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Database: UniProt
Entry: V4PAX5_9CAUL
LinkDB: V4PAX5_9CAUL
Original site: V4PAX5_9CAUL 
ID   V4PAX5_9CAUL            Unreviewed;       356 AA.
AC   V4PAX5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=glycerophosphodiester phosphodiesterase {ECO:0000256|ARBA:ARBA00012247};
DE            EC=3.1.4.46 {ECO:0000256|ARBA:ARBA00012247};
GN   ORFNames=AEAC466_05635 {ECO:0000313|EMBL:ESQ85191.1};
OS   Asticcacaulis sp. AC466.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ85191.1, ECO:0000313|Proteomes:UP000017826};
RN   [1] {ECO:0000313|EMBL:ESQ85191.1, ECO:0000313|Proteomes:UP000017826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC466 {ECO:0000313|EMBL:ESQ85191.1,
RC   ECO:0000313|Proteomes:UP000017826};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(2014).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESQ85191.1}.
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DR   EMBL; AWGE01000005; ESQ85191.1; -; Genomic_DNA.
DR   RefSeq; WP_023457159.1; NZ_AWGE01000005.1.
DR   AlphaFoldDB; V4PAX5; -.
DR   STRING; 1282362.AEAC466_05635; -.
DR   PATRIC; fig|1282362.3.peg.1127; -.
DR   eggNOG; COG0584; Bacteria.
DR   OrthoDB; 9795622at2; -.
DR   Proteomes; UP000017826; 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   InterPro; IPR006311; TAT_signal.
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; PS51318; TAT; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017826};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..356
FT                   /note="glycerophosphodiester phosphodiesterase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004724734"
FT   DOMAIN          30..355
FT                   /note="GP-PDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51704"
SQ   SEQUENCE   356 AA;  39490 MW;  B6173C097A9E1507 CRC64;
     MHLTRRRLIG AAAATMASAT LAYAATPRKP LIVGHRGAAG YLPEHTIPGY ELAIKMGADF
     IEPDVVATSD GHLIVRHEPL LSVTTDVAER SEFADRKRTR TLDGIETTDF FTCDFTLAEI
     KTLRAKQAFA DRDQSHNGQY GIVTLQEVID LAQAKTRQTG RVIGIYPEVK HSTFHRELGL
     PVEDKLLDML RQAGMEAKSS PVIIQSFETA NLKYLRTKTQ VRLMQLVDGS DTDAKGDMVL
     TPPSDKPYDW VMAGRAGNNL DQLTPRGLAD IAAYADIVAP WKRYLISFSD GKPRLNHKLV
     EDAHALGLQV HTWTMRNDRL DPFYHGDAVA EYRQLFAMGV DGVFTDFPDT GVKARA
//
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