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

Inorganic triphosphatase

Gene

NE1496

Organism
Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi). The enzyme has a strong preference for linear PPPi compared with cyclic PPPi (cyclic trimetaphosphate) and to the linear P4. The longer chains polyphosphate are not hydrolyzed. It has only a slight thiamine triphosphatase (ThTPase) activity. Nucleoside triphosphatase activity is negligible in the presence of magnesium, but a small activity is observed in the presence of manganese, in particular with GTP.1 Publication

Catalytic activityi

Triphosphate + H2O = diphosphate + phosphate.1 Publication

Enzyme regulationi

Activated by magnesium and mangenese ions, and inhibited by calcium, zinc and copper ions.1 Publication

Kineticsi

Kcat is 288 sec(-1) for hydrolysis of PPPi (at pH 9.7 and 50 degrees Celsius). Kcat is 76 sec(-1) for hydrolysis of PPPi (at pH 9.7 and 37 degrees Celsius). Kcat is 19 sec(-1) for hydrolysis of PPPi (at pH 7.1 and 37 degrees Celsius). Kcat is 0.36 sec(-1) for hydrolysis of ATP (at pH 8.1 and 50 degrees Celsius).

  1. KM=21 µM for PPPi (at pH 9.7 and 37 degrees Celsius)1 Publication
  2. KM=40 µM for PPPi (at pH 9.7 and 50 degrees Celsius)1 Publication
  3. KM=58 µM for PPPi (at pH 7.1 and 50 degrees Celsius)1 Publication
  4. KM=800 µM for ATP (at pH 8.1 and 50 degrees Celsius)1 Publication
  1. Vmax=910 µmol/min/mg enzyme with PPPi as substrate (at pH 9.7 and 50 degrees Celsius)1 Publication
  2. Vmax=240 µmol/min/mg enzyme with PPPi as substrate (at pH 9.7 and 37 degrees Celsius)1 Publication
  3. Vmax=60 µmol/min/mg enzyme with PPPi as substrate (at pH 7.1 and 37 degrees Celsius)1 Publication
  4. Vmax=1.2 µmol/min/mg enzyme with ATP as substrate (at pH 8.1 and 50 degrees Celsius)1 Publication

pH dependencei

Optimum pH is around 9.7.1 Publication

Temperature dependencei

Optimum temperature is between 50 and 55 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei27 – 271Proton acceptor1 Publication

GO - Molecular functioni

  • triphosphatase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciNEUR228410:GJNO-1526-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Inorganic triphosphatase (EC:3.6.1.25)
Short name:
PPPase
Gene namesi
Ordered Locus Names:NE1496
OrganismiNitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
Taxonomic identifieri228410 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
Proteomesi
  • UP000001416 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71K → A: No effect on hydrolase activity. 1 Publication
Mutagenesisi27 – 271Y → F: Strong loss of hydrolase activity. 1 Publication
Mutagenesisi51 – 511K → R: The affinity is strongly decreased and the catalytic efficiency is at least 1000 times lower than that of the wild-type. Manganese ions do not induce a significant activation. 1 Publication
Mutagenesisi84 – 841K → A: It is 10 times less active than the wild-type and the affinity for PPPi is 2 orders of magnitude lower than for the wild-type. Mutant is more strongly activated by manganese ions than by magnesium ions, and the inhibitory effects of calcium and zinc ions are less pronounced. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 151151Inorganic triphosphatasePRO_0000426735Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi228410.NE1496.

Structurei

Secondary structure

1
151
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 129Combined sources
Beta strandi19 – 2911Combined sources
Beta strandi33 – 4210Combined sources
Beta strandi45 – 517Combined sources
Beta strandi60 – 656Combined sources
Helixi67 – 737Combined sources
Helixi74 – 774Combined sources
Beta strandi80 – 9011Combined sources
Beta strandi96 – 1027Combined sources
Helixi104 – 1063Combined sources
Beta strandi110 – 1189Combined sources
Helixi119 – 1246Combined sources
Beta strandi131 – 1344Combined sources
Helixi139 – 1413Combined sources
Helixi143 – 1486Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FBLX-ray1.90A/B1-151[»]
3TYPX-ray1.90A/B2-151[»]
ProteinModelPortaliQ82UI9.
SMRiQ82UI9. Positions 2-151.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ82UI9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 148148CYTHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CYTH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105P0I. Bacteria.
COG2954. LUCA.
HOGENOMiHOG000004483.
OMAiTEDARYK.
OrthoDBiEOG6DC6QR.

