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Database: UniProt
Entry: A3MZ96_ACTP2
LinkDB: A3MZ96_ACTP2
Original site: A3MZ96_ACTP2 
ID   A3MZ96_ACTP2            Unreviewed;       362 AA.
AC   A3MZ96;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
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:ABN73482.1};
GN   OrderedLocusNames=APL_0378 {ECO:0000313|EMBL:ABN73482.1};
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269 {ECO:0000313|EMBL:ABN73482.1, ECO:0000313|Proteomes:UP000001432};
RN   [1] {ECO:0000313|EMBL:ABN73482.1, ECO:0000313|Proteomes:UP000001432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20 {ECO:0000313|EMBL:ABN73482.1,
RC   ECO:0000313|Proteomes:UP000001432};
RX   PubMed=18065534; DOI=10.1128/JB.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN73482.1; -; Genomic_DNA.
DR   RefSeq; WP_005596381.1; NC_009053.1.
DR   AlphaFoldDB; A3MZ96; -.
DR   STRING; 416269.APL_0378; -.
DR   EnsemblBacteria; ABN73482; ABN73482; APL_0378.
DR   GeneID; 69417555; -.
DR   KEGG; apl:APL_0378; -.
DR   eggNOG; COG0584; Bacteria.
DR   HOGENOM; CLU_030226_1_0_6; -.
DR   Proteomes; UP000001432; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABN73482.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001432};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..362
FT                   /note="glycerophosphodiester phosphodiesterase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002655540"
FT   DOMAIN          33..358
FT                   /note="GP-PDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51704"
SQ   SEQUENCE   362 AA;  41415 MW;  97674DD44B4EDF31 CRC64;
     MKTIKALAVS LITTAVLAGC SNTQPVEPVK SDKLIIAHRG ASGYLPEHTL ESKALAFAQQ
     ADYLEQDLAM TKDNRLIVIH DHFLDGLTDV AKKFPKRARK DGRFYVADFT LKEIQTLEMT
     ENFKTENGQQ VQVYPNRFPM WKSHFRIHTF EDEIEFIQGL EKSTGKQIGI YPEIKAPWLH
     HQEGKDIALE TLKVLKKYGY DQKSDKVYLQ TFDFNELKRI KTELLPKLGM DVKLVQLVAY
     TDWHETEEKD ASGKWVNYNY DWMFKDGAMA EVAKYADGVG PGWYMLVDDK NSKLGDIKYT
     PMVKDIAKTK MELHPYTVRK DALPEFFSDV NQMYDALLNK AGATGVFTDF PDTGVQFIKG
     TK
//
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