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Protein

Inorganic triphosphatase

Gene

ygiF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 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), which could be cytotoxic because of its high affinity for calcium ion, thereby interfering with calcium signaling. It also hydrolyzes slowly thiamine triphosphate (ThTP). YgiF is a specific PPPase, but it contributes only marginally to the total PPPase activity in E.coli, where the main enzyme responsible for hydrolysis of PPPi is inorganic pyrophosphatase (PPase).1 Publication

Catalytic activityi

Triphosphate + H2O = diphosphate + phosphate.1 Publication

Enzyme regulationi

Inhibited by calcium ion and activated by magnesium ion.1 Publication

Kineticsi

  1. KM=270 µM for inorganic triphosphate1 Publication
  1. Vmax=27 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 8.5.1 Publication

GO - Molecular functioni

  • metal ion binding Source: EcoCyc
  • triphosphatase activity Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciEcoCyc:EG11603-MONOMER.
ECOL316407:JW3026-MONOMER.
MetaCyc:EG11603-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Inorganic triphosphatase (EC:3.6.1.25)
Short name:
PPPase
Alternative name(s):
ORFXE
Gene namesi
Name:ygiF
Ordered Locus Names:b3054, JW3026
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11603. ygiF.

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene do not show decrease of specific PPPase activity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433Inorganic triphosphatasePRO_0000169406Add
BLAST

Proteomic databases

EPDiP30871.
PaxDbiP30871.
PRIDEiP30871.

Interactioni

Protein-protein interaction databases

BioGridi4259253. 4 interactions.
DIPiDIP-12218N.
IntActiP30871. 23 interactions.
MINTiMINT-1248396.
STRINGi511145.b3054.

Structurei

Secondary structure

1
433
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1110Combined sources
Helixi13 – 153Combined sources
Helixi16 – 238Combined sources
Beta strandi29 – 4214Combined sources
Helixi47 – 504Combined sources
Beta strandi54 – 607Combined sources
Beta strandi63 – 697Combined sources
Beta strandi73 – 753Combined sources
Beta strandi78 – 9215Combined sources
Helixi95 – 973Combined sources
Helixi100 – 1023Combined sources
Beta strandi103 – 1075Combined sources
Helixi112 – 1154Combined sources
Beta strandi117 – 13317Combined sources
Beta strandi136 – 14914Combined sources
Beta strandi152 – 16615Combined sources
Helixi168 – 17811Combined sources
Beta strandi181 – 1866Combined sources
Helixi191 – 1999Combined sources
Helixi221 – 24424Combined sources
Helixi250 – 26718Combined sources
Turni268 – 2714Combined sources
Helixi274 – 2774Combined sources
Helixi278 – 29316Combined sources
Helixi297 – 3026Combined sources
Helixi304 – 31815Combined sources
Turni319 – 3224Combined sources
Helixi323 – 3253Combined sources
Helixi328 – 3347Combined sources
Helixi338 – 35720Combined sources
Helixi366 – 3683Combined sources
Helixi369 – 38214Combined sources
Helixi388 – 40720Combined sources
Helixi410 – 42213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5A60X-ray1.82A1-433[»]
5A61X-ray1.50A1-433[»]
ProteinModelPortaliP30871.
SMRiP30871. Positions 1-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 202201CYTHPROSITE-ProRule annotationAdd
BLAST
Domaini218 – 433216CHADPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CHAD domain.PROSITE-ProRule annotation
Contains 1 CYTH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105I7R. Bacteria.
COG3025. LUCA.
HOGENOMiHOG000283528.
InParanoidiP30871.
KOiK18446.
OMAiQEPICEL.
OrthoDBiEOG60PHBT.

