CYSQ_ECOL6
ID CYSQ_ECOL6 Reviewed; 246 AA.
AC Q8FAG5;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase CysQ {ECO:0000255|HAMAP-Rule:MF_02095};
DE EC=3.1.3.7 {ECO:0000255|HAMAP-Rule:MF_02095};
DE AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_02095};
DE AltName: Full=3'-phosphoadenosine 5'-phosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_02095};
DE Short=PAP phosphatase {ECO:0000255|HAMAP-Rule:MF_02095};
GN Name=cysQ {ECO:0000255|HAMAP-Rule:MF_02095}; OrderedLocusNames=c5313;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_02095};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02095};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02095}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02095}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_02095}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. CysQ
CC family. {ECO:0000255|HAMAP-Rule:MF_02095, ECO:0000305}.
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DR EMBL; AE014075; AAN83734.1; -; Genomic_DNA.
DR RefSeq; WP_000886909.1; NC_004431.1.
DR AlphaFoldDB; Q8FAG5; -.
DR SMR; Q8FAG5; -.
DR STRING; 199310.c5313; -.
DR EnsemblBacteria; AAN83734; AAN83734; c5313.
DR KEGG; ecc:c5313; -.
DR eggNOG; COG1218; Bacteria.
DR HOGENOM; CLU_044118_3_0_6; -.
DR OMA; SADCYPR; -.
DR BioCyc; ECOL199310:C5313-MON; -.
DR Proteomes; UP000001410; 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: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 HAMAP; MF_02095; CysQ; 1.
DR InterPro; IPR006240; CysQ.
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; TIGR01331; bisphos_cysQ; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Magnesium; Membrane;
KW Metal-binding.
FT CHAIN 1..246
FT /note="3'(2'),5'-bisphosphate nucleotidase CysQ"
FT /id="PRO_0000142542"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095"
FT BINDING 85..88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095"
SQ SEQUENCE 246 AA; 27190 MW; 215BCD3717D02D18 CRC64;
MLDQVCQLAR NAGDAIMQVY DGTKPMDVVS KADNSPVTAA DIAAHTVIMD GLRTLTPDIP
VLSEEDPPGW EVRQHWQRYW LVDPLDGTKE FIKRNGEFTV NIALIDHGKP ILGVVYAPVM
NVMYSAAEGK AWKEECGVRK QIQVRDARPP LVVISRSHAD AELKEYLQQL GEHQTTSIGS
SLKFCLVAEG QAQLYPRFGP TNIWDTAAGH AVAAAAGAHV HDWQGKPLDY TPRESFLNPG
FRVSIY
