GPDQ_STRAW
ID GPDQ_STRAW Reviewed; 257 AA.
AC Q93GX3;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Synonyms=cpdA {ECO:0000312|EMBL:BAC68957.1}; OrderedLocusNames=SAV_1247;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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; AB070957; BAB69418.1; -; Genomic_DNA.
DR EMBL; BA000030; BAC68957.1; -; Genomic_DNA.
DR AlphaFoldDB; Q93GX3; -.
DR SMR; Q93GX3; -.
DR STRING; 227882.SAV_1247; -.
DR EnsemblBacteria; BAC68957; BAC68957; SAVERM_1247.
DR KEGG; sma:SAVERM_1247; -.
DR eggNOG; COG1409; Bacteria.
DR HOGENOM; CLU_070320_2_1_11; -.
DR OMA; TGIGHMD; -.
DR Proteomes; UP000000428; 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; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR026575; GpdQ/CpdA-like.
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..257
FT /note="Probable glycerophosphodiester phosphodiesterase
FT GpdQ"
FT /id="PRO_0000413379"
FT BINDING 6
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
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 44
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT BINDING 44
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT BINDING 74
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT BINDING 187
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
SQ SEQUENCE 257 AA; 27129 MW; C308521452EDFA66 CRC64;
MAHLSDPHLT TGLLAVDRVA AFSRALRCVL ALDPRPACVV VTGDLVDRGE AEEYEVLREV
IARFPLPVHL VPGNHDDPGT LLEAFGGGPH TGGARAFPYA VEYPNATVVV LSSTVPGAPS
GRLGDEQLDR LEELLSRRPE VPAFVCLHHP PVDIGIPYLD GMNLADADAF GEVIGRHPQV
VRVLAGHVHR AVTGEFAGST MVTAPSTYLQ SNLNLRVGGP VGYVDEPTAF LLHHLTGTGC
VTHTAQVSHA GGLIGGY
