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Protein

3'(2'),5'-bisphosphate nucleotidase

Gene

tol1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS.1 Publication
Confers resistance to lithium.1 Publication

Catalytic activityi

Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.

Cofactori

Mg2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi73 – 731Magnesium 1By similarity
Binding sitei73 – 731SubstrateBy similarity
Metal bindingi136 – 1361Magnesium 1By similarity
Metal bindingi136 – 1361Magnesium 2By similarity
Metal bindingi138 – 1381Magnesium 1; via carbonyl oxygenBy similarity
Metal bindingi139 – 1391Magnesium 2By similarity
Metal bindingi286 – 2861Magnesium 2By similarity
Binding sitei286 – 2861SubstrateBy similarity

GO - Molecular functioni

  • 3'(2'),5'-bisphosphate nucleotidase activity Source: PomBase
  • inositol-1,3,4-trisphosphate 1-phosphatase activity Source: PomBase
  • inositol-1,4-bisphosphate 1-phosphatase activity Source: PomBase
  • magnesium ion binding Source: GO_Central

GO - Biological processi

  • methionine biosynthetic process Source: GO_Central
  • phosphatidylinositol phosphorylation Source: InterPro
  • sulfate assimilation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
3'(2'),5'-bisphosphate nucleotidase (EC:3.1.3.7)
Alternative name(s):
3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase
DPNPase
Halotolerance protein tol1
Target of lithium protein 1
Gene namesi
Name:tol1
ORF Names:SPCC1753.04
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1753.04.
PomBaseiSPCC1753.04. tol1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3533533'(2'),5'-bisphosphate nucleotidasePRO_0000142536Add
BLAST

Proteomic databases

MaxQBiO94505.

Interactioni

Protein-protein interaction databases

BioGridi275528. 21 interactions.
MINTiMINT-4684747.

Structurei

3D structure databases

ProteinModelPortaliO94505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni138 – 1414Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

HOGENOMiHOG000170673.
InParanoidiO94505.
KOiK01082.
OMAiHATEYKE.
OrthoDBiEOG7VB2R7.
PhylomeDBiO94505.

Family and domain databases

InterProiIPR006239. Bisphos_HAL2.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 2 hits.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSiPR00377. IMPHPHTASES.
TIGRFAMsiTIGR01330. bisphos_HAL2. 1 hit.
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94505-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFDAEKQLA IAAVRRASYL TEKVFNQLIK EKSAAGALTK DDKSPVTIGD
60 70 80 90 100
FGAQAIVISM LKDAFPNDPI VGEEDSDFLR ENTQTCSRVW ELVQETIQHA
110 120 130 140 150
TEYKELGQIK SAEEMMSIID QGSYHGGRNG RMWTLDPIDG TKGFLRGAQY
160 170 180 190 200
AICLALIENG KPVVSAIGCP NLPYDFNQPE TSPKGIIMSA VRNHGCFQYS
210 220 230 240 250
LHNEKLEPVQ VHMQDVQNTK DSKFCEGVEA GHSMQGTQEE IAKYLGITRG
260 270 280 290 300
PTKMDSQAKY ASLARGDGDI YLRLPTKMTF EEKIWDHAGG SLLVEEAGGV
310 320 330 340 350
VSDMFGKPLD FGVGRTLKNN NGVIAAYKGI FEKVIEATAA VTSKDPHFQK

VAQ
Length:353
Mass (Da):38,748
Last modified:May 1, 1999 - v1
Checksum:iF88CCAB21C653349
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86083 Genomic DNA. Translation: BAA96866.1.
CU329672 Genomic DNA. Translation: CAA22778.1.
PIRiT41127.
RefSeqiNP_588230.1. NM_001023220.2.

Genome annotation databases

EnsemblFungiiSPCC1753.04.1; SPCC1753.04.1:pep; SPCC1753.04.
GeneIDi2538954.
KEGGispo:SPCC1753.04.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86083 Genomic DNA. Translation: BAA96866.1.
CU329672 Genomic DNA. Translation: CAA22778.1.
PIRiT41127.
RefSeqiNP_588230.1. NM_001023220.2.

3D structure databases

ProteinModelPortaliO94505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275528. 21 interactions.
MINTiMINT-4684747.

Proteomic databases

MaxQBiO94505.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1753.04.1; SPCC1753.04.1:pep; SPCC1753.04.
GeneIDi2538954.
KEGGispo:SPCC1753.04.

Organism-specific databases

EuPathDBiFungiDB:SPCC1753.04.
PomBaseiSPCC1753.04. tol1.

Phylogenomic databases

HOGENOMiHOG000170673.
InParanoidiO94505.
KOiK01082.
OMAiHATEYKE.
OrthoDBiEOG7VB2R7.
PhylomeDBiO94505.

Miscellaneous databases

PROiO94505.

Family and domain databases

InterProiIPR006239. Bisphos_HAL2.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 2 hits.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSiPR00377. IMPHPHTASES.
TIGRFAMsiTIGR01330. bisphos_HAL2. 1 hit.
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Tol1, a fission yeast phosphomonoesterase, is an in vivo target of lithium, and its deletion leads to sulfite auxotrophy."
    Miyamoto R., Sugiura R., Kamitani S., Yada T., Lu Y., Sio S.O., Asakura M., Matsuhisa A., Shuntoh H., Kuno T.
    J. Bacteriol. 182:3619-3625(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiDPNP_SCHPO
AccessioniPrimary (citable) accession number: O94505
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: May 1, 1999
Last modified: July 6, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.