UniProtKB - Q84G06 (PPHA_VARSP)
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>sp|Q84G06|PPHA_VARSP Phosphonopyruvate hydrolase OS=Variovorax sp. (strain Pal2) OX=218557 GN=pphA PE=1 SV=1 MTKNQALRAALDSGRLFTAMAAHNPLVAKLAEQAGFGGIWGSGFELSASYAVPDANILSM STHLEMMRAIASTVSIPLIADIDTGFGNAVNVHYVVPQYEAAGASAIVMEDKTFPKDTSL RTDGRQELVRIEEFQGKIAAATAARADRDFVVIARVEALIAGLGQQEAVRRGQAYEEAGA DAILIHSRQKTPDEILAFVKSWPGKVPLVLVPTAYPQLTEADIAALSKVGIVIYGNHAIR AAVGAVREVFARIRRDGGIREVDAALPSVKEIIELQGDERMRAVEARYLKCommunity curation ()Add a publicationFeedback
Protein
Phosphonopyruvate hydrolase
Gene
pphA
Organism
Variovorax sp. (strain Pal2)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Hydrolyzes phosphonopyruvate. Not active towards phosphoenolpyruvate, glycerophosphate, phospho-L-serine or phosphoglycolic acid.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract]
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- 3-phosphonopyruvateEC:3.11.1.3
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Manual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract]
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract]
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
3-phosphonopyruvate- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=H+- Search proteins in UniProtKB for this molecule.
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+phosphate- Search proteins in UniProtKB for this molecule.
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+pyruvate- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Co2+
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- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract]
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract]
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract]
Manual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract]
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Partially inhibited by EDTA. Activity is restored by Co2+, and to a lesser extent by Ni2+ and Mg2+. Unaffected by Cs2+ and Ca2+. Activity is reduced by Mn2+ and Cu2+.1 Publication
Manual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract]
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=0.53 mM for phosphonopyruvate (at 37 degrees Celsius, pH 7.0, with 5 µmol CoCl2)2 Publications
Manual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract] - Ref.3"Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily."
Chen C.C., Han Y., Niu W., Kulakova A.N., Howard A., Quinn J.P., Dunaway-Mariano D., Herzberg O.
Biochemistry 45:11491-11504(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH MAGNESIUM IONS; PHOSPHONOPYRUVATE AND OXALATE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-188, SUBUNIT.
- KM=19.5 µM for phosphonopyruvate (at 25 degrees Celsius, pH 7.5, with 5 mM MgCl2)2 Publications
Manual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract] - Ref.3"Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily."
Chen C.C., Han Y., Niu W., Kulakova A.N., Howard A., Quinn J.P., Dunaway-Mariano D., Herzberg O.
Biochemistry 45:11491-11504(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH MAGNESIUM IONS; PHOSPHONOPYRUVATE AND OXALATE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-188, SUBUNIT.
- Vmax=202 µmol/min/mg enzyme (at 37 degrees Celsius, pH 7.0, with 5 µmol CoCl2)2 Publications
Manual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract] - Ref.3"Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily."
Chen C.C., Han Y., Niu W., Kulakova A.N., Howard A., Quinn J.P., Dunaway-Mariano D., Herzberg O.
Biochemistry 45:11491-11504(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH MAGNESIUM IONS; PHOSPHONOPYRUVATE AND OXALATE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-188, SUBUNIT.
pH dependencei
Optimum pH is 7.0. Active from pH 6.0 to 9.0.2 Publications
Manual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract] - Ref.3"Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily."
Chen C.C., Han Y., Niu W., Kulakova A.N., Howard A., Quinn J.P., Dunaway-Mariano D., Herzberg O.
Biochemistry 45:11491-11504(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH MAGNESIUM IONS; PHOSPHONOPYRUVATE AND OXALATE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-188, SUBUNIT.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 54 | Nucleophile1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 81 | Magnesium1 Publication Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 155 | Substrate | 1 | |
| Binding sitei | 186 | Substrate | 1 | |
| Binding sitei | 188 | Substrate | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- phosphonopyruvate hydrolase activity Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract]
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Hydrolase |
| Ligand | Cobalt, Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:MONOMER-16715 |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.11.1.3, 8611 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Phosphonopyruvate hydrolase1 PublicationManual assertion based on opinion ini
Short name: PPH1 Publication Manual assertion based on opinion ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:pphA1 Publication Manual assertion based on opinion ini
Synonyms:palAImported <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Variovorax sp. (strain Pal2) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 218557 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Variovorax › unclassified Variovorax |
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 188 | R → A: Reduced affinity for substrate. 1 Publication Manual assertion based on experiment ini
| 1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000401168 | 1 – 290 | Phosphonopyruvate hydrolaseAdd BLAST | 290 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
By phosphonoalanine or phosphonopyruvate.1 Publication
Manual assertion based on experiment ini
- Ref.2"Expression of the phosphonoalanine-degradative gene cluster from Variovorax sp. Pal2 is induced by growth on phosphonoalanine and phosphonopyruvate."
