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Database: UniProt
Entry: Q0T2P2_SHIF8
LinkDB: Q0T2P2_SHIF8
Original site: Q0T2P2_SHIF8 
ID   Q0T2P2_SHIF8            Unreviewed;       358 AA.
AC   Q0T2P2;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 80.
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:ABF04423.1};
GN   OrderedLocusNames=SFV_2311 {ECO:0000313|EMBL:ABF04423.1};
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384 {ECO:0000313|EMBL:ABF04423.1, ECO:0000313|Proteomes:UP000000659};
RN   [1] {ECO:0000313|EMBL:ABF04423.1, ECO:0000313|Proteomes:UP000000659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401 {ECO:0000313|EMBL:ABF04423.1,
RC   ECO:0000313|Proteomes:UP000000659};
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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; CP000266; ABF04423.1; -; Genomic_DNA.
DR   RefSeq; WP_000768978.1; NC_008258.1.
DR   AlphaFoldDB; Q0T2P2; -.
DR   KEGG; sfv:SFV_2311; -.
DR   HOGENOM; CLU_030226_1_0_6; -.
DR   Proteomes; UP000000659; Chromosome.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
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};
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_5004177003"
FT   DOMAIN          31..355
FT                   /note="GP-PDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51704"
SQ   SEQUENCE   358 AA;  40923 MW;  ABCD17485FE41840 CRC64;
     MKLKLKNLSM AIMMSTIVMG SSAMAADSNE KIVIAHRGAS GYLPEHTLPA KAMAYAQGAD
     YLEQDLVMTK DDHLVVLHDH YLDRVTDVAD RFPDRARKDG RYYTIDFTLD EIKSLKFTEG
     FDIENGKKVQ TYPGRFPMGK SDFRVHTFEE EIEFVQGLNH STGKNIGIYP EIKAPWFHHQ
     EGKDIAAKTL EVLKKYGYTG KDDKVYLQCF DADELKRIKN ELEPKMGMEL NLVQLIAYTD
     WNETQQKQPD GSWVNYNYDW MFKPGAMKQV AEYADGIGPD YHMLIEETSQ PGNIKLTGMV
     QDAQQNKLVV HPYTVRSDKL PEYTPDVNQL YDALYNKAGV NGLFTDFPDK AVKFLNKE
//
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