HAL21_CANAW
ID HAL21_CANAW Reviewed; 364 AA.
AC P0CY21; P46594; Q59WV3; Q59XQ8;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase 1;
DE EC=3.1.3.7;
DE AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase 1;
DE AltName: Full=DPNPase 1;
DE AltName: Full=Halotolerance protein HAL21;
GN Name=HAL21; Synonyms=MET222;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 260-364.
RC STRAIN=WO-1;
RX PubMed=7725800; DOI=10.1002/yea.320101214;
RA Sychorova H., Souciet J.-L.;
RT "CAN1, a gene encoding a permease for basic amino acids in Candida
RT albicans.";
RL Yeast 10:1647-1651(1994).
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 (By similarity). {ECO:0000250}.
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; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; CM000312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X76689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0CY21; -.
DR SMR; P0CY21; -.
DR STRING; 5476.P0CY21; -.
DR PRIDE; P0CY21; -.
DR Proteomes; UP000001429; Chromosome 6.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro.
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 TIGRFAMs; TIGR01330; bisphos_HAL2; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..364
FT /note="3'(2'),5'-bisphosphate nucleotidase 1"
FT /id="PRO_0000413037"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 143..146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 334
FT /note="D -> N (in Ref. 2; X76689)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 39359 MW; 70687AABBB2C2247 CRC64;
MSHTTHPYQK ELEVATLAVK RASLLTKQLS DSIVQTARSG TLTKDDKSPV TIGDFALQAI
INHAIKLNFP SDEIVGEEDS QELQENSSLA DQVLSLIIKI QQETSVYNDV VGTLTDKNKV
FQSIDYGNSQ GGLKGRFWAL DPIDGTKGFL RGDQFAVCLA LIEDGKVVLG VIGCPNLLEN
IVSNEEHSGV VGGLYSAVKG VGSFYSELFK EGAEPLSQQK PIKMQNHTNP SQLKVVEGVE
KGHSSHSTQA EIKAKLGFDP TTVAKQTVNL DSQVKYCVLA SGQADIYLRL PVSDTYREKI
WDHAAGNILI YESGGQVGDV TGAPLNFGNG RTLDSKGVIA ANKEIFDKVI DAVTEIRKSS
TPRV
