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Database: UniProt
Entry: H0C229_9BURK
LinkDB: H0C229_9BURK
Original site: H0C229_9BURK 
ID   H0C229_9BURK            Unreviewed;       389 AA.
AC   H0C229;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=glycerophosphodiester phosphodiesterase {ECO:0000256|ARBA:ARBA00012247};
DE            EC=3.1.4.46 {ECO:0000256|ARBA:ARBA00012247};
GN   ORFNames=KYG_18656 {ECO:0000313|EMBL:EHL21354.1};
OS   Acidovorax sp. NO-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL21354.1, ECO:0000313|Proteomes:UP000003485};
RN   [1] {ECO:0000313|EMBL:EHL21354.1, ECO:0000313|Proteomes:UP000003485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NO-1 {ECO:0000313|EMBL:EHL21354.1,
RC   ECO:0000313|Proteomes:UP000003485};
RX   PubMed=22374962; DOI=10.1128/JB.06814-11;
RA   Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT   "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT   Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL   J. Bacteriol. 194:1635-1636(2012).
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; AGTS01000105; EHL21354.1; -; Genomic_DNA.
DR   RefSeq; WP_008906374.1; NZ_AGTS01000105.1.
DR   AlphaFoldDB; H0C229; -.
DR   STRING; 512030.KYG_18656; -.
DR   PATRIC; fig|512030.4.peg.3688; -.
DR   OrthoDB; 9795622at2; -.
DR   Proteomes; UP000003485; Unassembled WGS sequence.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003485};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          38..387
FT                   /note="GP-PDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51704"
FT   REGION          297..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   389 AA;  42552 MW;  DCAE6542A723008C CRC64;
     MHLSGAKLGV LAVAVGLVAC GGNDDDSSRY STLNGDKPLV IGHRGASGYL PEHTLESYKR
     AIELGADFIE PDLVATKDGV LVARHEPNIT GTTDVSTRPE FADRKTKKVV DGVEEEGWFA
     SDFTLAEIKT LRAIQPMAER DQSYNGKFQI PTLDEVLDLA KSEGAKTNRT VGVYPETKHP
     TYHVNLGLQL EDRLLAALAK YGYTSKASPV IVQSFEVSNL KYLRTKTQIR LVQLVDANDV
     NPNGTVDLTA PYDKPYDFAV AGDARTFASL LTPAGLKEVK TYADGIGPWK PYLIPSRQVD
     ANNDGKPDDL NNDGKIDDRD RVMMPATDVV KNAHAVGLMV HPYTFRSEAR RLASDFKGDP
     KAEYKLFYEL GVDGVFSDFP DAAKAARDN
//
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