ID B2AH74_CUPTR Unreviewed; 422 AA.
AC B2AH74;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, 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 OrderedLocusNames=RALTA_A0455 {ECO:0000313|EMBL:CAP63123.1};
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880 {ECO:0000313|EMBL:CAP63123.1, ECO:0000313|Proteomes:UP000001692};
RN [1] {ECO:0000313|EMBL:CAP63123.1, ECO:0000313|Proteomes:UP000001692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC R1 {ECO:0000313|Proteomes:UP000001692};
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU633749; CAP63123.1; -; Genomic_DNA.
DR AlphaFoldDB; B2AH74; -.
DR KEGG; cti:RALTA_A0455; -.
DR eggNOG; COG0584; Bacteria.
DR HOGENOM; CLU_030226_0_0_4; -.
DR Proteomes; UP000001692; Chromosome 1.
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 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, ECO:0000313|EMBL:CAP63123.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..48
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 49..422
FT /note="glycerophosphodiester phosphodiesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002772836"
FT DOMAIN 85..417
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 56..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 44860 MW; 69C129EB99B47B84 CRC64;
MAPPQERCMP SPSRPCAPRP RASFARVVAA CRRWLLPAAA AAACAALAAG CATAPRPKRA
APAAPPAPAP AASAPASAPA AQPKPLVIAH RGASALRPEH TLAAYAKAIE DGADAIEPDL
VMTRDGVLVA RHENDITGTT NVAELPQFAE RKRTKVIDGE RLTGWFTEDF TLAELKTLRA
RERIPRLRPA NARLNDQFEV PTFDEIVRLA EQAALRTGKP VGIYAELKHP SYFRGIGLPL
EDKLAAAVRA QPYLRNAPVF IQCFESGSLR ALRRTLGNGL PNVKLVQLIG NPRKGPADWK
LAGDGRTFGD MLSTTGLREV AAYADGIGPE KSSVVPRDAQ GALGAPTAVV QQAHAAGLFV
HPYTFRPENS FLPKALQSGG DEATRSPAGM EREVQAFVAA GIDGFFTDDP ALGRRAVDTP
AR
//
