ID   A0A2S0N671_9PROT        Unreviewed;       271 AA.
AC   A0A2S0N671;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   07-NOV-2018, entry version 4.
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; Proteobacteria; Alphaproteobacteria; 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: Adenosine 3',5'-bisphosphate + H(2)O =
CC       adenosine 5'-phosphate + phosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_02095}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02095};
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-
CC       Rule:MF_02095}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       CysQ family. {ECO:0000256|HAMAP-Rule:MF_02095}.
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DR   EMBL; CP027668; AVO43642.1; -; Genomic_DNA.
DR   KEGG; phr:C6569_00285; -.
DR   KO; K01082; -.
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 phosphorylation; IEA:InterPro.
DR   GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro.
DR   HAMAP; MF_02095; CysQ; 1.
DR   InterPro; IPR006240; CysQ.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Complete proteome {ECO:0000313|Proteomes:UP000237889};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237889}.
FT   REGION       90     93       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_02095}.
FT   METAL        69     69       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        88     88       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        88     88       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        90     90       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02095}.
FT   METAL        91     91       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL       221    221       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   BINDING      69     69       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   BINDING     221    221       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                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
//