GPDQ_ENTLS
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 03-AUG-2022, entry version 67.
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}; OrderedLocusNames=Entcl_3882;
OS Enterobacter lignolyticus (strain SCF1).
OC Bacteria; Proteobacteria; 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}.
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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 EnsemblBacteria; ADO50122; ADO50122; Entcl_3882.
DR KEGG; esc:Entcl_3882; -.
DR eggNOG; COG1409; Bacteria.
DR HOGENOM; CLU_070320_2_1_6; -.
DR OMA; TAVFMHH; -.
DR OrthoDB; 1242748at2; -.
DR Proteomes; UP000006872; Chromosome.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR CDD; cd07402; MPP_GpdQ; 1.
DR Gene3D; 3.30.750.180; -; 1.
DR Gene3D; 3.60.21.40; -; 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 Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 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
