Q55F34 (DPNP_DICDI) Reviewed, UniProtKB/Swiss-Prot

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
Inositol polyphosphate 1-phosphatase
Short name=IPPase
Inositol-1,4-bisphosphate 1-phosphatase
EC=3.1.3.57

Gene names

ORF Names:

DDB_G0268652

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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. Is also able to hydrolyze inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate By similarity.
Catalytic activity	Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate. 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate.
Cofactor	Magnesium By similarity.
Sequence similarities	Belongs to the inositol monophosphatase family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	sulfur compound metabolic process Inferred from sequence or structural similarity. Source: dictyBase
Molecular function	3'(2'),5'-bisphosphate nucleotidase activity Inferred from sequence or structural similarity. Source: dictyBase inositol-1,4-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC metal 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 – 332	332	3'(2'),5'-bisphosphate nucleotidase		PRO_0000327519
Regions
	Region	131 – 134	4	Substrate binding By similarity
Sites
	Metal binding	73	1	Magnesium 1 By similarity
	Metal binding	129	1	Magnesium 1 By similarity
	Metal binding	129	1	Magnesium 2 By similarity
	Metal binding	131	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	132	1	Magnesium 2 By similarity
	Metal binding	274	1	Magnesium 2 By similarity
	Binding site	73	1	Substrate By similarity
	Binding site	274	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55F34 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 56F8D137C9244277	FASTA	332	36,888
	10 20 30 40 50 60 MSLCNLAKIR SVAIKAVEKA CIACLDIQKQ LISEDTINKK DQSPVTVGDY TVQALVINEL 70 80 90 100 110 120 LKGLDEEYPI IAEEDSKTLS SQKDVESKVL SFFNRYSNES FVESQLSSLL DKGNKKKDLN 130 140 150 160 170 180 SSNRWWTLDP IDGTLGFLRK DQYAVALALM EDNKPILGIL GCPNLPVSKG STEKGCIFVG 190 200 210 220 230 240 LKNKGSFMIK LSNLDQEEPI KVSNQSDPTK AIFTESFVSR GFGHELNQKI SNSMGVTAEP 250 260 270 280 290 300 LKIDSQCKYA MVARGDSDCY LRLTQLDYKE CIWDHAAGHI IVEEAGGIVT DFKKQQLDYS 310 320 330 KGFKLENNVG IVCSNKLLND SLFDSIKKSI QF

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000004 Genomic DNA. Translation: EAL72915.1.
RefSeq	XP_646836.1. XM_641744.1.
3D structure databases
HSSP	HSSP built from PDB template 1KA1 based on UniProtKB P32179.
ProteinModelPortal	Q55F34.
ModBase	Search...
Protein-protein interaction databases
STRING	Q55F34.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0238884; DDB0238884; DDB_G0268652.
GeneID	8616518.
KEGG	ddi:DDB_G0268652.
Organism-specific databases
dictyBase	DDB_G0268652. ippB.
Phylogenomic databases
eggNOG	KOG1528.
GeneTree	EPrGT00050000006003.
HOGENOM	HBG599916.
OMA	VYASWES.
PhylomeDB	Q55F34.
ProtClustDB	CLSZ2431470.
Family and domain databases
InterPro	IPR006239. Bisphos_HAL2. IPR020583. Inositol_monoP_metal-BS. IPR000760. Inositol_monophosphatase. IPR020550. Inositol_monophosphatase_CS. [Graphical view]
KO	K01082.
PANTHER	PTHR20854. Inositol_P. 1 hit.
Pfam	PF00459. Inositol_P. 1 hit. [Graphical view]
PRINTS	PR00377. IMPHPHTASES.
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_DICDI

Accession

Primary (citable) accession number: Q55F34

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)