ID A2U357_9FLAO Unreviewed; 295 AA.
AC A2U357;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase {ECO:0000256|ARBA:ARBA00016378};
DE EC=3.6.1.13 {ECO:0000256|ARBA:ARBA00012453};
DE EC=3.6.1.16 {ECO:0000256|ARBA:ARBA00012443};
DE EC=3.6.1.53 {ECO:0000256|ARBA:ARBA00012529};
DE AltName: Full=ADPRibase-Mn {ECO:0000256|ARBA:ARBA00032579};
DE AltName: Full=CDP-choline phosphohydrolase {ECO:0000256|ARBA:ARBA00030848};
GN ORFNames=MED152_12824 {ECO:0000313|EMBL:EAQ40921.2};
OS Polaribacter sp. MED152.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=313598 {ECO:0000313|EMBL:EAQ40921.2, ECO:0000313|Proteomes:UP000006470};
RN [1] {ECO:0000313|EMBL:EAQ40921.2, ECO:0000313|Proteomes:UP000006470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED152 {ECO:0000313|EMBL:EAQ40921.2};
RX PubMed=17215843; DOI=10.1038/nature05381;
RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA Neutze R., Pedros-Alio C., Pinhassi J.;
RT "Light stimulates growth of proteorhodopsin-containing marine
RT Flavobacteria.";
RL Nature 445:210-213(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+);
CC Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC EC=3.6.1.13; Evidence={ECO:0000256|ARBA:ARBA00001454};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+);
CC Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC EC=3.6.1.53; Evidence={ECO:0000256|ARBA:ARBA00001583};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CDP-choline + H2O = CMP + 2 H(+) + phosphocholine;
CC Xref=Rhea:RHEA:32487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:295975;
CC EC=3.6.1.53; Evidence={ECO:0000256|ARBA:ARBA00001789};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CDP-glycerol + H2O = CMP + 2 H(+) + sn-glycerol 3-phosphate;
CC Xref=Rhea:RHEA:21692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:58311, ChEBI:CHEBI:60377; EC=3.6.1.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001209};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the ADPRibase-Mn family.
CC {ECO:0000256|ARBA:ARBA00006362}.
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DR EMBL; CP004349; EAQ40921.2; -; Genomic_DNA.
DR RefSeq; WP_015482287.1; NC_020830.1.
DR AlphaFoldDB; A2U357; -.
DR STRING; 313598.MED152_12824; -.
DR KEGG; pom:MED152_12824; -.
DR eggNOG; COG1409; Bacteria.
DR HOGENOM; CLU_039893_2_0_10; -.
DR OrthoDB; 9791866at2; -.
DR Proteomes; UP000006470; Chromosome.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0047734; F:CDP-glycerol diphosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07396; MPP_Nbla03831; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041869; MPP_ADPRM.
DR PANTHER; PTHR16509; -; 1.
DR PANTHER; PTHR16509:SF1; MANGANESE-DEPENDENT ADP-RIBOSE_CDP-ALCOHOL DIPHOSPHATASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006470};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 25..243
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
SQ SEQUENCE 295 AA; 34552 MW; 7037701A32FF0481 CRC64;
MKNILFFLSI LVLITSCSTH KTTDFKIGII ADCQYCDCEI KWDRYYKKSP QRLKDAVTEL
NKDSLNYTIH LGDFIDQKMA SLDSILPTWH KLKSNTYHVL GNHDFDVGET NKEKIISKLD
LKNRYYSFSK SDWRFIVLDG NDLSFYGSTT KTKKQQTDSL YNLLKDKNLP YVKKYNGGLS
KTQLNWVKTE LEEAKAKNQN VGFYCHFPIY PIDQHNIWNR EQFLQIIKAY KNVKFFFNGH
NHAGGYEMVN NVHYLTFKGM VDTENTSAFA KAKFTKDTIF IQGYEREPSR KLVIK
//
