ID A8MKJ8_ALKOO Unreviewed; 670 AA.
AC A8MKJ8;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 10-JUN-2026, entry version 76.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN OrderedLocusNames=Clos_2799 {ECO:0000313|EMBL:ABW20330.1};
OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS OhILAs)).
OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC Natronincolaceae; Alkaliphilus.
OX NCBI_TaxID=350688 {ECO:0000313|EMBL:ABW20330.1, ECO:0000313|Proteomes:UP000000269};
RN [1] {ECO:0000313|Proteomes:UP000000269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OhILAs {ECO:0000313|Proteomes:UP000000269};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL Submitted (OCT-2007) 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|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC -!- SIMILARITY: Belongs to the GdpP/PdeA phosphodiesterase family.
CC {ECO:0000256|PIRNR:PIRNR026583}.
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DR EMBL; CP000853; ABW20330.1; -; Genomic_DNA.
DR RefSeq; WP_012160637.1; NC_009922.1.
DR AlphaFoldDB; A8MKJ8; -.
DR STRING; 350688.Clos_2799; -.
DR KEGG; aoe:Clos_2799; -.
DR eggNOG; COG3887; Bacteria.
DR HOGENOM; CLU_018278_0_0_9; -.
DR Proteomes; UP000000269; 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; IPR049553; GdpP-like_PAS.
DR InterPro; IPR014528; GdpP/PdeA.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
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 Pfam; PF21370; PAS_GdpP; 1.
DR PIRSF; PIRSF026583; YybT; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50887; GGDEF; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR026583}; Hydrolase {ECO:0000256|PIRNR:PIRNR026583};
KW Manganese {ECO:0000256|PIRSR:PIRSR026583-50};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR026583};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR026583-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000000269};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 167..317
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT BINDING 360
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 364
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 366
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 433
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 433
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 457
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 512
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
SQ SEQUENCE 670 AA; 75930 MW; 59AD32E8233DA2D7 CRC64;
MKAIRNSKFI KMLVPDTRIY LIMLFIFILI ISYYNKAIGI IGIFLLAYLI YYNLKISNIR
REEWTKYIEG LSSDIDSATK YAVLNLPIPL TIVEFDGTIT WYNRKFLEVL DTKDLLEKDI
QDIIPNFDLR NLLQTENELS EVMNINNKYF KVVYNIVKLP KGHTSNYIIM LYWIDVTKFE
ELAKKYYREQ MVVGLIQVDN YDEVMQSTEE MRRPLVGAEI EHRLNLWAGK INGFIRKYSK
DKFMVIFQHE YLEKLEQKKF EIIDEIREIN QGNTMPITLS IGIGVYGENA LQTWNFANGA
KDLALGRGGD QVAVKKGDKI SFYGGKAKAV EKRTKVKARV VSHALRELID QSTNVIVMGH
KISDLDAFGS ALGIYRAAKN RGKDAYIVLN GSNPSIEGLL DRIYEIEEYN SVIISCDEAK
VKTLRTSLLV VVDTHRPNFT ECPELLKISD KIVLIDHHRK GTDFIENAVL NYHETYASST
SELVTELLSY MEEKISMPPI EADALLAGIA VDTKNFTFKT GVRTFEAASI LRRAGADTTS
VKQLFEDEFN TIITRADVIR RAEIIYQTIA ISTVEDISRA SQLIAAQAAD ELLDARGITA
SFVLGRKDDT MVFISGRSMG DINVQVILEK LGGGGHMTIA GAQIEGISME EAKEALEAAI
EEYFEEGEEE
//
