ID A0A2S0N671_9HYPH Unreviewed; 271 AA. AC A0A2S0N671; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 02-OCT-2024, entry version 21. DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase CysQ {ECO:0000256|HAMAP-Rule:MF_02095}; DE EC=3.1.3.7 {ECO:0000256|HAMAP-Rule:MF_02095}; DE AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase {ECO:0000256|HAMAP-Rule:MF_02095}; DE AltName: Full=3'-phosphoadenosine 5'-phosphate phosphatase {ECO:0000256|HAMAP-Rule:MF_02095}; DE Short=PAP phosphatase {ECO:0000256|HAMAP-Rule:MF_02095}; GN Name=cysQ {ECO:0000256|HAMAP-Rule:MF_02095}; GN ORFNames=C6569_00285 {ECO:0000313|EMBL:AVO43642.1}; OS Phreatobacter cathodiphilus. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Phreatobacteraceae; Phreatobacter. OX NCBI_TaxID=1868589 {ECO:0000313|EMBL:AVO43642.1, ECO:0000313|Proteomes:UP000237889}; RN [1] {ECO:0000313|EMBL:AVO43642.1, ECO:0000313|Proteomes:UP000237889} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S-12 {ECO:0000313|EMBL:AVO43642.1, RC ECO:0000313|Proteomes:UP000237889}; RA Kim S.-J., Heo J., Kwon S.-W.; RT "Genome sequencing of Phreatobacter sp."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Converts adenosine-3',5'-bisphosphate (PAP) to AMP. CC {ECO:0000256|HAMAP-Rule:MF_02095}. 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|HAMAP-Rule:MF_02095}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02095, CC ECO:0000256|PIRSR:PIRSR600760-2}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_02095}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_02095}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_02095}. CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. CysQ CC family. {ECO:0000256|ARBA:ARBA00005289, ECO:0000256|HAMAP- CC Rule:MF_02095}. 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; CP027668; AVO43642.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2S0N671; -. DR KEGG; phr:C6569_00285; -. DR OrthoDB; 9785695at2; -. DR Proteomes; UP000237889; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro. DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro. DR CDD; cd01638; CysQ; 1. DR Gene3D; 3.40.190.80; -; 1. DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1. DR HAMAP; MF_02095; CysQ; 1. DR InterPro; IPR006240; CysQ. DR InterPro; IPR050725; CysQ/Inositol_MonoPase. DR InterPro; IPR000760; Inositol_monophosphatase-like. DR InterPro; IPR020550; Inositol_monophosphatase_CS. DR PANTHER; PTHR43028; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE 1; 1. DR PANTHER; PTHR43028:SF5; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE 1; 1. DR Pfam; PF00459; Inositol_P; 1. DR PRINTS; PR00377; IMPHPHTASES. DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1. DR PROSITE; PS00630; IMP_2; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP- KW Rule:MF_02095}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_02095}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_02095}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02095, ECO:0000256|PIRSR:PIRSR600760- KW 2}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02095}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02095, KW ECO:0000256|PIRSR:PIRSR600760-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000237889}. FT BINDING 69 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095" FT BINDING 69 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" FT BINDING 69 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095" FT BINDING 88 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095" FT BINDING 88 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" FT BINDING 88 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095" FT BINDING 90..93 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095" FT BINDING 90 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" FT BINDING 90 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095" FT BINDING 91 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095" FT BINDING 91 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" FT BINDING 221 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095" FT BINDING 221 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" FT BINDING 221 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095" SQ SEQUENCE 271 AA; 27745 MW; 7A84CC19C46BB290 CRC64; MSTDFTDARL LDALGTLAST AGAAIMAHYG GASSIKSDGS PVTAADHAAE QVILAGLAGL LPEVPVLAEE AAAAGRWPAS TRMLVAVDPL DGTREFISQN GEFTVNIGLI ADGRPVAGVV FAPALSRLWL GAGSKAEAME LPPGAPISAA TRRRTIRTRP LPAGGPVALV SRSHPDAATS AYYAGRGIGE QRPVGSSLKY TLIAEGEADV SARFASITEW DIAAAHAVLA AAGGEMTQPD GAPLVYGRAE RQFRTDHFIA CSGAYAAAGR R //