ID V7AHF7_PHAVU Unreviewed; 330 AA.
AC V7AHF7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase {ECO:0000256|ARBA:ARBA00012633, ECO:0000256|RuleBase:RU368076};
DE EC=3.1.3.7 {ECO:0000256|ARBA:ARBA00012633, ECO:0000256|RuleBase:RU368076};
DE Flags: Fragment;
GN ORFNames=PHAVU_011G148400g {ECO:0000313|EMBL:ESW05057.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW05057.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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. {ECO:0000256|RuleBase:RU368076}.
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|RuleBase:RU368076};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU368076};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759, ECO:0000256|RuleBase:RU368076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002298; ESW05057.1; -; Genomic_DNA.
DR RefSeq; XP_007133063.1; XM_007133001.1.
DR AlphaFoldDB; V7AHF7; -.
DR STRING; 3885.V7AHF7; -.
DR EnsemblPlants; ESW05057; ESW05057; PHAVU_011G148400g.
DR GeneID; 18616230; -.
DR Gramene; ESW05057; ESW05057; PHAVU_011G148400g.
DR KEGG; pvu:PHAVU_011G148400g; -.
DR eggNOG; KOG1528; Eukaryota.
DR OMA; WSSHVRY; -.
DR OrthoDB; 5486961at2759; -.
DR Proteomes; UP000000226; Chromosome 11.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043647; P:inositol phosphate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
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:SF24; PAP-SPECIFIC PHOSPHATASE HAL2-LIKE; 1.
DR PANTHER; PTHR43200; PHOSPHATASE; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368076};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU368076};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU368076};
KW Reference proteome {ECO:0000313|Proteomes:UP000000226}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ESW05057.1"
SQ SEQUENCE 330 AA; 35620 MW; F21070FE4C0F62AB CRC64;
DFSVQATISW LLSEIFGVQN VSIVAEEDIQ TISKDESASL LEDVVNTVNE SLAFASKYGL
QSPETTLGST EILEAIARCN STGGPRGRYW VLDPVDGTLG FVRGDQYAVA LALIEDGKVV
LGVLGCPNYP VKTEWLNYHY QHHQTAPQSS VTTPDTGGKG CVLYAKRGSG EAWLQSLIDG
EKMLEWPNHA KLIRVSSIDD PALATLCEPV ERANSNHSFT AGLAHSVGLR KQPLRVHSMV
KYAAIARGDA EIFMKFARSG YKEKIWDHAA GVVIVEEAGG VVTDAGGDPL DFSKGVYLEG
LDRGIIACSG LPLHHKFIAA VYASWDSSNL
//
