Reviewed, UniProtKB/Swiss-Prot O94505 (DPNP_SCHPO)

Names and origin

Protein names

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 names

Name:	tol1
ORF Names:	SPCC1753.04

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	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. Ref.1 Confers resistance to lithium. Ref.1
Catalytic activity	Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
Cofactor	Magnesium. Ref.1
Sequence similarities	Belongs to the inositol monophosphatase family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	sulfur metabolic process Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	3'(2'),5'-bisphosphate nucleotidase activity Ref.1 Inferred from direct assay. Source: GeneDB_SPombe inositol-1,4-bisphosphate 1-phosphatase activity Ref.1 Inferred from direct assay. Source: GeneDB_SPombe magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 353	353	3'(2'),5'-bisphosphate nucleotidase		PRO_0000142536
Sites
	Metal binding	73	1	Magnesium 1 By similarity
	Metal binding	136	1	Magnesium 1 By similarity
	Metal binding	136	1	Magnesium 2 By similarity
	Metal binding	138	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	139	1	Magnesium 2 By similarity
	Metal binding	286	1	Magnesium 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	O94505-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: F88CCAB21C653349	FASTA	353	38,748
	10 20 30 40 50 60 MSFDAEKQLA IAAVRRASYL TEKVFNQLIK EKSAAGALTK DDKSPVTIGD FGAQAIVISM 70 80 90 100 110 120 LKDAFPNDPI VGEEDSDFLR ENTQTCSRVW ELVQETIQHA TEYKELGQIK SAEEMMSIID 130 140 150 160 170 180 QGSYHGGRNG RMWTLDPIDG TKGFLRGAQY AICLALIENG KPVVSAIGCP NLPYDFNQPE 190 200 210 220 230 240 TSPKGIIMSA VRNHGCFQYS LHNEKLEPVQ VHMQDVQNTK DSKFCEGVEA GHSMQGTQEE 250 260 270 280 290 300 IAKYLGITRG PTKMDSQAKY ASLARGDGDI YLRLPTKMTF EEKIWDHAGG SLLVEEAGGV 310 320 330 340 350 VSDMFGKPLD FGVGRTLKNN NGVIAAYKGI FEKVIEATAA VTSKDPHFQK VAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10850973] [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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D86083 Genomic DNA. Translation: BAA96866.1. CU329672 Genomic DNA. Translation: CAA22778.1.
PIR	T41127.
RefSeq	NP_588230.1.
3D structure databases
HSSP	HSSP built from PDB template 1KA0 based on UniProtKB P32179.
ModBase	Search...
Genome annotation databases
GeneID	2538954.
KEGG	spo:SPCC1753.04.
NMPDR	fig|4896.1.peg.568.
Organism-specific databases
GeneDB_Spombe	SPCC1753.04.
Phylogenomic databases
OMA	O94505. ENIWDHA.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000162-MON.
BRENDA	3.1.3.7. 653.
Gene expression databases
ArrayExpress	O94505.
Family and domain databases
InterPro	IPR006239. Bisphos_HAL2. IPR000760. Inositol_P. [Graphical view]
PANTHER	PTHR20854. Inositol_P. 1 hit.
Pfam	PF00459. Inositol_P. 1 hit. [Graphical view]
PRINTS	PR00378. INOSPHPHTASE.
TIGRFAMs	TIGR01330. bisphos_HAL2. 1 hit.
PROSITE	PS00629. IMP_1. 1 hit. PS00630. IMP_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DPNP_SCHPO

Accession

Primary (citable) accession number: O94505

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)