ID D4LBH3_RUMC1 Unreviewed; 656 AA.
AC D4LBH3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 10-JUN-2026, entry version 72.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN OrderedLocusNames=RUM_07760 {ECO:0000313|EMBL:CBL16968.1};
OS Ruminococcus champanellensis (strain DSM 18848 / JCM 17042 / KCTC 15320 /
OS 18P13).
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC Oscillospiraceae; Ruminococcus.
OX NCBI_TaxID=213810 {ECO:0000313|EMBL:CBL16968.1, ECO:0000313|Proteomes:UP000007054};
RN [1] {ECO:0000313|EMBL:CBL16968.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Type strain: 18P13 {ECO:0000313|EMBL:CBL16968.1};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Bernalier A.;
RT "The genome sequence of Ruminococcus sp. 18P13.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL16968.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain: 18P13 {ECO:0000313|EMBL:CBL16968.1};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has phosphodiesterase (PDE) activity against cyclic-di-AMP
CC (c-di-AMP). {ECO:0000256|PIRNR:PIRNR026583}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',3'-c-di-AMP + H2O = 5'-O-phosphonoadenylyl-(3'->5')-
CC adenosine + H(+); Xref=Rhea:RHEA:54420, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:71500, ChEBI:CHEBI:138171;
CC Evidence={ECO:0000256|PIRNR:PIRNR026583};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR026583-50};
CC Note=For phosphodiesterase activity, probably binds 2 Mn(2+) per
CC subunit. {ECO:0000256|PIRSR:PIRSR026583-50};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR026583}.
CC -!- SIMILARITY: Belongs to the GdpP/PdeA phosphodiesterase family.
CC {ECO:0000256|PIRNR:PIRNR026583}.
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DR EMBL; FP929052; CBL16968.1; -; Genomic_DNA.
DR RefSeq; WP_015557875.1; NC_021039.1.
DR AlphaFoldDB; D4LBH3; -.
DR STRING; 213810.RUM_07760; -.
DR GeneID; 83155562; -.
DR KEGG; rch:RUM_07760; -.
DR PATRIC; fig|213810.4.peg.690; -.
DR HOGENOM; CLU_018278_0_0_9; -.
DR BioCyc; RCHA213810:RUM_RS03735-MONOMER; -.
DR Proteomes; UP000007054; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0106409; F:cyclic-di-AMP phosphodiesterase activity; IEA:RHEA.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR FunFam; 3.90.1640.10:FF:000002; Cyclic-di-AMP phosphodiesterase; 1.
DR Gene3D; 3.10.310.30; -; 1.
DR Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR014528; GdpP/PdeA.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR051319; Oligoribo/pAp-PDE_c-di-AMP_PDE.
DR PANTHER; PTHR47618; BIFUNCTIONAL OLIGORIBONUCLEASE AND PAP PHOSPHATASE NRNA; 1.
DR PANTHER; PTHR47618:SF2; CYCLIC-DI-AMP PHOSPHODIESTERASE GDPP; 1.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF24898; GGDEF_GdpP; 1.
DR PIRSF; PIRSF026583; YybT; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR PROSITE; PS50887; GGDEF; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|PIRNR:PIRNR026583};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR026583};
KW Manganese {ECO:0000256|PIRSR:PIRSR026583-50};
KW Membrane {ECO:0000256|PIRNR:PIRNR026583, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR026583-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000007054};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 178..306
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT BINDING 349
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 355
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 420
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 420
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 444
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 499
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
SQ SEQUENCE 656 AA; 72948 MW; E020F0B1C90AD9E6 CRC64;
MREKRPVWFC ITVGLLLCSA GYAAYGLHGY DTERFWLSVV LLFVSAVLFL ISFFLFSKRN
IRFIATLNDE LAAAEHETMY SLPVPTVILD DSGLILWYNL LFGRDILEND DVFGLRIGEV
LDLDLPTLLE TGSGSVHYCD KQYEISVTTC TRNDRNLHLL CFTDVTDYAA LQDTFLNTRP
TVMLLVIDNY EDVLQNAKES EKATVFVAIE QMLERFMAPT TGVLRKLSSD RFVAVVEEQH
LQQMIRGKFR ILDDARTITV GERYAITLSI GVGHGASTLE ESEAFAKQAL DMALGRGGDQ
VALKTENGYK FFGGVSKGVE KKSRAKTRII ANAMQELIHT CDRVMIMGHR YGDLDSIGSA
IGLAGAILQS GKPAHVVVDR QTTLAGVLID RMEAEDIHLT IDVPTALTQM TEQTLLIVVD
THSKDFVESV DLYQNARQVV VIDHHRKIVN FIDNAVIFYH EPYASSAAEL VTELLQHFRN
TEHLNPAYAD VLLAGIMLDT KNFVMRTGVR TFEAAAYLRK MGADTIAVRQ FFSSSIETYQ
HRAHLVSQAE LYHHCAIAVA DEVFNDIKLV APQAADELLG IRSVAASFVL YSLNGEVNIS
ARFMGSMNVQ VVMEKLGGGG HQTMAATQIP DITVAEAKQQ LLQVLAEEFA QPEQSK
//
