CYSQ_ECOLI
ID CYSQ_ECOLI Reviewed; 246 AA.
AC P22255; Q2M691;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase CysQ {ECO:0000255|HAMAP-Rule:MF_02095, ECO:0000305};
DE EC=3.1.3.7 {ECO:0000255|HAMAP-Rule:MF_02095, ECO:0000269|PubMed:10224133};
DE AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_02095, ECO:0000305};
DE AltName: Full=3'-phosphoadenosine 5'-phosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_02095, ECO:0000305};
DE Short=PAP phosphatase {ECO:0000255|HAMAP-Rule:MF_02095, ECO:0000305};
DE AltName: Full=DPNPase {ECO:0000305};
GN Name=cysQ {ECO:0000255|HAMAP-Rule:MF_02095, ECO:0000303|PubMed:1729235};
GN Synonyms=amtA {ECO:0000303|PubMed:1856684};
GN OrderedLocusNames=b4214, JW4172;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1856684; DOI=10.1099/00221287-137-4-983;
RA Fabiny J.M., Jayakumar A., Chinault A.C., Barnes E.M. Jr.;
RT "Ammonium transport in Escherichia coli: localization and nucleotide
RT sequence of the amtA gene.";
RL J. Gen. Microbiol. 137:983-989(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX PubMed=1729235; DOI=10.1128/jb.174.2.415-425.1992;
RA Neuwald A.F., Krishnan B.R., Brikun I., Kulakauskas S., Suziedelis K.,
RA Tomcsanyi T., Leyh T.S., Berg D.E.;
RT "cysQ, a gene needed for cysteine synthesis in Escherichia coli K-12 only
RT during aerobic growth.";
RL J. Bacteriol. 174:415-425(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
RC STRAIN=K12;
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).
RN [7]
RP FUNCTION.
RX PubMed=7493934; DOI=10.1074/jbc.270.49.29105;
RA Peng Z., Verma D.P.S.;
RT "A rice HAL2-like gene encodes a Ca(2+)-sensitive 3'(2'),5'-
RT diphosphonucleoside 3'(2')-phosphohydrolase and complements yeast met22 and
RT Escherichia coli cysQ mutations.";
RL J. Biol. Chem. 270:29105-29110(1995).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10224133; DOI=10.1074/jbc.274.19.13619;
RA Spiegelberg B.D., Xiong J.-P., Smith J.J., Gu R.F., York J.D.;
RT "Cloning and characterization of a mammalian lithium-sensitive bisphosphate
RT 3'-nucleotidase inhibited by inositol 1,4-bisphosphate.";
RL J. Biol. Chem. 274:13619-13628(1999).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=15911532; DOI=10.1074/mcp.d500006-mcp200;
RA Lopez-Campistrous A., Semchuk P., Burke L., Palmer-Stone T., Brokx S.J.,
RA Broderick G., Bottorff D., Bolch S., Weiner J.H., Ellison M.J.;
RT "Localization, annotation, and comparison of the Escherichia coli K-12
RT proteome under two states of growth.";
RL Mol. Cell. Proteomics 4:1205-1209(2005).
RN [10]
RP FUNCTION, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=16682444; DOI=10.1093/nar/gkl247;
RA Mechold U., Ogryzko V., Ngo S., Danchin A.;
RT "Oligoribonuclease is a common downstream target of lithium-induced pAp
RT accumulation in Escherichia coli and human cells.";
RL Nucleic Acids Res. 34:2364-2373(2006).
CC -!- FUNCTION: Converts adenosine-3',5'-bisphosphate (PAP) to AMP. May also
CC convert adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine
CC 5'-phosphosulfate (APS). Has 10000-fold lower activity towards inositol
CC 1,4-bisphosphate (Ins(1,4)P2). {ECO:0000269|PubMed:10224133,
CC ECO:0000269|PubMed:16682444, ECO:0000269|PubMed:7493934}.
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 ECO:0000269|PubMed:10224133};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02095,
CC ECO:0000305|PubMed:16682444};
CC -!- ACTIVITY REGULATION: Inhibited by lithium and calcium.
