ID GPDQ_ENTLS Reviewed; 278 AA. AC E3GCF1; DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 1. DT 27-MAR-2024, entry version 72. DE RecName: Full=Glycerophosphodiester phosphodiesterase GpdQ {ECO:0000250|UniProtKB:Q6XBH1}; DE Short=GDPD {ECO:0000250|UniProtKB:Q6XBH1}; DE Short=Glycerophosphoryl diester phosphodiesterase {ECO:0000250|UniProtKB:Q6XBH1}; DE EC=3.1.4.46 {ECO:0000250|UniProtKB:Q6XBH1}; DE AltName: Full=Glycerophosphodiesterase {ECO:0000250|UniProtKB:Q6XBH1}; DE AltName: Full=Glycerophosphorylethanolamine phosphodiesterase {ECO:0000250|UniProtKB:Q6XBH1}; DE Short=GPE phosphodiesterase {ECO:0000250|UniProtKB:Q6XBH1}; GN Name=gpdQ {ECO:0000250|UniProtKB:Q6XBH1}; GN OrderedLocusNames=Entcl_3882; OS Enterobacter lignolyticus (strain SCF1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Pluralibacter. OX NCBI_TaxID=701347; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCF1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B., Woo H., RA Hazen T.C., Woyke T.; RT "Complete sequence of Enterobacter cloacae SCF1."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the hydrolysis of the 3'-5' phosphodiester bond of CC glycerophosphodiesters such as glycerophosphorylethanolamine (GPE), a CC typical phospholipid metabolite. {ECO:0000250|UniProtKB:Q6XBH1}. 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:0000250|UniProtKB:Q6XBH1}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + sn-glycero-3-phosphoethanolamine = ethanolamine + H(+) + CC sn-glycerol 3-phosphate; Xref=Rhea:RHEA:29319, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57597, ChEBI:CHEBI:57603, CC ChEBI:CHEBI:143890; Evidence={ECO:0000250|UniProtKB:Q6XBH1}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000250|UniProtKB:Q6XBH1}; CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:Q6XBH1}; CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class- CC III family. {ECO:0000305}. 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; CP002272; ADO50122.1; -; Genomic_DNA. DR RefSeq; WP_013367845.1; NC_014618.1. DR AlphaFoldDB; E3GCF1; -. DR SMR; E3GCF1; -. DR STRING; 701347.Entcl_3882; -. DR KEGG; esc:Entcl_3882; -. DR eggNOG; COG1409; Bacteria. DR HOGENOM; CLU_070320_2_1_6; -. DR Proteomes; UP000006872; Chromosome. DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC. DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:RHEA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW. DR CDD; cd07402; MPP_GpdQ; 1. DR Gene3D; 3.30.750.180; GpdQ, beta-strand dimerisation domain; 1. DR Gene3D; 3.60.21.40; GpdQ, catalytic alpha/beta sandwich domain; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR026575; GpdQ/CpdA-like. DR InterPro; IPR042281; GpdQ_beta-strand. DR InterPro; IPR042283; GpdQ_catalytic. DR InterPro; IPR029052; Metallo-depent_PP-like. DR PANTHER; PTHR42988:SF2; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE CBUA0032-RELATED; 1. DR PANTHER; PTHR42988; PHOSPHOHYDROLASE; 1. DR Pfam; PF00149; Metallophos; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. PE 3: Inferred from homology; KW Glycerol metabolism; Hydrolase; Iron; Metal-binding; Reference proteome. FT CHAIN 1..278 FT /note="Glycerophosphodiester phosphodiesterase GpdQ" FT /id="PRO_0000413367" FT BINDING 8 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q6XBH1" FT BINDING 10 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q6XBH1" FT BINDING 50 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q6XBH1" FT BINDING 50 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q6XBH1" FT BINDING 80 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q6XBH1" FT BINDING 156 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q6XBH1" FT BINDING 195 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q6XBH1" FT BINDING 197 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q6XBH1" SQ SEQUENCE 278 AA; 31308 MW; CFF0D7D4DDB3AF10 CRC64; MLLAHISDTH FRSQNHKLYG FIDVNAGNAD VVSQLNGLRE RPDAVVVSGD IVNCGRPEEY QVARQVLGAL RYPLLLIPGN HDDKACFLEY LRPLCPQLGS DPQNMRYAID DFATRLLFID SSLAGHAKGW LTDNTVAWLE AQLSDAGDKP TAVFMHHPPL PLGNAQMDPI ACENGHRLLA LVERFPSLVR IFCGHNHNLT MTQYRQATIA TLPATVHQVP YCHEDTRPYY DMSPPSCLMH RQVGEQWVSY QHSLAHYAGP WLYDEHISCP TDERRSPC //