ID Q5FQ92_GLUOX Unreviewed; 368 AA.
AC Q5FQ92;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=glycerophosphodiester phosphodiesterase {ECO:0000256|ARBA:ARBA00012247};
DE EC=3.1.4.46 {ECO:0000256|ARBA:ARBA00012247};
GN OrderedLocusNames=GOX1714 {ECO:0000313|EMBL:AAW61454.1};
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW61454.1, ECO:0000313|Proteomes:UP000006375};
RN [1] {ECO:0000313|EMBL:AAW61454.1, ECO:0000313|Proteomes:UP000006375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H {ECO:0000313|EMBL:AAW61454.1,
RC ECO:0000313|Proteomes:UP000006375};
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW61454.1; -; Genomic_DNA.
DR RefSeq; WP_011253236.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FQ92; -.
DR STRING; 290633.GOX1714; -.
DR KEGG; gox:GOX1714; -.
DR eggNOG; COG0584; Bacteria.
DR HOGENOM; CLU_030226_0_0_5; -.
DR Proteomes; UP000006375; Chromosome.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd08602; GDPD_ScGlpQ1_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:AAW61454.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006375};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..368
FT /note="glycerophosphodiester phosphodiesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004256508"
FT DOMAIN 32..364
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
SQ SEQUENCE 368 AA; 40399 MW; 219179A264774D39 CRC64;
MLSRRRALGL LAAGVPALHL RAKAAPSLAP KPLVFAHRGA SALRPEHTLA SYARAMMDGA
DFIEPDLVMT KDGHLVVRHE SNIAGTTDVA DHPEFASRHR TLKIDGKNET GWFTTDFTLA
ELKTLRARER LSTIRVHNTR YDDHFEIPTF EEVIEQVAAQ SAATGKVFGL VPEIKHSTHF
NSLGLNPEAA FLRTIAAHDY TRQAPLELQS FETGNLGRIR ADVLSINPQA RLMLLMGERK
DVPPDLLAAG KTTTFGDLMT PEGLKEIRRY ADVIGPSNTD LIPRDSKGAW LEPSTLVTDA
HKAGLLVHSY TARPENHFLP AQLRSDAGDA ARNPKGMIAE VRRYLDMGID GFFTDDPALG
RIAVKGTI
//
