CYSQ_ECO57
ID CYSQ_ECO57 Reviewed; 246 AA.
AC Q8XCG6;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
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};
GN OrderedLocusNames=Z5825, ECs5192;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG59412.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38615.1; -; Genomic_DNA.
DR PIR; H86118; H86118.
DR PIR; H91277; H91277.
DR RefSeq; NP_313219.1; NC_002695.1.
DR RefSeq; WP_000886884.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XCG6; -.
DR SMR; Q8XCG6; -.
DR STRING; 155864.EDL933_5560; -.
DR PRIDE; Q8XCG6; -.
DR EnsemblBacteria; AAG59412; AAG59412; Z5825.
DR EnsemblBacteria; BAB38615; BAB38615; ECs_5192.
DR GeneID; 913943; -.
DR KEGG; ece:Z5825; -.
DR KEGG; ecs:ECs_5192; -.
DR PATRIC; fig|386585.9.peg.5427; -.
DR eggNOG; COG1218; Bacteria.
DR HOGENOM; CLU_044118_3_0_6; -.
DR OMA; SADCYPR; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome.
FT CHAIN 1..246
FT /note="3'(2'),5'-bisphosphate nucleotidase CysQ"
FT /id="PRO_0000142543"
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; 27160 MW; 1A2BD090DDAC8AD7 CRC64;
MLDQVCQLAR NAGDAIMQVY DGAKPMDVVS KADNSPVTAA DIAAHTVIMD GLRTLTPDIP
VLSEEDPPGW EVRQHWQRYW LVDPLDGTKE FIKRNGEFTV NIALIDHGKP ILGVVYAPVM
NVMYSAAEGK AWKEECGVRK QIQVRDARPP LVVISRSHAD AELKEYLQQL GEHQTTSIGS
SLKFCLVAEG QAQLYPRFGP TNIWDTAAGH AVAAAAGAHV HDWQGKPLDY TPRESFLNPG
FRVSIY