CC {ECO:0000269|PubMed:16682444}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 uM for PAP {ECO:0000269|PubMed:10224133};
CC KM=1.2 mM for Ins(1,4)P2 {ECO:0000269|PubMed:10224133};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02095, ECO:0000269|PubMed:15911532}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_02095, ECO:0000305}; Cytoplasmic
CC side {ECO:0000255|HAMAP-Rule:MF_02095, ECO:0000305}.
CC -!- INDUCTION: Strongly repressed during nitrogen excess.
CC -!- DISRUPTION PHENOTYPE: Mutants require cysteine or sulfite to grow under
CC aerobic conditions. {ECO:0000269|PubMed:1729235}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. CysQ
CC family. {ECO:0000255|HAMAP-Rule:MF_02095, ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an ammonium transport protein.
CC {ECO:0000305|PubMed:1856684}.
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DR EMBL; M55170; AAA23444.1; -; Genomic_DNA.
DR EMBL; M80795; AAA23657.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97110.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77171.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78215.1; -; Genomic_DNA.
DR EMBL; X54008; CAA37953.1; -; Genomic_DNA.
DR PIR; S56439; S56439.
DR RefSeq; NP_418635.1; NC_000913.3.
DR RefSeq; WP_000886919.1; NZ_LN832404.1.
DR AlphaFoldDB; P22255; -.
DR SMR; P22255; -.
DR BioGRID; 4259304; 39.
DR DIP; DIP-9385N; -.
DR IntAct; P22255; 6.
DR STRING; 511145.b4214; -.
DR jPOST; P22255; -.
DR PaxDb; P22255; -.
DR PRIDE; P22255; -.
DR EnsemblBacteria; AAC77171; AAC77171; b4214.
DR EnsemblBacteria; BAE78215; BAE78215; BAE78215.
DR GeneID; 948728; -.
DR KEGG; ecj:JW4172; -.
DR KEGG; eco:b4214; -.
DR PATRIC; fig|1411691.4.peg.2487; -.
DR EchoBASE; EB0041; -.
DR eggNOG; COG1218; Bacteria.
DR HOGENOM; CLU_044118_3_0_6; -.
DR InParanoid; P22255; -.
DR OMA; SADCYPR; -.
DR PhylomeDB; P22255; -.
DR BioCyc; EcoCyc:EG10043-MON; -.
DR BioCyc; MetaCyc:EG10043-MON; -.
DR SABIO-RK; P22255; -.
DR PRO; PR:P22255; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
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; IMP:EcoCyc.
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 1: Evidence at protein 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_0000142541"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P29218, ECO:0000255|HAMAP-
FT Rule:MF_02095"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218, ECO:0000255|HAMAP-
FT Rule:MF_02095"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P29218, ECO:0000255|HAMAP-
FT Rule:MF_02095"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218, ECO:0000255|HAMAP-
FT Rule:MF_02095"
FT BINDING 85..88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218, ECO:0000255|HAMAP-
FT Rule:MF_02095"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P29218, ECO:0000255|HAMAP-
FT Rule:MF_02095"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218, ECO:0000255|HAMAP-
FT Rule:MF_02095"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218, ECO:0000255|HAMAP-
FT Rule:MF_02095"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218, ECO:0000255|HAMAP-
FT Rule:MF_02095"
FT CONFLICT 193..194
FT /note="QL -> HV (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 27176 MW; F0CBDFAA98DDAF85 CRC64;
MLDQVCQLAR NAGDAIMQVY DGTKPMDVVS KADNSPVTAA DIAAHTVIMD GLRTLTPDVP
VLSEEDPPGW EVRQHWQRYW LVDPLDGTKE FIKRNGEFTV NIALIDHGKP ILGVVYAPVM
NVMYSAAEGK AWKEECGVRK QIQVRDARPP LVVISRSHAD AELKEYLQQL GEHQTTSIGS
SLKFCLVAEG QAQLYPRFGP TNIWDTAAGH AVAAAAGAHV HDWQGKPLDY TPRESFLNPG
FRVSIY
