Reviewed, UniProtKB/Swiss-Prot Q09790 (APS1_SCHPO)

Names and origin

Protein names

Recommended name:
    Diphosphoinositol polyphosphate phosphohydrolase aps1
    EC=3.6.1.52
Alternative name(s):
    Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase
      Short name=Ap6A hydrolase
    EC=3.6.1.-

Gene names

Name:	aps1
ORF Names:	SPAC13G6.14, SPAC24B11.03

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	210 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate). Also catalyzes the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A.
Catalytic activity	Diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate. Ref.3 Ref.4
Cofactor	Magnesium By similarity.
Subunit structure	Monomer.
Sequence similarities	Belongs to the Nudix hydrolase family. DIPP subfamily.
Biophysicochemical properties	Kinetic parameters: KM=31 nM for PP-InsP5

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	diadenosine polyphosphate metabolic process Ref.1 Inferred from direct assay. Source: GeneDB_SPombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	diphosphoinositol-polyphosphate diphosphatase 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 – 210	210	Diphosphoinositol polyphosphate phosphohydrolase aps1		PRO_0000057068
Regions
	Motif	74 – 95	22	Nudix box
Sites
	Metal binding	89	1	Magnesium By similarity
	Metal binding	93	1	Magnesium By similarity
Experimental info
	Mutagenesis	93	1	E → Q: Does not affect intracellular Ap5A level, but strongly reduces DIPP enzyme activity. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q09790-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 492F7BF9563A1C98	FASTA	210	23,724
	10 20 30 40 50 60 MLENNGSVIL MEPDHLRTAV NRSMTSREGR TKNRFNPITG ARLAAGVVAL SADKRKVLLV 70 80 90 100 110 120 SSAKKHPSWV VPKGGWEADE SVQQAALREG WEEGGLVGHI TRSLGSFKDK RPTDTIDRRK 130 140 150 160 170 180 KYLKQLMSKS SGNDVSTNTE LGAEAEKLLL PPRAECEFFE VIVERLEDNY PEMRKRRRKW 190 200 210 MSYQEAKEAL TSRKDILAAL EKSSIIKEEN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Schizosaccharomyces pombe Aps1, a diadenosine 5',5'''-P1, P6-hexaphosphate hydrolase that is a member of the nudix (MutT) family of hydrolases: cloning of the gene and characterization of the purified enzyme." Ingram S.W., Stratemann S.A., Barnes L.D. Biochemistry 38:3649-3655(1999) [PubMed: 10090752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: ATCC 38366 / 972.
[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.
[3]	"The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein." Safrany S.T., Ingram S.W., Cartwright J.L., Falck J.R., McLennan A.G., Barnes L.D., Shears S.B. J. Biol. Chem. 274:21735-21740(1999) [PubMed: 10419486] [Abstract] Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"Disruption and overexpression of the Schizosaccharomyces pombe aps1 gene, and effects on growth rate, morphology and intracellular diadenosine 5',5''-P1,P5-pentaphosphate and diphosphoinositol polyphosphate concentrations." Ingram S.W., Safrany S.T., Barnes L.D. Biochem. J. 369:519-528(2003) [PubMed: 12387729] [Abstract] Cited for: ENZYME ACTIVITY, MUTAGENESIS OF GLU-93.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF125215 Genomic DNA. Translation: AAD20015.1. CU329670 Genomic DNA. Translation: CAA91107.1.
PIR	S62443.
RefSeq	NP_592840.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2542890.
KEGG	spo:SPAC13G6.14.
NMPDR	fig|4896.1.peg.2810.
Organism-specific databases
GeneDB_Spombe	SPAC13G6.14.
Phylogenomic databases
OMA	Q09790. WMREALQ.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000511-MON.
BRENDA	3.6.1.52. 653.
Gene expression databases
ArrayExpress	Q09790.
Family and domain databases
InterPro	IPR000086. NUDIX_hydrolase_core. [Graphical view]
Gene3D	G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
Pfam	PF00293. NUDIX. 1 hit. [Graphical view]
PROSITE	PS00893. NUDIX. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APS1_SCHPO

Accession

Primary (citable) accession number: Q09790

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)