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P32179

- MET22_YEAST

UniProt

P32179 - MET22_YEAST

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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: 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi72 – 721Magnesium 1
Binding sitei72 – 721SubstrateBy similarity
Metal bindingi142 – 1421Magnesium 1
Metal bindingi142 – 1421Magnesium 2
Metal bindingi144 – 1441Magnesium 1; via carbonyl oxygen
Metal bindingi145 – 1451Magnesium 2
Metal bindingi294 – 2941Magnesium 2
Binding sitei294 – 2941SubstrateBy similarity

GO - Molecular functioni

  1. 3'(2'),5'-bisphosphate nucleotidase activity Source: SGD
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. hyperosmotic salinity response Source: SGD
  3. methionine biosynthetic process Source: SGD
  4. phosphatidylinositol phosphorylation Source: InterPro
  5. 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.

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
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOL064c.
SGDiS000005425. MET22.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3573573'(2'),5'-bisphosphate nucleotidasePRO_0000142537Add
BLAST

Proteomic databases

MaxQBiP32179.
PaxDbiP32179.
PeptideAtlasiP32179.

Expressioni

Inductioni

By salt stress.

Gene expression databases

GenevestigatoriP32179.

Interactioni

Protein-protein interaction databases

BioGridi34337. 142 interactions.
DIPiDIP-4072N.
IntActiP32179. 1 interaction.
MINTiMINT-506588.
STRINGi4932.YOL064C.

Structurei

Secondary structure

1
357
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 3027Combined sources
Turni31 – 344Combined sources
Beta strandi35 – 384Combined sources
Beta strandi44 – 463Combined sources
Helixi47 – 6317Combined sources
Beta strandi69 – 724Combined sources
Helixi80 – 10021Combined sources
Beta strandi111 – 1133Combined sources
Helixi118 – 1269Combined sources
Beta strandi134 – 14512Combined sources
Helixi147 – 1515Combined sources
Beta strandi157 – 1648Combined sources
Beta strandi167 – 1759Combined sources
Helixi180 – 1834Combined sources
Turni189 – 1946Combined sources
Beta strandi196 – 2016Combined sources
Turni202 – 2043Combined sources
Beta strandi206 – 2105Combined sources
Turni211 – 2133Combined sources
Beta strandi218 – 2203Combined sources
Helixi228 – 2303Combined sources
Beta strandi232 – 2354Combined sources
Turni239 – 2413Combined sources
Helixi244 – 25310Combined sources
Beta strandi258 – 2614Combined sources
Helixi266 – 2738Combined sources
Beta strandi277 – 2815Combined sources
Helixi292 – 2943Combined sources
Helixi296 – 3049Combined sources
Beta strandi308 – 3103Combined sources
Beta strandi312 – 3143Combined sources
Beta strandi322 – 3254Combined sources
Beta strandi327 – 3293Combined sources
Beta strandi331 – 3355Combined sources
Helixi338 – 35316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-355.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32179.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 1474Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

eggNOGiCOG1218.
KOiK01082.
OMAiGRFWCLD.
OrthoDBiEOG7VB2R7.

Family and domain databases

InterProiIPR006239. Bisphos_HAL2.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 1 hit.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401N → S in strain: Montrache.
Natural varianti61 – 611K → M in strain: Montrache.
Natural varianti63 – 631N → S in strain: Montrache.
Natural varianti308 – 3081I → V in strain: Montrache.

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 .
PIRi S35318.
RefSeqi NP_014577.1. NM_001183319.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P32179.
SMRi P32179. Positions 2-355.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34337. 142 interactions.
DIPi DIP-4072N.
IntActi P32179. 1 interaction.
MINTi MINT-506588.
STRINGi 4932.YOL064C.

Proteomic databases

MaxQBi P32179.
PaxDbi P32179.
PeptideAtlasi P32179.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOL064C ; YOL064C ; YOL064C .
GeneIDi 854090.
KEGGi sce:YOL064C.

Organism-specific databases

CYGDi YOL064c.
SGDi S000005425. MET22.

Phylogenomic databases

eggNOGi COG1218.
KOi K01082.
OMAi GRFWCLD.
OrthoDBi EOG7VB2R7.

Enzyme and pathway databases

BioCyci YEAST:YOL064C-MONOMER.

Miscellaneous databases

EvolutionaryTracei P32179.
NextBioi 975743.

Gene expression databases

Genevestigatori P32179.

Family and domain databases

InterProi IPR006239. Bisphos_HAL2.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view ]
PANTHERi PTHR20854. PTHR20854. 1 hit.
Pfami PF00459. Inositol_P. 1 hit.
[Graphical view ]
PRINTSi PR00377. IMPHPHTASES.
TIGRFAMsi TIGR01330. bisphos_HAL2. 1 hit.
PROSITEi PS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND AMP.

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 26, 2014
This is version 129 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

External Data

Dasty 3