Substrate1 Publication
Metal bindingi206 – 2061Zinc 2; via tele nitrogen1 Publication
Metal bindingi241 – 2411Zinc 11 Publication
Metal bindingi242 – 2421Zinc 1; via tele nitrogen1 Publication
Binding sitei242 – 2421Substrate1 Publication
Metal bindingi368 – 3681Zinc 2; via tele nitrogen1 Publication
Binding sitei368 – 3681Substrate1 Publication

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • phosphonoacetate hydrolase activity Source: UniProtKB

GO - Biological processi

  • phosphonoacetate metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-202.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphonoacetate hydrolaseImported (EC:3.11.1.2)
Gene namesi
Name:phnAImported
OrganismiPseudomonas fluorescens
Taxonomic identifieri294 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 407406Phosphonoacetate hydrolase1 PublicationPRO_0000402579Add
BLAST

Expressioni

Inductioni

By phosphonoacetate.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
407
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi10 – 134Combined sources
Beta strandi19 – 235Combined sources
Helixi29 – 379Combined sources
Helixi42 – 465Combined sources
Helixi47 – 493Combined sources
Beta strandi51 – 577Combined sources
Helixi64 – 7310Combined sources
Helixi77 – 804Combined sources
Beta strandi84 – 896Combined sources
Turni90 – 934Combined sources
Beta strandi94 – 974Combined sources
Helixi101 – 1033Combined sources
Helixi109 – 1157Combined sources
Beta strandi120 – 1267Combined sources
Helixi127 – 1337Combined sources
Turni134 – 1363Combined sources
Beta strandi139 – 1446Combined sources
Helixi152 – 1554Combined sources
Helixi160 – 1645Combined sources
Beta strandi171 – 1733Combined sources
Helixi175 – 18915Combined sources
Beta strandi194 – 1996Combined sources
Helixi203 – 2075Combined sources
Helixi213 – 23119Combined sources
Beta strandi235 – 2395Combined sources
Beta strandi256 – 2583Combined sources
Helixi259 – 2679Combined sources
Beta strandi271 – 2755Combined sources
Helixi286 – 2883Combined sources
Beta strandi290 – 2978Combined sources
Helixi303 – 3119Combined sources
Beta strandi316 – 3216Combined sources
Helixi322 – 3298Combined sources
Helixi333 – 3353Combined sources
Beta strandi338 – 3436Combined sources
Beta strandi348 – 3514Combined sources
Turni353 – 3553Combined sources
Helixi358 – 3603Combined sources
Helixi371 – 3733Combined sources
Beta strandi375 – 3828Combined sources
Helixi395 – 3973Combined sources
Helixi398 – 4047Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EI6X-ray2.10A/B/C/D2-407[»]
ProteinModelPortaliQ51782.
SMRiQ51782. Positions 2-407.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ51782.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK19670.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR002591. Phosphodiest/P_Trfase.
IPR012710. Phosphonoacetate_hydro.
[Graphical view]
PfamiPF01663. Phosphodiest. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
TIGRFAMsiTIGR02335. hydr_PhnA. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q51782-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQLISVNSR SYRLSSAPTI VICVDGCEQE YINQAIQAGQ APFLAELTGF
60 70 80 90 100
GTVLTGDCVV PSFTNPNNLS IVTGAPPSVH GICGNFFFDQ ETQEEVLMND
110 120 130 140 150
AKYLRAPTIL AEMAKAGQLV AVVTAKDKLR NLLGHQLKGI CFSAEKADQV
160 170 180 190 200
NLEEHGVENI LARVGMPVPS VYSADLSEFV FAAGLSLLTN ERPDFMYLST
210 220 230 240 250
TDYVQHKHAP GTPEANAFYA MMDSYFKRYH EQGAIVAITA DHGMNAKTDA
260 270 280 290 300
IGRPNILFLQ DLLDAQYGAQ RTRVLLPITD PYVVHHGALG SYATVYLRDA
310 320 330 340 350
VPQRDAIDFL AGIAGVEAVL TRSQACQRFE LPEDRIGDLV VLGERLTVLG
360 370 380 390 400
SAADKHDLSG LTVPLRSHGG VSEQKVPLIF NRKLVGLDSP GRLRNFDIID

LALNHLA
Length:407
Mass (Da):44,239
Last modified:November 1, 1996 - v1
Checksum:iB706D4A07C42C795
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61S → N in CAI93864 (PubMed:16623750).Curated
Sequence conflicti265 – 2651A → T in CAI93864 (PubMed:16623750).Curated
Sequence conflicti380 – 3801F → V in CAI93864 (PubMed:16623750).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L49465 Genomic DNA. Translation: AAC15507.1.
AJ969111 Genomic DNA. Translation: CAI93864.1.
PIRiS63510.

Genome annotation databases

KEGGiag:AAC15507.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L49465 Genomic DNA. Translation: AAC15507.1.
AJ969111 Genomic DNA. Translation: CAI93864.1.
PIRiS63510.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EI6X-ray2.10A/B/C/D2-407[»]
ProteinModelPortaliQ51782.
SMRiQ51782. Positions 2-407.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC15507.

Phylogenomic databases

KOiK19670.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-202.

Miscellaneous databases

EvolutionaryTraceiQ51782.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR002591. Phosphodiest/P_Trfase.
IPR012710. Phosphonoacetate_hydro.
[Graphical view]
PfamiPF01663. Phosphodiest. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
TIGRFAMsiTIGR02335. hydr_PhnA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning of the phosphonoacetate hydrolase gene from Pseudomonas fluorescens 23F encoding a new type of carbon-phosphorus bond cleaving enzyme and its expression in Escherichia coli and Pseudomonas putida."
    Kulakova A.N., Kulakov L.A., Quinn J.P.
    Gene 195:49-53(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY.
    Strain: 23FImported.
  2. "Detection of phosphonoacetate degradation and phnA genes in soil bacteria from distinct geographical origins suggest its possible biogenic origin."
    Panas P., Ternan N.G., Dooley J.S., McMullan G.
    Environ. Microbiol. 8:939-945(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: R3eImported.
  3. "The purification and properties of phosphonoacetate hydrolase, a novel carbon-phosphorus bond-cleavage enzyme from Pseudomonas fluorescens 23F."
    McGrath J.W., Wisdom G.B., McMullan G., Larkin M.J., Quinn J.P.
    Eur. J. Biochem. 234:225-230(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: 23F1 Publication.
  4. "In vitro characterization of a phosphate starvation-independent carbon-phosphorus bond cleavage activity in Pseudomonas fluorescens 23F."
    McMullan G., Quinn J.P.
    J. Bacteriol. 176:320-324(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, INDUCTION.
    Strain: 23F1 Publication.
  5. "Crystal structure of phosphonoacetate hydrolase complexed with phosphonoformate."
    Holden H.M., Benning M.M., Dunaway-Mariano D., Kim A.D.
    Submitted (FEB-2000) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 4-407, ZINC-BINDING.
    Strain: 23F1 Publication.

Entry informationi

Entry nameiPHNHY_PSEFL
AccessioniPrimary (citable) accession number: Q51782
Secondary accession number(s): Q50HR7, Q9R4G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: November 1, 1996
Last modified: January 20, 2016
This is version 59 of the entry and version 1 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

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.