ID GPDQ_ARCNC Reviewed; 273 AA. AC D5V0N9; DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot. DT 13-JUL-2010, sequence version 1. DT 27-MAR-2024, entry version 69. DE RecName: Full=Probable 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=Arnit_2199; OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG OS 7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Arcobacteraceae; Arcobacter. OX NCBI_TaxID=572480; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / RC CI; RX PubMed=21304714; DOI=10.4056/sigs.912121; RA Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M., RA Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R., RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Arcobacter nitrofigilis type strain (CI)."; RL Stand. Genomic Sci. 2:300-308(2010). 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; CP001999; ADG93851.1; -; Genomic_DNA. DR RefSeq; WP_013135996.1; NC_014166.1. DR AlphaFoldDB; D5V0N9; -. DR SMR; D5V0N9; -. DR STRING; 572480.Arnit_2199; -. DR KEGG; ant:Arnit_2199; -. DR eggNOG; COG1409; Bacteria. DR HOGENOM; CLU_070320_2_1_7; -. DR OrthoDB; 1662393at2; -. DR Proteomes; UP000000939; 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..273 FT /note="Probable glycerophosphodiester phosphodiesterase FT GpdQ" FT /id="PRO_0000413364" 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 154 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q6XBH1" FT BINDING 194 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q6XBH1" FT BINDING 196 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q6XBH1" SQ SEQUENCE 273 AA; 31373 MW; 2F230D65CA257CB6 CRC64; MIVVQVSDTH IKSKGKLAYN KVDIHKALYN CILHINNLKP KPDLVIFTGD ITDNGTNEEY KLFKETVKLL DVPFYVIPGN HDNAENLKRE FEEYDWFEEN NHLSLVIEDF PIRIIGLDSS IKGKSYGGLS EERLLWLEKQ LNKFPDKKVL LFIHHPPVKI GIEHMDVQNL QIGRERLADL LGKYEQVLAL ACGHVHRVST TLWNKIIVLT AASPSHQVAL DLRKDAKAEF VMEPPSVQLH YWTEEQGLTT HTSYIGKFEG PYPFYNEKGE LID //