Family and domain databases

Gene3Di2.40.320.10. 1 hit.
InterProiIPR033469. CYTH-like_dom.
IPR023577. CYTH_domain.
IPR012042. NeuTTM/CthTTM-like.
[Graphical view]
PfamiPF01928. CYTH. 1 hit.
[Graphical view]
PIRSFiPIRSF016487. CYTH_UCP016487. 1 hit.
SMARTiSM01118. CYTH. 1 hit.
[Graphical view]
SUPFAMiSSF55154. SSF55154. 1 hit.
PROSITEiPS51707. CYTH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q82UI9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEIERKFLV ATFPDGELHA VPLRQGYLTT PTDSIELRLR QQGTEYFMTL
60 70 80 90 100
KSEGGLSRQE YEIQIDVTQF EMLWPATEGR RVEKTRYSGK LPDGQLFELD
110 120 130 140 150
VFAGHLSPLM LVEVEFLSED AAQAFIPPPW FGEEVTEDKR YKNKALALSI

P
Length:151
Mass (Da):17,314
Last modified:June 1, 2003 - v1
Checksum:iB5A584857833ECCA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL954747 Genomic DNA. Translation: CAD85407.1.
RefSeqiWP_011112064.1. NC_004757.1.

Genome annotation databases

EnsemblBacteriaiCAD85407; CAD85407; NE1496.
KEGGineu:NE1496.
PATRICi22714171. VBINitEur56163_1679.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL954747 Genomic DNA. Translation: CAD85407.1.
RefSeqiWP_011112064.1. NC_004757.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FBLX-ray1.90A/B1-151[»]
3TYPX-ray1.90A/B2-151[»]
ProteinModelPortaliQ82UI9.
SMRiQ82UI9. Positions 2-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi228410.NE1496.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAD85407; CAD85407; NE1496.
KEGGineu:NE1496.
PATRICi22714171. VBINitEur56163_1679.

Phylogenomic databases

eggNOGiENOG4105P0I. Bacteria.
COG2954. LUCA.
HOGENOMiHOG000004483.
OMAiTEDARYK.
OrthoDBiEOG6DC6QR.

Enzyme and pathway databases

BioCyciNEUR228410:GJNO-1526-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ82UI9.

Family and domain databases

Gene3Di2.40.320.10. 1 hit.
InterProiIPR033469. CYTH-like_dom.
IPR023577. CYTH_domain.
IPR012042. NeuTTM/CthTTM-like.
[Graphical view]
PfamiPF01928. CYTH. 1 hit.
[Graphical view]
PIRSFiPIRSF016487. CYTH_UCP016487. 1 hit.
SMARTiSM01118. CYTH. 1 hit.
[Graphical view]
SUPFAMiSSF55154. SSF55154. 1 hit.
PROSITEiPS51707. CYTH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
    Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
    J. Bacteriol. 185:2759-2773(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19718 / NBRC 14298.
  2. "The crystal structure of the hypothetical protein NE1496."
    Lunin V.V., Skarina T., Onopriyenko O., Binkowski T.A., Joachimiak A., Edwards A.M., Savchenko A.
    Submitted (DEC-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), SUBUNIT.
  3. "A specific inorganic triphosphatase from Nitrosomonas europaea: structure and catalytic mechanism."
    Delvaux D., Murty M.R., Gabelica V., Lakaye B., Lunin V.V., Skarina T., Onopriyenko O., Kohn G., Wins P., De Pauw E., Bettendorff L.
    J. Biol. Chem. 286:34023-34035(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-7; TYR-27; LYS-51 AND LYS-84, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, REACTION MECHANISM, ENZYME REGULATION, SUBUNIT.

Entry informationi

Entry namei3PASE_NITEU
AccessioniPrimary (citable) accession number: Q82UI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: June 1, 2003
Last modified: May 11, 2016
This is version 80 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, Complete proteome, Reference proteome

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.