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   27-MAR-2024, entry version 189.
DE   RecName: Full=3'(2'),5'-bisphosphate nucleotidase {ECO:0000303|PubMed:7809627};
DE            EC=3.1.3.7 {ECO:0000269|PubMed:10656801, ECO:0000269|PubMed:7809627};
DE   AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase;
DE   AltName: Full=3'-phosphoadenosine-5'-phosphate phosphatase {ECO:0000305};
DE            Short=3'-phosphoadenosine-5'-phosphatase {ECO:0000303|PubMed:12126627};
DE            Short=PAP phosphatase {ECO:0000305};
DE            Short=PAPase {ECO:0000303|PubMed:12126627};
DE   AltName: Full=DPNPase;
DE   AltName: Full=Halotolerance protein HAL2;
DE   AltName: Full=Methionine-requiring protein 22;
GN   Name=MET22; Synonyms=HAL2 {ECO:0000303|PubMed:7809627};
GN   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   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, AND ACTIVITY
RP   REGULATION.
RX   PubMed=7809627; DOI=10.1126/science.7809627;
RA   Murguia J.R., Belles J.M., Serrano R.;
RT   "A salt-sensitive 3'(2'),5'-bisphosphate nucleotidase involved in sulfate
RT   activation.";
RL   Science 267:232-234(1995).
RN   [9] {ECO:0007744|PDB:1QGX}
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND
RP   AMP, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP   VAL-70 AND GLU-238.
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).
RN   [10] {ECO:0007744|PDB:1K9Z, ECO:0007744|PDB:1KA0}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEXES WITH AMP AND ZN(2+).
RA   Patel S., Albert A., Blundell T.L.;
RT   "Hal2p: Ion selectivity and implications on inhibition mechanism.";
RL   Submitted (OCT-2001) to the PDB data bank.
RN   [11] {ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1KA1}
RP   X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEXES WITH AMP; ADENOSINE
RP   3',5'-BISPHOSPHATE; PHOSPHATE AND MAGNESIUM, COFACTOR, REACTION MECHANISM,
RP   AND ACTIVE SITE.
RX   PubMed=12126627; DOI=10.1016/s0022-2836(02)00564-8;
RA   Patel S., Martinez-Ripoll M., Blundell T.L., Albert A.;
RT   "Structural enzymology of Li(+)-sensitive/Mg(2+)-dependent phosphatases.";
RL   J. Mol. Biol. 320:1087-1094(2002).
CC   -!- FUNCTION: Phosphatase that converts adenosine 3'-phosphate 5'-
CC       phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-
CC       phosphoadenosine 5'-phosphate (PAP) to AMP. May regulate the flux of
CC       sulfur in the sulfur-activation pathway by converting PAPS to APS
CC       (PubMed:7809627). Involved in salt tolerance. Confers resistance to
CC       lithium. Shows no activity on inositol mono- and diphosphates, 3'-AMP,
CC       AMP, nicotinamide adenine dinucleotide phosphate (NADP), and p-
CC       nitrophenylphosphate (PubMed:7809627). {ECO:0000269|PubMed:7809627}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + H2O = adenosine 5'-phosphosulfate
CC         + phosphate; Xref=Rhea:RHEA:77639, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339; EC=3.1.3.7;
CC         Evidence={ECO:0000269|PubMed:7809627};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77640;
CC         Evidence={ECO:0000305|PubMed:7809627};
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         Evidence={ECO:0000269|PubMed:10656801, ECO:0000269|PubMed:7809627};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10041;
CC         Evidence={ECO:0000305|PubMed:7809627};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 2',5'-bisphosphate + H2O = AMP + phosphate;
CC         Xref=Rhea:RHEA:77643, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:194156, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC         Evidence={ECO:0000269|PubMed:7809627};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77644;
CC         Evidence={ECO:0000305|PubMed:7809627};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:7809627};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:12126627};
CC   -!- ACTIVITY REGULATION: Phosphatase activity is very sensitive to lithium
CC       and moderately sensitive to sodium. The inhibitory effects of lithium
CC       and sodium are overcome by high concentrations of potassium
CC       (PubMed:7809627). Lithium exerts its inhibitory action by blocking the
CC       products of the PAP hydrolysis at the active site (PubMed:10656801).
CC       {ECO:0000269|PubMed:10656801, ECO:0000269|PubMed:7809627}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4 uM for adenosine 3',5'-bisphosphate
CC         {ECO:0000269|PubMed:10656801};
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; 398.
DR   DIP; DIP-4072N; -.
DR   IntAct; P32179; 2.
DR   MINT; P32179; -.
DR   STRING; 4932.YOL064C; -.
DR   iPTMnet; P32179; -.
