ID CYSQ_HAEIN Reviewed; 269 AA. AC P44332; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 2. DT 28-JAN-2026, entry version 136. 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=HI_0559; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22214.1; Type=Frameshift; Evidence={ECO:0000305}; 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; L42023; AAC22214.1; ALT_FRAME; Genomic_DNA. DR PIR; F64077; F64077. DR AlphaFoldDB; P44332; -. DR SMR; P44332; -. DR STRING; 71421.HI_0559; -. DR EnsemblBacteria; AAC22214; AAC22214; HI_0559. DR KEGG; hin:HI_0559; -. DR PATRIC; fig|71421.8.peg.579; -. DR eggNOG; COG1218; Bacteria. DR HOGENOM; CLU_044118_3_0_6; -. DR OrthoDB; 9785695at2; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IBA:GO_Central. DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro. DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central. DR CDD; cd01638; CysQ; 1. DR FunFam; 3.30.540.10:FF:000007; 3'(2'),5'-bisphosphate nucleotidase 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; IPR020583; Inositol_monoP_metal-BS. DR InterPro; IPR000760; Inositol_monophosphatase-like. DR InterPro; IPR020550; Inositol_monophosphatase_CS. DR NCBIfam; TIGR01331; bisphos_cysQ; 1. DR PANTHER; PTHR43028; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE 1; 1. DR PANTHER; PTHR43028:SF7; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE CYSQ; 1. DR Pfam; PF00459; Inositol_P; 1. DR PRINTS; PR00377; IMPHPHTASES. DR SUPFAM; SSF56655; Carbohydrate phosphatase; 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..269 FT /note="3'(2'),5'-bisphosphate nucleotidase CysQ" FT /id="PRO_0000142549" FT BINDING 69 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095" FT BINDING 69 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095" FT BINDING 89 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095" FT BINDING 89 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095" FT BINDING 91..94 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095" FT BINDING 91 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095" FT BINDING 92 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095" FT BINDING 216 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095" FT BINDING 216 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02095" SQ SEQUENCE 269 AA; 30723 MW; 52DC1BB9E0FD71DC CRC64; MLTLNEHLLN QVLLIAYQSG KHLQQFYQKQ VHVELKEDNT PVTEADLFVS QFLTEKLTAL FPNVPVLSEE NCHISFEERK NWKEYWLIDP LDGTQQFINR TDQFSVLITL VRKNKPVLSV IHAPILSTTY YAMCDFGTFK KQLDQVKKLT KNTTNFDRPL RIAVGATTSQ EKVRSILPKD FPCEFVVVGS SSLKSGLVAE GAVDCYVRLG QTGEWDTAGA EVLLGETHGA IFDSHFEPLT YNQRETLINP HFVMVGDQSF DWRSIFQFN //