ID A0A022Q805_ERYGU Unreviewed; 408 AA.
AC A0A022Q805;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase {ECO:0000256|ARBA:ARBA00012633};
DE EC=3.1.3.7 {ECO:0000256|ARBA:ARBA00012633};
GN ORFNames=MIMGU_mgv1a007420mg {ECO:0000313|EMBL:EYU23739.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU23739.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU23739.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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:0000256|ARBA:ARBA00001625};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759}.
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DR EMBL; KI632154; EYU23739.1; -; Genomic_DNA.
DR RefSeq; XP_012853709.1; XM_012998255.1.
DR AlphaFoldDB; A0A022Q805; -.
DR STRING; 4155.A0A022Q805; -.
DR GeneID; 105973236; -.
DR KEGG; egt:105973236; -.
DR eggNOG; KOG1528; Eukaryota.
DR OMA; MSYQQER; -.
DR OrthoDB; 5486961at2759; -.
DR PhylomeDB; A0A022Q805; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
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 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030748}.
FT REGION 49..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 408 AA; 43964 MW; 2B46563451F7E170 CRC64;
MSVSIGQTPL IRVVSHSLHI NAITVTSPHS ISKRFPFIFS LHRSTTATPP PNLRAVRRRS
SSSSSASTMS YDRQLAAAKK AASLASRLCQ KVQKALLQSD VQSKSDKSPV TVADYGSQAL
VSLVLGKELP SFPFSLVAEE DSEDLRKEES RETLHRITEL VNETLASDGT IDISPLSEED
VLKAIDNGKS EGGPHGQHWV LDPIDGTKGF VRGDQYAIAL GLLDEGKVVL GVLACPNLPM
ASDEKKGCLF YAQIDAGTYV QSLDGSPPTK VHVSTIENPE EASFFESYEA AHSLHELSSS
IAKKLGVKAP PVRIDSQAKY GALSRGDGAI YLRFPHKGYR EKIWDHAAGY MVVAEAGGVV
TDAGGNPLDF SKGRYLDLDT GIIVTNKKLM PALLKAVQDS IHERSSSL
//
