ID B7LM89_ESCF3 Unreviewed; 378 AA.
AC B7LM89;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:CAQ88462.1};
GN OrderedLocusNames=EFER_0927 {ECO:0000313|EMBL:CAQ88462.1};
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054 {ECO:0000313|EMBL:CAQ88462.1, ECO:0000313|Proteomes:UP000000745};
RN [1] {ECO:0000313|Proteomes:UP000000745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 /
RC JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73
RC {ECO:0000313|Proteomes:UP000000745};
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};
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DR EMBL; CU928158; CAQ88462.1; -; Genomic_DNA.
DR AlphaFoldDB; B7LM89; -.
DR KEGG; efe:EFER_0927; -.
DR HOGENOM; CLU_030226_1_0_6; -.
DR Proteomes; UP000000745; 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 GDPD6; 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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAQ88462.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..44
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 45..378
FT /note="glycerophosphodiester phosphodiesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002860087"
FT DOMAIN 50..374
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
SQ SEQUENCE 378 AA; 43023 MW; 3EE75BF06393D05B CRC64;
MAKNVAMNNY CKNAMEANGM KLTLKNLSMA IMMSTMVMGS SAMAADSSEK IVIAHRGASG
YLPEHTLPAK AMAYAQGADY LEQDLVMTKD DHLVVLHDHY LDRVTDVADR FPDRARKDGR
YYAIDFTLDE IKSLKFTEGF DIENGKKVQT YPGRFPMGKS DFRVHTFEEE IEFVQGLNHS
TGKNIGIYPE IKAPWFHHQE GKDIAAKTLE VLKKYGYTGK DDKVYLQCFD ADELKRIKNE
LEPKMGMDLN LVQLIAYTDW NETQQKQPDG SWVNYSYDWM FKPGAMKQVA EYADGIGPDY
HMLIEEKSQP GNIQLTGMVK DAQHNNLVVH PYTVRADQLP TYTTNVNQLY DILYNKAGVN
GLFTDFPDKA VNFLQQQK
//
