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Protein

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

Gene

MET22

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Involved in salt tolerance. Confers resistance to lithium.

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi72Magnesium 11
Binding sitei72SubstrateBy similarity1
Metal bindingi142Magnesium 11
Metal bindingi142Magnesium 21
Metal bindingi144Magnesium 1; via carbonyl oxygen1
Metal bindingi145Magnesium 21
Metal bindingi294Magnesium 21
Binding sitei294SubstrateBy similarity1

GO - Molecular functioni

  • 3'(2'),5'-bisphosphate nucleotidase activity Source: SGD
  • magnesium ion binding Source: GO_Central

GO - Biological processi

  • hyperosmotic salinity response Source: SGD
  • methionine biosynthetic process Source: SGD
  • phosphatidylinositol phosphorylation Source: InterPro
  • sulfate assimilation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Stress response

Keywords - Ligandi

Lithium, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YOL064C-MONOMER.
BRENDAi3.1.3.7. 984.

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 HAL2
Methionine-requiring protein 22
Gene namesi
Name:MET22
Synonyms:HAL2
Ordered Locus Names:YOL064C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL064C.
SGDiS000005425. MET22.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001425371 – 3573'(2'),5'-bisphosphate nucleotidaseAdd BLAST357

Proteomic databases

MaxQBiP32179.
PRIDEiP32179.

Expressioni

Inductioni

By salt stress.

Interactioni

Protein-protein interaction databases

BioGridi34337. 142 interactors.
DIPiDIP-4072N.
IntActiP32179. 1 interactor.
MINTiMINT-506588.

Structurei

Secondary structure

1357
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 30Combined sources27
Turni31 – 34Combined sources4
Beta strandi35 – 38Combined sources4
Beta strandi44 – 46Combined sources3
Helixi47 – 63Combined sources17
Beta strandi69 – 72Combined sources4
Helixi80 – 100Combined sources21
Beta strandi111 – 113Combined sources3
Helixi118 – 126Combined sources9
Beta strandi134 – 145Combined sources12
Helixi147 – 151Combined sources5
Beta strandi157 – 164Combined sources8
Beta strandi167 – 175Combined sources9
Helixi180 – 183Combined sources4
Turni189 – 194Combined sources6
Beta strandi196 – 201Combined sources6
Turni202 – 204Combined sources3
Beta strandi206 – 210Combined sources5
Turni211 – 213Combined sources3
Beta strandi218 – 220Combined sources3
Helixi228 – 230Combined sources3
Beta strandi232 – 235Combined sources4
Turni239 – 241Combined sources3
Helixi244 – 253Combined sources10
Beta strandi258 – 261Combined sources4
Helixi266 – 273Combined sources8
Beta strandi277 – 281Combined sources5
Helixi292 – 294Combined sources3
Helixi296 – 304Combined sources9
Beta strandi308 – 310Combined sources3
Beta strandi312 – 314Combined sources3
Beta strandi322 – 325Combined sources4
Beta strandi327 – 329Combined sources3
Beta strandi331 – 335Combined sources5
Helixi338 – 353Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K9YX-ray1.90A1-357[»]
1K9ZX-ray1.50A1-357[»]
1KA0X-ray1.80A1-357[»]
1KA1X-ray1.30A1-357[»]
1QGXX-ray1.60A1-357[»]
ProteinModelPortaliP32179.
SMRiP32179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32179.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 147Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

KOiK01082.
OMAiKANDEVY.
OrthoDBiEOG092C2J9G.

Family and domain databases

InterProiIPR006239. Bisphos_HAL2.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase-like.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 3 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.

P32179-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALERELLVA TQAVRKASLL TKRIQSEVIS HKDSTTITKN DNSPVTTGDY
60 70 80 90 100
AAQTIIINAI KSNFPDDKVV GEESSSGLSD AFVSGILNEI KANDEVYNKN
110 120 130 140 150
YKKDDFLFTN DQFPLKSLED VRQIIDFGNY EGGRKGRFWC LDPIDGTKGF
160 170 180 190 200
LRGEQFAVCL ALIVDGVVQL GCIGCPNLVL SSYGAQDLKG HESFGYIFRA
210 220 230 240 250
VRGLGAFYSP SSDAESWTKI HVRHLKDTKD MITLEGVEKG HSSHDEQTAI
260 270 280 290 300
KNKLNISKSL HLDSQAKYCL LALGLADVYL RLPIKLSYQE KIWDHAAGNV
310 320 330 340 350
IVHEAGGIHT DAMEDVPLDF GNGRTLATKG VIASSGPREL HDLVVSTSCD

VIQSRNA
Length:357
Mass (Da):39,149
Last modified:October 1, 1993 - v1
Checksum:iAB2E5F90B285702B
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti40N → S in strain: Montrache. 1
Natural varianti61K → M in strain: Montrache. 1
Natural varianti63N → S in strain: Montrache. 1
Natural varianti308I → V in strain: Montrache. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72847 Genomic DNA. Translation: CAA51361.1.
AY500154 Genomic DNA. Translation: AAR89916.1.
Z74806 Genomic DNA. Translation: CAA99074.1.
BK006948 Genomic DNA. Translation: DAA10719.1.
PIRiS35318.
RefSeqiNP_014577.1. NM_001183319.1.

Genome annotation databases

EnsemblFungiiYOL064C; YOL064C; YOL064C.
GeneIDi854090.
KEGGisce:YOL064C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72847 Genomic DNA. Translation: CAA51361.1.
AY500154 Genomic DNA. Translation: AAR89916.1.
Z74806 Genomic DNA. Translation: CAA99074.1.
BK006948 Genomic DNA. Translation: DAA10719.1.
PIRiS35318.
RefSeqiNP_014577.1. NM_001183319.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K9YX-ray1.90A1-357[»]
1K9ZX-ray1.50A1-357[»]
1KA0X-ray1.80A1-357[»]
1KA1X-ray1.30A1-357[»]
1QGXX-ray1.60A1-357[»]
ProteinModelPortaliP32179.
SMRiP32179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34337. 142 interactors.
DIPiDIP-4072N.
IntActiP32179. 1 interactor.
MINTiMINT-506588.

Proteomic databases

MaxQBiP32179.
PRIDEiP32179.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL064C; YOL064C; YOL064C.
GeneIDi854090.
KEGGisce:YOL064C.

Organism-specific databases

EuPathDBiFungiDB:YOL064C.
SGDiS000005425. MET22.

Phylogenomic databases

KOiK01082.
OMAiKANDEVY.
OrthoDBiEOG092C2J9G.

Enzyme and pathway databases

BioCyciYEAST:YOL064C-MONOMER.
BRENDAi3.1.3.7. 984.

Miscellaneous databases

EvolutionaryTraceiP32179.
PROiP32179.

Family and domain databases

InterProiIPR006239. Bisphos_HAL2.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase-like.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 3 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...

Entry informationi

Entry nameiMET22_YEAST
AccessioniPrimary (citable) accession number: P32179
Secondary accession number(s): D6W203, Q6RFY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 30, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7330 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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.