CYSQ_SALTY
ID CYSQ_SALTY Reviewed; 246 AA.
AC P26264;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 129.
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=STM4404;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-198.
RC STRAIN=LT2;
RX PubMed=2172762; DOI=10.1007/bf00283039;
RA Liu J., Beacham I.R.;
RT "Transcription and regulation of the cpdB gene in Escherichia coli K12 and
RT Salmonella typhimurium LT2: evidence for modulation of constitutive
RT promoters by cyclic AMP-CRP complex.";
RL Mol. Gen. Genet. 222:161-165(1990).
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 -!- INDUCTION: Strongly repressed during nitrogen excess.
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; AE006468; AAL23224.1; -; Genomic_DNA.
DR EMBL; X54009; CAA37955.1; -; Genomic_DNA.
DR RefSeq; NP_463265.1; NC_003197.2.
DR RefSeq; WP_000893398.1; NC_003197.2.
DR AlphaFoldDB; P26264; -.
DR SMR; P26264; -.
DR STRING; 99287.STM4404; -.
DR PaxDb; P26264; -.
DR PRIDE; P26264; -.
DR EnsemblBacteria; AAL23224; AAL23224; STM4404.
DR GeneID; 1255930; -.
DR KEGG; stm:STM4404; -.
DR PATRIC; fig|99287.12.peg.4630; -.
DR HOGENOM; CLU_044118_3_0_6; -.
DR OMA; SADCYPR; -.
DR PhylomeDB; P26264; -.
DR BioCyc; SENT99287:STM4404-MON; -.
DR Proteomes; UP000001014; 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:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
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 2: Evidence at transcript level;
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_0000142545"
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; 27490 MW; 11CF3A56BDF43C9A CRC64;
MLEQVCQLAR NAGDAIMQVY DGAKPMEYAR KQDDSPVTAA DIAAHTVILE GLRTLTPDIP
VLSEEDPPAW EVRQHWQRYW LVDPLDGTKE FIKRNGEFTV NIALIEQGKP VLGVVYAPVL
KVMYYAAEGK AWKEECGVRK QIQVRDARPP LVVISRSHTD DELTEYLQQL GEHQTTSIGS
SLKFCLVAEG QAQLYPRFGP TSVWDTAAGH AIAVAAGAHV HDWQGKTLDY TPRESFLNPG
FRVTIY
