Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Metal bindingi25Zinc 11 Publication1
Metal bindingi64Zinc 11 Publication1
Binding sitei64Substrate1 Publication1
Metal bindingi202Zinc 21 Publication1
Binding sitei202Substrate1 Publication1
Metal bindingi206Zinc 2; via tele nitrogen1 Publication1
Metal bindingi241Zinc 11 Publication1
Metal bindingi242Zinc 1; via tele nitrogen1 Publication1
Binding sitei242Substrate1 Publication1
Metal bindingi368Zinc 2; via tele nitrogen1 Publication1
Binding sitei368Substrate1 Publication1

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00004025792 – 407Phosphonoacetate hydrolase1 PublicationAdd BLAST406

Expressioni

Inductioni

By phosphonoacetate.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1407
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi10 – 13Combined sources4
Beta strandi19 – 23Combined sources5
Helixi29 – 37Combined sources9
Helixi42 – 46Combined sources5
Helixi47 – 49Combined sources3
Beta strandi51 – 57Combined sources7
Helixi64 – 73Combined sources10
Helixi77 – 80Combined sources4
Beta strandi84 – 89Combined sources6
Turni90 – 93Combined sources4
Beta strandi94 – 97Combined sources4
Helixi101 – 103Combined sources3
Helixi109 – 115Combined sources7
Beta strandi120 – 126Combined sources7
Helixi127 – 133Combined sources7
Turni134 – 136Combined sources3
Beta strandi139 – 144Combined sources6
Helixi152 – 155Combined sources4
Helixi160 – 164Combined sources5
Beta strandi171 – 173Combined sources3
Helixi175 – 189Combined sources15
Beta strandi194 – 199Combined sources6
Helixi203 – 207Combined sources5
Helixi213 – 231Combined sources19
Beta strandi235 – 239Combined sources5
Beta strandi256 – 258Combined sources3
Helixi259 – 267Combined sources9
Beta strandi271 – 275Combined sources5
Helixi286 – 288Combined sources3
Beta strandi290 – 297Combined sources8
Helixi303 – 311Combined sources9
Beta strandi316 – 321Combined sources6
Helixi322 – 329Combined sources8
Helixi333 – 335Combined sources3
Beta strandi338 – 343Combined sources6
Beta strandi348 – 351Combined sources4
Turni353 – 355Combined sources3
Helixi358 – 360Combined sources3
Helixi371 – 373Combined sources3
Beta strandi375 – 382Combined sources8
Helixi395 – 397Combined sources3
Helixi398 – 404Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EI6X-ray2.10A/B/C/D2-407[»]
ProteinModelPortaliQ51782.
SMRiQ51782.
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)DescriptionActionsGraphical viewLength
Sequence conflicti6S → N in CAI93864 (PubMed:16623750).Curated1
Sequence conflicti265A → T in CAI93864 (PubMed:16623750).Curated1
Sequence conflicti380F → V in CAI93864 (PubMed:16623750).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EI6X-ray2.10A/B/C/D2-407[»]
ProteinModelPortaliQ51782.
SMRiQ51782.
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...

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: November 2, 2016
This is version 61 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.