Family and domain databases

Gene3Di2.40.320.10. 1 hit.
InterProiIPR007899. CHAD_dom.
IPR033469. CYTH-like_dom.
IPR023577. CYTH_domain.
[Graphical view]
PfamiPF01928. CYTH. 1 hit.
[Graphical view]
SMARTiSM01118. CYTH. 1 hit.
[Graphical view]
SUPFAMiSSF55154. SSF55154. 1 hit.
PROSITEiPS51708. CHAD. 1 hit.
PS51707. CYTH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQEIELKFI VNHSAVEALR DHLNTLGGEH HDPVQLLNIY YETPDNWLRG
60 70 80 90 100
HDMGLRIRGE NGRYEMTMKV AGRVTGGLHQ RPEYNVALSE PTLDLAQLPT
110 120 130 140 150
EVWPNGELPA DLASRVQPLF STDFYREKWL VAVDGSQIEI ALDQGEVKAG
160 170 180 190 200
EFAEPICELE LELLSGDTRA VLKLANQLVS QTGLRQGSLS KAARGYHLAQ
210 220 230 240 250
GNPAREIKPT TILHVAAKAD VEQGLEAALE LALAQWQYHE ELWVRGNDAA
260 270 280 290 300
KEQVLAAISL VRHTLMLFGG IVPRKASTHL RDLLTQCEAT IASAVSAVTA
310 320 330 340 350
VYSTETAMAK LALTEWLVSK AWQPFLDAKA QGKISDSFKR FADIHLSRHA
360 370 380 390 400
AELKSVFCQP LGDRYRDQLP RLTRDIDSIL LLAGYYDPVV AQAWLENWQG
410 420 430
LHHAIATGQR IEIEHFRNEA NNQEPFWLHS GKR
Length:433
Mass (Da):48,389
Last modified:July 1, 1993 - v1
Checksum:iF2CB1519123C0277
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21844 Genomic DNA. Translation: CAA79891.1.
U00096 Genomic DNA. Translation: AAC76090.1.
AP009048 Genomic DNA. Translation: BAE77105.1.
PIRiS37754.
RefSeqiNP_417526.1. NC_000913.3.
WP_000046281.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76090; AAC76090; b3054.
BAE77105; BAE77105; BAE77105.
GeneIDi947554.
KEGGiecj:JW3026.
eco:b3054.
PATRICi32121520. VBIEscCol129921_3147.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21844 Genomic DNA. Translation: CAA79891.1.
U00096 Genomic DNA. Translation: AAC76090.1.
AP009048 Genomic DNA. Translation: BAE77105.1.
PIRiS37754.
RefSeqiNP_417526.1. NC_000913.3.
WP_000046281.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5A60X-ray1.82A1-433[»]
5A61X-ray1.50A1-433[»]
ProteinModelPortaliP30871.
SMRiP30871. Positions 1-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259253. 4 interactions.
DIPiDIP-12218N.
IntActiP30871. 23 interactions.
MINTiMINT-1248396.
STRINGi511145.b3054.

Proteomic databases

EPDiP30871.
PaxDbiP30871.
PRIDEiP30871.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76090; AAC76090; b3054.
BAE77105; BAE77105; BAE77105.
GeneIDi947554.
KEGGiecj:JW3026.
eco:b3054.
PATRICi32121520. VBIEscCol129921_3147.

Organism-specific databases

EchoBASEiEB1560.
EcoGeneiEG11603. ygiF.

Phylogenomic databases

eggNOGiENOG4105I7R. Bacteria.
COG3025. LUCA.
HOGENOMiHOG000283528.
InParanoidiP30871.
KOiK18446.
OMAiQEPICEL.
OrthoDBiEOG60PHBT.

Enzyme and pathway databases

BioCyciEcoCyc:EG11603-MONOMER.
ECOL316407:JW3026-MONOMER.
MetaCyc:EG11603-MONOMER.

Miscellaneous databases

PROiP30871.

Family and domain databases

Gene3Di2.40.320.10. 1 hit.
InterProiIPR007899. CHAD_dom.
IPR033469. CYTH-like_dom.
IPR023577. CYTH_domain.
[Graphical view]
PfamiPF01928. CYTH. 1 hit.
[Graphical view]
SMARTiSM01118. CYTH. 1 hit.
[Graphical view]
SUPFAMiSSF55154. SSF55154. 1 hit.
PROSITEiPS51708. CHAD. 1 hit.
PS51707. CYTH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli."
    van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.
    Mol. Microbiol. 9:443-458(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / CS520.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "High inorganic triphosphatase activities in bacteria and mammalian cells: identification of the enzymes involved."
    Kohn G., Delvaux D., Lakaye B., Servais A.C., Scholer G., Fillet M., Elias B., Derochette J.M., Crommen J., Wins P., Bettendorff L.
    PLoS ONE 7:E43879-E43879(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, ENZYME REGULATION, SUBSTRATE SPECIFICITY.

Entry informationi

Entry namei3PASE_ECOLI
AccessioniPrimary (citable) accession number: P30871
Secondary accession number(s): Q2M9F1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 11, 2016
This is version 122 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.