ID A0A2Y9BA38_9FIRM Unreviewed; 681 AA.
AC A0A2Y9BA38;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 10-JUN-2026, entry version 26.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=A8806_10235 {ECO:0000313|EMBL:PWJ31179.1};
OS Faecalicatena orotica.
OC Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
OC Lachnospiraceae; Faecalicatena.
OX NCBI_TaxID=1544 {ECO:0000313|EMBL:PWJ31179.1, ECO:0000313|Proteomes:UP000245845};
RN [1] {ECO:0000313|EMBL:PWJ31179.1, ECO:0000313|Proteomes:UP000245845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NLAE-zl-C242 {ECO:0000313|EMBL:PWJ31179.1,
RC ECO:0000313|Proteomes:UP000245845};
RA Kelly W.;
RT "The Hungate 1000. A catalogue of reference genomes from the rumen
RT microbiome.";
RL Submitted (MAY-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWJ31179.1}.
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DR EMBL; QGDL01000002; PWJ31179.1; -; Genomic_DNA.
DR RefSeq; WP_109729903.1; NZ_BAAACK010000006.1.
DR AlphaFoldDB; A0A2Y9BA38; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000245845; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 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 SUPFAM; SSF64182; DHH phosphoesterases; 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:UP000245845};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 366..522
FT /note="DDH"
FT /evidence="ECO:0000259|Pfam:PF01368"
FT DOMAIN 598..672
FT /note="DHHA1"
FT /evidence="ECO:0000259|Pfam:PF02272"
FT BINDING 372
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 376
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 378
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 446
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 446
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 470
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 525
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
SQ SEQUENCE 681 AA; 77197 MW; 0AD897646B56CD70 CRC64;
MGKKNMRLKG QLRMYMQWPL IMTVLLIAMN IWMYMIDRKA GVMMSVFVVV YLVIVGLLYF
YNRSLILADL IQFSTQYKGI QNTLLKELTI PYAILLEDGR ILWKNDSFND MIEGQKREKY
LNKLIPELNT GVFPREESDH VELEVVYKER DYQVELRRVS VEGFSEAEQL LQIPREKEYF
IAVYMKDVTE LNSYIRENED QRLIAGLIYI DNYDEVMESV EEVRQSLLVA LIDRKINKYI
GDIDGIVKKL EKDKYFIVIK KESYRKIEAD KFSLLEDVKQ VNIGNARSAT LSIGLGLNTS
TYAQSYNYAR VAIDLALARG GDQAVIKDCK GITYFGGKKE QTAKNTRVKA RVKAEALREF
IVAKDQVIVM GHKIGDADSL GACMGIYRAA VELEKKAHVV INEITTSVRP LYDEIAGSPA
YGKDIFLTSE QALDYVTDNT MVVVVDTNKP QMTECPELLK CSKTIAVLDH HRQSSNVIEN
AVLSYVEPYS SSTSEMVAEV LQYIVDDIKF PSVEADCLYA GIMIDTRNFM NRTGVRTFEA
AAFLRRCGAD ITRVRKMFRD DMESYRAKAE AVRMAEVYRD EYAIAQSPGD IESPTVLAAQ
AANELLDISG IKASFVLTIY EGRIYLSARS IDEVNVQIIA EKLGGGGHIN SAGAQFDHTN
MHQAIKVLKE TIDQMIEEGD I
//
