MET22_YEAST
ID MET22_YEAST Reviewed; 357 AA.
AC P32179; D6W203; Q6RFY5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase;
DE EC=3.1.3.7;
DE AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase;
DE AltName: Full=DPNPase;
DE AltName: Full=Halotolerance protein HAL2;
DE AltName: Full=Methionine-requiring protein 22;
GN Name=MET22; Synonyms=HAL2; OrderedLocusNames=YOL064C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8393782; DOI=10.1002/j.1460-2075.1993.tb05979.x;
RA Glaeser H.-U., Thomas D., Gaxiola R., Montrichard F., Surdin-Kerjan Y.,
RA Serrano R.;
RT "Salt tolerance and methionine biosynthesis in Saccharomyces cerevisiae
RT involve a putative phosphatase gene.";
RL EMBO J. 12:3105-3110(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Montrache;
RA Thanananta N., Apisitwanich S., Peyachoknagul S.;
RT "Cloning of HAL2 gene from Saccharomyces cerevisiae Montrache.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9178509;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<583::aid-yea111>3.0.co;2-y;
RA Tzermia M., Katsoulou C., Alexandraki D.;
RT "Sequence analysis of a 33.2 kb segment from the left arm of yeast
RT chromosome XV reveals eight known genes and ten new open reading frames
RT including homologues of ABC transporters, inositol phosphatases and human
RT expressed sequence tags.";
RL Yeast 13:583-589(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND
RP AMP.
RX PubMed=10656801; DOI=10.1006/jmbi.1999.3408;
RA Albert A., Yenush L., Gil-Mascarell M.R., Rodriguez P.L., Patel S.,
RA Martinez-Ripoll M., Blundell T.L., Serrano R.;
RT "X-ray structure of yeast Hal2p, a major target of lithium and sodium
RT toxicity, and identification of framework interactions determining cation
RT sensitivity.";
RL J. Mol. Biol. 295:927-938(2000).
CC -!- FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to
CC adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine
CC 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-
CC activation pathway by converting PAPS to APS. Involved in salt
CC tolerance. Confers resistance to lithium.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By salt stress.
CC -!- MISCELLANEOUS: Present with 7330 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; X72847; CAA51361.1; -; Genomic_DNA.
DR EMBL; AY500154; AAR89916.1; -; Genomic_DNA.
DR EMBL; Z74806; CAA99074.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10719.1; -; Genomic_DNA.
DR PIR; S35318; S35318.
DR RefSeq; NP_014577.1; NM_001183319.1.
DR PDB; 1K9Y; X-ray; 1.90 A; A=1-357.
DR PDB; 1K9Z; X-ray; 1.50 A; A=1-357.
DR PDB; 1KA0; X-ray; 1.80 A; A=1-357.
DR PDB; 1KA1; X-ray; 1.30 A; A=1-357.
DR PDB; 1QGX; X-ray; 1.60 A; A=1-357.
DR PDBsum; 1K9Y; -.
DR PDBsum; 1K9Z; -.
DR PDBsum; 1KA0; -.
DR PDBsum; 1KA1; -.
DR PDBsum; 1QGX; -.
DR AlphaFoldDB; P32179; -.
DR SMR; P32179; -.
DR BioGRID; 34337; 393.
DR DIP; DIP-4072N; -.
DR IntAct; P32179; 2.
DR MINT; P32179; -.
DR STRING; 4932.YOL064C; -.
DR iPTMnet; P32179; -.
DR MaxQB; P32179; -.
DR PaxDb; P32179; -.
DR PRIDE; P32179; -.
DR EnsemblFungi; YOL064C_mRNA; YOL064C; YOL064C.
DR GeneID; 854090; -.
DR KEGG; sce:YOL064C; -.
DR SGD; S000005425; MET22.
DR VEuPathDB; FungiDB:YOL064C; -.
DR eggNOG; KOG1528; Eukaryota.
DR HOGENOM; CLU_033446_2_1_1; -.
DR OMA; MSYQQER; -.
DR BioCyc; YEAST:YOL064C-MON; -.
DR BRENDA; 3.1.3.7; 984.
DR SABIO-RK; P32179; -.
DR EvolutionaryTrace; P32179; -.
DR PRO; PR:P32179; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P32179; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042578; F:phosphoric ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:SGD.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IMP:SGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; IMP:SGD.
DR InterPro; IPR006239; Bisphos_HAL2.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR TIGRFAMs; TIGR01330; bisphos_HAL2; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Lithium; Magnesium; Metal-binding;
KW Nucleus; Reference proteome; Stress response.
FT CHAIN 1..357
FT /note="3'(2'),5'-bisphosphate nucleotidase"
FT /id="PRO_0000142537"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 144..147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VARIANT 40
FT /note="N -> S (in strain: Montrache)"
FT VARIANT 61
FT /note="K -> M (in strain: Montrache)"
FT VARIANT 63
FT /note="N -> S (in strain: Montrache)"
FT VARIANT 308
FT /note="I -> V (in strain: Montrache)"
FT HELIX 4..30
FT /evidence="ECO:0007829|PDB:1KA1"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1KA1"
FT HELIX 47..63
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1KA1"
FT HELIX 80..100
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1KA1"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 134..145
FT /evidence="ECO:0007829|PDB:1KA1"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:1KA1"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:1KA1"
FT TURN 189..194
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:1KA1"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1K9Z"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1KA1"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1K9Z"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:1KA1"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:1KA1"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1KA1"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1KA1"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:1KA1"
FT HELIX 296..304
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:1KA1"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:1KA1"
FT HELIX 338..353
FT /evidence="ECO:0007829|PDB:1KA1"
SQ SEQUENCE 357 AA; 39149 MW; AB2E5F90B285702B CRC64;
MALERELLVA TQAVRKASLL TKRIQSEVIS HKDSTTITKN DNSPVTTGDY AAQTIIINAI
KSNFPDDKVV GEESSSGLSD AFVSGILNEI KANDEVYNKN YKKDDFLFTN DQFPLKSLED
VRQIIDFGNY EGGRKGRFWC LDPIDGTKGF LRGEQFAVCL ALIVDGVVQL GCIGCPNLVL
SSYGAQDLKG HESFGYIFRA VRGLGAFYSP SSDAESWTKI HVRHLKDTKD MITLEGVEKG
HSSHDEQTAI KNKLNISKSL HLDSQAKYCL LALGLADVYL RLPIKLSYQE KIWDHAAGNV
IVHEAGGIHT DAMEDVPLDF GNGRTLATKG VIASSGPREL HDLVVSTSCD VIQSRNA
