Reviewed, UniProtKB/Swiss-Prot P32179 (HAL2_YEAST)

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 HAL2

Gene names

Name:	HAL2
Synonyms:	MET22
Ordered Locus Names:	YOL064C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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. Involved in salt tolerance. Confers resistance to lithium.
Catalytic activity	Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
Cofactor	Magnesium.
Induction	By salt stress.
Miscellaneous	Present with 7330 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the inositol monophosphatase family.

Ontologies

Keywords
Biological process	Stress response
Ligand	Lithium Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	hyperosmotic salinity response Traceable author statement. Source: SGD methionine biosynthetic process Ref.1 Traceable author statement. Source: SGD response to drug Inferred from mutant phenotype. Source: SGD sulfate assimilation Traceable author statement. Source: SGD
Cellular component	cytoplasm Ref.6 Inferred from direct assay. Source: SGD
Molecular function	3'(2'),5'-bisphosphate nucleotidase activity Traceable author statement. Source: SGD inositol or phosphatidylinositol phosphatase activity Inferred from electronic annotation. Source: InterPro lithium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 357

357

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

PRO_0000142537

Sites

Metal binding

72

1

Magnesium 1

Metal binding

142

1

Magnesium 1

Metal binding

142

1

Magnesium 2

Metal binding

144

1

Magnesium 1; via carbonyl oxygen

Metal binding

145

1

Magnesium 2

Metal binding

294

1

Magnesium 2

Natural variations

Natural variant

40

1

N → S in strain: Montrache.

Natural variant

61

1

K → M in strain: Montrache.

Natural variant

63

1

N → S in strain: Montrache.

Natural variant

308

1

I → V in strain: Montrache.

Secondary structure

1

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357

Helix Strand Turn

Details...

Helix

4 – 30

27

Turn

31 – 34

4

Beta strand

35 – 38

4

Beta strand

44 – 46

3

Helix

47 – 63

17

Beta strand

69 – 72

4

Helix

80 – 100

21

Beta strand

111 – 113

3

Helix

118 – 126

9

Beta strand

134 – 145

12

Helix

147 – 151

5

Beta strand

157 – 164

8

Beta strand

167 – 175

9

Helix

180 – 183

4

Turn

189 – 194

6

Beta strand

196 – 201

6

Beta strand

206 – 210

5

Turn

211 – 213

3

Helix

228 – 230

3

Beta strand

232 – 235

4

Turn

239 – 241

3

Helix

244 – 253

10

Beta strand

258 – 261

4

Helix

266 – 273

8

Beta strand

277 – 281

5

Helix

292 – 294

3

Helix

296 – 304

9

Beta strand

308 – 310

3

Beta strand

312 – 314

3

Beta strand

322 – 325

4

Beta strand

327 – 329

3

Beta strand

331 – 335

5

Helix

338 – 353

16

Sequences

	Sequence		Length	Mass (Da)
	P32179-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: AB2E5F90B285702B	FASTA	357	39,149
	10 20 30 40 50 60 MALERELLVA TQAVRKASLL TKRIQSEVIS HKDSTTITKN DNSPVTTGDY AAQTIIINAI 70 80 90 100 110 120 KSNFPDDKVV GEESSSGLSD AFVSGILNEI KANDEVYNKN YKKDDFLFTN DQFPLKSLED 130 140 150 160 170 180 VRQIIDFGNY EGGRKGRFWC LDPIDGTKGF LRGEQFAVCL ALIVDGVVQL GCIGCPNLVL 190 200 210 220 230 240 SSYGAQDLKG HESFGYIFRA VRGLGAFYSP SSDAESWTKI HVRHLKDTKD MITLEGVEKG 250 260 270 280 290 300 HSSHDEQTAI KNKLNISKSL HLDSQAKYCL LALGLADVYL RLPIKLSYQE KIWDHAAGNV 310 320 330 340 350 IVHEAGGIHT DAMEDVPLDF GNGRTLATKG VIASSGPREL HDLVVSTSCD VIQSRNA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Salt tolerance and methionine biosynthesis in Saccharomyces cerevisiae involve a putative phosphatase gene." Glaeser H.-U., Thomas D., Gaxiola R., Montrichard F., Surdin-Kerjan Y., Serrano R. EMBO J. 12:3105-3110(1993) [PubMed: 8393782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning of HAL2 gene from Saccharomyces cerevisiae Montrache." Thanananta N., Apisitwanich S., Peyachoknagul S. Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Montrache.
[3]	"Sequence analysis of a 33.2 kb segment from the left arm of yeast chromosome XV reveals eight known genes and ten new open reading frames including homologues of ABC transporters, inositol phosphatases and human expressed sequence tags." Tzermia M., Katsoulou C., Alexandraki D. Yeast 13:583-589(1997) [PubMed: 9178509] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"X-ray structure of yeast Hal2p, a major target of lithium and sodium toxicity, and identification of framework interactions determining cation sensitivity." Albert A., Yenush L., Gil-Mascarell M.R., Rodriguez P.L., Patel S., Martinez-Ripoll M., Blundell T.L., Serrano R. J. Mol. Biol. 295:927-938(2000) [PubMed: 10656801] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND AMP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X72847 Genomic DNA. Translation: CAA51361.1.
AY500154 Genomic DNA. Translation: AAR89916.1.
Z74806 Genomic DNA. Translation: CAA99074.1.

PIR

S35318.

RefSeq

NP_014577.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K9Y	X-ray	1.90	A	1-357	[»]
1K9Z	X-ray	1.50	A	1-357	[»]
1KA0	X-ray	1.80	A	1-357	[»]
1KA1	X-ray	1.30	A	1-357	[»]
1QGX	X-ray	1.60	A	1-357	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:4072N.

IntAct

P32179. 4 interactions.

Proteomic databases

PeptideAtlas

P32179.

PRIDE

P32179.

Genome annotation databases

Ensembl

YOL064C. Saccharomyces cerevisiae. [Contig view]

GeneID

854090.

GenomeReviews

Gene locus YOL064C in contig Y13140_GR.

KEGG

sce:YOL064C.

NMPDR

fig|4932.3.peg.5669.

Organism-specific databases

CYGD

YOL064c.

SGD

S000005425. MET22.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P32179.

OMA

P32179. ENIWDHA.

Enzyme and pathway databases

BRENDA

3.1.3.7. 250.

Gene expression databases

GermOnline

YOL064C. Saccharomyces cerevisiae.

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...

Other Resources

DrugBank

DB00131. Adenosine monophosphate.

NextBio

975743.

Entry information

Entry name

HAL2_YEAST

Accession

Primary (citable) accession number: P32179
Secondary accession number(s): Q6RFY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)