UGPQ_ECOLI
ID UGPQ_ECOLI Reviewed; 247 AA.
AC P10908; P22633; Q2M7B2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Glycerophosphodiester phosphodiesterase, cytoplasmic;
DE Short=Glycerophosphoryl diester phosphodiesterase, cytoplasmic;
DE EC=3.1.4.46;
GN Name=ugpQ; OrderedLocusNames=b3449, JW3414;
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;
RX PubMed=2541415; DOI=10.1093/nar/17.7.2854;
RA Kasahara M., Makino K., Amemura M., Nakata A.;
RT "Nucleotide sequence of the ugpQ gene encoding glycerophosphoryl diester
RT phosphodiesterase of Escherichia coli K-12.";
RL Nucleic Acids Res. 17:2854-2854(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1851953; DOI=10.1007/bf00273621;
RA Tommassen J., Eiglmeier K., Cole S.T., Overduin P., Larson T.J., Boos W.;
RT "Characterization of two genes, glpQ and ugpQ, encoding glycerophosphoryl
RT diester phosphodiesterases of Escherichia coli.";
RL Mol. Gen. Genet. 226:321-327(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
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 1-50.
RC STRAIN=K12;
RX PubMed=3062310; DOI=10.1111/j.1365-2958.1988.tb00088.x;
RA Overduin P., Boos W., Tommassen J.;
RT "Nucleotide sequence of the ugp genes of Escherichia coli K-12: homology to
RT the maltose system.";
RL Mol. Microbiol. 2:767-775(1988).
RN [7]
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=18083802; DOI=10.1128/jb.01223-07;
RA Ohshima N., Yamashita S., Takahashi N., Kuroishi C., Shiro Y., Takio K.;
RT "Escherichia coli cytosolic glycerophosphodiester phosphodiesterase (UgpQ)
RT requires Mg2+, Co2+, or Mn2+ for its enzyme activity.";
RL J. Bacteriol. 190:1219-1223(2008).
CC -!- FUNCTION: Glycerophosphoryl diester phosphodiesterase hydrolyzes
CC deacylated phospholipids to G3P and the corresponding alcohols.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-
CC glycerol 3-phosphate; Xref=Rhea:RHEA:12969, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:83408; EC=3.1.4.46;
CC Evidence={ECO:0000269|PubMed:18083802};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18083802};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:18083802};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18083802};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.22 mM for glycerophosphoethanolamine
CC {ECO:0000269|PubMed:18083802};
CC KM=0.66 mM for glycerophosphoserine {ECO:0000269|PubMed:18083802};
CC KM=0.62 mM for glycerophosphoglycerol {ECO:0000269|PubMed:18083802};
CC KM=0.39 mM for glycerophosphoinositol {ECO:0000269|PubMed:18083802};
CC KM=2.0 mM for glycerophosphocholine {ECO:0000269|PubMed:18083802};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:18083802};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18083802}.
CC -!- INDUCTION: Up-regulated by low levels of phosphate in the medium.
CC {ECO:0000269|PubMed:18083802}.
CC -!- MISCELLANEOUS: There are 2 isozymes of glycerophosphoryl diester
CC phosphodiesterase in E.coli: a periplasmic isozyme (GlpQ) and a
CC cytosolic isozyme (UgpQ).
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; X14437; CAA32609.1; -; Genomic_DNA.
DR EMBL; X13141; CAA31535.1; -; Genomic_DNA.
DR EMBL; X56908; CAA40224.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18424.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76474.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77844.1; -; Genomic_DNA.
DR PIR; JV0024; ESECGD.
DR RefSeq; NP_417906.1; NC_000913.3.
DR RefSeq; WP_000073623.1; NZ_LN832404.1.
DR AlphaFoldDB; P10908; -.
DR SMR; P10908; -.
DR BioGRID; 4261665; 14.
DR BioGRID; 852264; 3.
DR IntAct; P10908; 10.
DR STRING; 511145.b3449; -.
DR jPOST; P10908; -.
DR PaxDb; P10908; -.
DR PRIDE; P10908; -.
DR DNASU; 947955; -.
DR EnsemblBacteria; AAC76474; AAC76474; b3449.
DR EnsemblBacteria; BAE77844; BAE77844; BAE77844.
DR GeneID; 947955; -.
DR KEGG; ecj:JW3414; -.
DR KEGG; eco:b3449; -.
DR PATRIC; fig|1411691.4.peg.3278; -.
DR EchoBASE; EB1043; -.
DR eggNOG; COG0584; Bacteria.
DR HOGENOM; CLU_030006_3_2_6; -.
DR InParanoid; P10908; -.
DR OMA; YRMFECD; -.
DR PhylomeDB; P10908; -.
DR BioCyc; EcoCyc:GLYCPDIESTER-CYTO-MON; -.
DR BioCyc; MetaCyc:GLYCPDIESTER-CYTO-MON; -.
DR BRENDA; 3.1.4.46; 2026.
DR PRO; PR:P10908; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047389; F:glycerophosphocholine phosphodiesterase activity; IDA:EcoCyc.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IDA:EcoCyc.
DR GO; GO:0047395; F:glycerophosphoinositol glycerophosphodiesterase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS51704; GP_PDE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycerol metabolism; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..247
FT /note="Glycerophosphodiester phosphodiesterase,
FT cytoplasmic"
FT /id="PRO_0000200574"
FT DOMAIN 7..244
FT /note="GP-PDE"
SQ SEQUENCE 247 AA; 27410 MW; FF5EBFB4C6D7CC0D CRC64;
MSNWPYPRIV AHRGGGKLAP ENTLASIDVG AKYGHKMIEF DAKLSKDGEI FLLHDDNLER
TSNGWGVAGE LNWQDLLRVD AGSWYSKMFK GEPLPLLSQV AERCREHGMM ANIEIKPTTG
TGPLTGKMVA LAARELWAGM TPPLLSSFEI DALEAAQQAA PELPRGLLLD EWRDDWRELT
ARLGCVSIHL NHKLLNKARV MQLKDAGLRI LVYTVNKPQR AAELLRWGVD CICTDAIDVI
GPNFTAQ
