ID G2PB28_STRV4 Unreviewed; 277 AA. AC G2PB28; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 02-SEP-2026, entry version 55. DE SubName: Full=Glycerophosphoryl diester phosphodiesterase {ECO:0000313|EMBL:AEM88427.1}; GN ORFNames=Strvi_9138 {ECO:0000313|EMBL:AEM88427.1}; OS Streptomyces violaceusniger (strain Tu 4113). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group. OX NCBI_TaxID=653045 {ECO:0000313|EMBL:AEM88427.1, ECO:0000313|Proteomes:UP000008703}; RN [1] {ECO:0000313|EMBL:AEM88427.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tu 4113 {ECO:0000313|EMBL:AEM88427.1}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ivanova N., Daligault H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Hagen A., Katz L., RA Fiedler H.-P., Keasling J., Fortman J., Woyke T.; RT "Complete sequence of chromosome of Streptomyces violaceusniger Tu 4113."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01041}; 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; CP002994; AEM88427.1; -; Genomic_DNA. DR RefSeq; WP_014061881.1; NC_015957.1. DR AlphaFoldDB; G2PB28; -. DR KEGG; svl:Strvi_9138; -. DR eggNOG; COG0584; Bacteria. DR HOGENOM; CLU_030006_3_0_11; -. DR Proteomes; UP000008703; Chromosome. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro. DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro. DR CDD; cd08582; GDPD_like_2; 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; PTHR46211:SF13; GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE 1-RELATED; 1. DR PANTHER; PTHR46211; 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|PROSITE-ProRule:PRU01041}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01041}; KW Reference proteome {ECO:0000313|Proteomes:UP000008703}. FT DOMAIN 17..274 FT /note="GP-PDE" FT /evidence="ECO:0000259|PROSITE:PS51704" FT REGION 1..28 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..11 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 49 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01041" FT BINDING 51 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01041" FT BINDING 64 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01041" SQ SEQUENCE 277 AA; 30584 MW; 14F47E6A870FAE57 CRC64; MTYARPARDS HPGPPTVSVV AHRGASEDAP EHTLAAYRKA IEEGADALEC DVRLTADGHL VCVHDRRVDR TSNGRGAVSA LELSDLAALD FGSWKGRATD KEEPDRDSRD STSVLTLERL LALIADAGRQ IELAIETKHP TRWAGQVEER LLTLLRRYGL DAPPPGERSP VRVMSFSARS LHRIRTGAPA IPTVYLMQFI LPRHRDGQLP AGVRIAGPSI RIVRNHPGYV ARLQREGHRV HVWTVDEPED VDLCVRLGVD ALITNRPKQV LSQLGRS //