Kulakova A.N., Kulakov L.A., Villarreal-Chiu J.F., Gilbert J.A., McGrath J.W., Quinn J.P.
FEMS Microbiol. Lett. 292:100-106(2009) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer (PubMed:12697754). Homotetramer (PubMed:16981709).
2 PublicationsManual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract] - Ref.3"Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily."
Chen C.C., Han Y., Niu W., Kulakova A.N., Howard A., Quinn J.P., Dunaway-Mariano D., Herzberg O.
Biochemistry 45:11491-11504(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH MAGNESIUM IONS; PHOSPHONOPYRUVATE AND OXALATE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-188, SUBUNIT.
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 3 – 13 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 17 – 21 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 25 – 34 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 37 – 41 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 43 – 49 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 54 – 56 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 60 – 71 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Beta strandi | 78 – 81 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 83 – 86 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 89 – 102 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| Beta strandi | 105 – 110 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 131 – 144 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| Beta strandi | 150 – 156 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Turni | 158 – 162 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 165 – 177 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 181 – 185 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 190 – 192 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 193 – 201 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 208 – 210 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 220 – 224 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 229 – 234 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 237 – 256 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| Turni | 260 – 265 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 269 – 275 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 278 – 288 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q84G06 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q84G06 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 40 – 44 | Substrate binding | 5 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Family and domain databases
Conserved Domains Database More...CDDi | cd00377, ICL_PEPM, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.20.20.60, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR039556, ICL/PEPM IPR012649, PPH IPR015813, Pyrv/PenolPyrv_Kinase-like_dom IPR040442, Pyrv_Kinase-like_dom_sf |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51621, SSF51621, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR02321, Pphn_pyruv_hyd, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
Q84G06-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MTKNQALRAA LDSGRLFTAM AAHNPLVAKL AEQAGFGGIW GSGFELSASY
60 70 80 90 100
AVPDANILSM STHLEMMRAI ASTVSIPLIA DIDTGFGNAV NVHYVVPQYE
110 120 130 140 150
AAGASAIVME DKTFPKDTSL RTDGRQELVR IEEFQGKIAA ATAARADRDF
160 170 180 190 200
VVIARVEALI AGLGQQEAVR RGQAYEEAGA DAILIHSRQK TPDEILAFVK
210 220 230 240 250
SWPGKVPLVL VPTAYPQLTE ADIAALSKVG IVIYGNHAIR AAVGAVREVF
260 270 280 290
ARIRRDGGIR EVDAALPSVK EIIELQGDER MRAVEARYLK
Length:290
Mass (Da):31,179
Last modified:June 1, 2003 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i9B041151AE069F47
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 132 | E → I AA sequence (PubMed:12697754).Curated | 1 |
<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi
Molecular mass is 31187 Da. Determined by MALDI. 1 Publication
Manual assertion based on experiment ini
- Ref.1"The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2."
Kulakova A.N., Wisdom G.B., Kulakov L.A., Quinn J.P.
J. Biol. Chem. 278:23426-23431(2003) [PubMed] [Europe PMC] [Abstract]
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AY179862 Genomic DNA Translation: AAO24736.1 |
Genome annotation databases
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ag:AAO24736 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q84G06 | Phosphonopyruvate hydrolase | 290 | UniRef100_Q84G06 |
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q84G06 | Phosphonopyruvate hydrolase | 290 | UniRef90_Q84G06 | |||
| +1 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q84G06 | Phosphonopyruvate hydrolase | 290 | UniRef50_Q84G06 | |||
| Phosphoenolpyruvate phosphomutase | 290 | |||||
| Phosphonopyruvate hydrolase | 290 | |||||
| Unannotated protein | 290 | |||||
| Phosphonopyruvate hydrolase | 290 | |||||
| +273 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY179862 Genomic DNA Translation: AAO24736.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2DUA | X-ray | 2.00 | A | 1-290 | [»] | |
| 2HJP | X-ray | 1.90 | A | 1-290 | [»] | |
| 2HRW | X-ray | 2.20 | A | 1-290 | [»] | |
| SMRi | Q84G06 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Genome annotation databases
| KEGGi | ag:AAO24736 |
Enzyme and pathway databases
| BioCyci | MetaCyc:MONOMER-16715 |
| BRENDAi | 3.11.1.3, 8611 |
Miscellaneous databases
| EvolutionaryTracei | Q84G06 |
Family and domain databases
| CDDi | cd00377, ICL_PEPM, 1 hit |
| Gene3Di | 3.20.20.60, 1 hit |
| InterProi | View protein in InterPro IPR039556, ICL/PEPM IPR012649, PPH IPR015813, Pyrv/PenolPyrv_Kinase-like_dom IPR040442, Pyrv_Kinase-like_dom_sf |
| SUPFAMi | SSF51621, SSF51621, 1 hit |
| TIGRFAMsi | TIGR02321, Pphn_pyruv_hyd, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | PPHA_VARSP | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q84G06Primary (citable) accession number: Q84G06 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 30, 2010 |
| Last sequence update: | June 1, 2003 | |
| Last modified: | April 7, 2021 | |
| This is version 65 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