DR   MaxQB; P32179; -.
DR   PaxDb; 4932-YOL064C; -.
DR   PeptideAtlas; P32179; -.
DR   EnsemblFungi; YOL064C_mRNA; YOL064C; YOL064C.
DR   GeneID; 854090; -.
DR   KEGG; sce:YOL064C; -.
DR   AGR; SGD:S000005425; -.
DR   SGD; S000005425; MET22.
DR   VEuPathDB; FungiDB:YOL064C; -.
DR   eggNOG; KOG1528; Eukaryota.
DR   HOGENOM; CLU_033446_2_1_1; -.
DR   InParanoid; P32179; -.
DR   OMA; MSYQQER; -.
DR   OrthoDB; 5486961at2759; -.
DR   BioCyc; YEAST:YOL064C-MONOMER; -.
DR   BRENDA; 3.1.3.7; 984.
DR   SABIO-RK; P32179; -.
DR   BioGRID-ORCS; 854090; 4 hits in 10 CRISPR screens.
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:0042538; P:hyperosmotic salinity response; IMP:SGD.
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   CDD; cd01517; PAP_phosphatase; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
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   NCBIfam; TIGR01330; bisphos_HAL2; 1.
DR   PANTHER; PTHR43200:SF6; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE; 1.
DR   PANTHER; PTHR43200; PHOSPHATASE; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 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   ACT_SITE        49
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305|PubMed:12126627"
FT   ACT_SITE        147
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305|PubMed:12126627"
FT   BINDING         72
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:10656801,
FT                   ECO:0000269|PubMed:12126627, ECO:0007744|PDB:1K9Y,
FT                   ECO:0007744|PDB:1QGX"
FT   BINDING         72
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:10656801,
FT                   ECO:0000269|PubMed:12126627, ECO:0007744|PDB:1K9Y,
FT                   ECO:0007744|PDB:1QGX"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:10656801,
FT                   ECO:0000269|PubMed:12126627, ECO:0007744|PDB:1K9Y,
FT                   ECO:0007744|PDB:1QGX"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12126627,
FT                   ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1KA1"
FT   BINDING         144
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:10656801,
FT                   ECO:0000269|PubMed:12126627, ECO:0007744|PDB:1K9Y,
FT                   ECO:0007744|PDB:1QGX"
FT   BINDING         145
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12126627,
FT                   ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1KA1"
FT   BINDING         147
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000269|PubMed:12126627,
FT                   ECO:0007744|PDB:1KA1"
FT   BINDING         241
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000269|PubMed:12126627,
FT                   ECO:0007744|PDB:1KA1"
FT   BINDING         241
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:10656801,
FT                   ECO:0000269|PubMed:12126627, ECO:0000269|Ref.10,
FT                   ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1KA0,
FT                   ECO:0007744|PDB:1QGX"
FT   BINDING         264
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000269|PubMed:12126627,
FT                   ECO:0007744|PDB:1KA1"
FT   BINDING         264
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:10656801,
FT                   ECO:0000269|PubMed:12126627, ECO:0000269|Ref.10,
FT                   ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1KA0,
FT                   ECO:0007744|PDB:1QGX"
FT   BINDING         267
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000269|PubMed:12126627,
FT                   ECO:0007744|PDB:1KA1"
FT   BINDING         267
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:10656801,
FT                   ECO:0000269|PubMed:12126627, ECO:0000269|Ref.10,
FT                   ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1KA0,
FT                   ECO:0007744|PDB:1QGX"
FT   BINDING         281
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:1KA1"
FT   BINDING         281
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:10656801,
FT                   ECO:0000269|PubMed:12126627, ECO:0000269|Ref.10,
FT                   ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1KA0,
FT                   ECO:0007744|PDB:1QGX"
FT   BINDING         294
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000269|PubMed:12126627,
FT                   ECO:0007744|PDB:1KA1"
FT   BINDING         294
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:10656801,
FT                   ECO:0000269|PubMed:12126627, ECO:0000269|Ref.10,
FT                   ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1KA0,
FT                   ECO:0007744|PDB:1QGX"
FT   BINDING         294
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12126627,
FT                   ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1KA1"
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   MUTAGEN         70
FT                   /note="V->A: Increases levels of lithium and sodium
FT                   resistance while maintaining a relatively high specific
FT                   activity. Increases affinity for PAP."
FT                   /evidence="ECO:0000269|PubMed:10656801"
FT   MUTAGEN         238
FT                   /note="E->K: Increases levels of lithium and sodium
FT                   resistance while maintaining a relatively high specific
FT                   activity. 5-fold decrease in affinity for PAP."
FT                   /evidence="ECO:0000269|PubMed:10656801"
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
//