GPDQ_ARCNC
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 03-AUG-2022, entry version 63.
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}; OrderedLocusNames=Arnit_2199;
OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS 7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC Bacteria; Proteobacteria; 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 / 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}.
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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 EnsemblBacteria; ADG93851; ADG93851; Arnit_2199.
DR KEGG; ant:Arnit_2199; -.
DR eggNOG; COG1409; Bacteria.
DR HOGENOM; CLU_070320_2_1_7; -.
DR OMA; TGIGHMD; -.
DR OrthoDB; 1242748at2; -.
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; -; 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..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
