ID B7N5K3_ECOLU Unreviewed; 358 AA.
AC B7N5K3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=glycerophosphodiester phosphodiesterase {ECO:0000256|ARBA:ARBA00012247};
DE EC=3.1.4.46 {ECO:0000256|ARBA:ARBA00012247};
GN Name=glpQ {ECO:0000313|EMBL:CAR13762.1};
GN OrderedLocusNames=ECUMN_2579 {ECO:0000313|EMBL:CAR13762.1};
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056 {ECO:0000313|EMBL:CAR13762.1, ECO:0000313|Proteomes:UP000007097};
RN [1] {ECO:0000313|Proteomes:UP000007097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC {ECO:0000313|Proteomes:UP000007097};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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:0000256|ARBA:ARBA00029315};
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000256|ARBA:ARBA00007277}.
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DR EMBL; CU928163; CAR13762.1; -; Genomic_DNA.
DR RefSeq; WP_000779113.1; NC_011751.1.
DR RefSeq; YP_002413290.1; NC_011751.1.
DR AlphaFoldDB; B7N5K3; -.
DR STRING; 585056.ECUMN_2579; -.
DR KEGG; eum:ECUMN_2579; -.
DR PATRIC; fig|585056.7.peg.2758; -.
DR HOGENOM; CLU_030226_1_0_6; -.
DR OMA; CRHENDI; -.
DR Proteomes; UP000007097; Chromosome.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd08600; GDPD_EcGlpQ_like; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR PANTHER; PTHR43620:SF7; GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE GDPD5-RELATED; 1.
DR PANTHER; PTHR43620; GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE; 1.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS51704; GP_PDE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAR13762.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..358
FT /note="glycerophosphodiester phosphodiesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002857928"
FT DOMAIN 31..355
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
SQ SEQUENCE 358 AA; 40871 MW; 26F5BA1049D3ACF8 CRC64;
MKLTLKNLSM AIMMSTMVMG SGAMAADNNE KIVIAHRGAS GYLPEHTLPA KAMAYAQGAD
YLEQDLVMTK DDHLVVLHDH YLDRVTDVAD RFPDRARKDG RYYAIDFTLD EIKSLKFTEG
FDIENGKKVQ TYPGRFPMGK SDFRVHTFEE EIEFVQGLNH STGKNIGIYP EIKAPWFHHQ
EGKDIAAKTL EVLKKYGYTG KDDKVYLQCF DADELKRIKN ELEPKMGMDL NLVQLIAYTD
WNETQQKQPD GSWVNYNYDW MFKPGAMKQV AEYADGIGPD YHMLIEETSQ PGNIKLTGMV
QDAQQNKLVV HPYTVRSDKL PEYTTDVNQL YDALYNKAGV NGLFTDFPDK AVKFLNKE
//