ADPRM_DANRE
ID ADPRM_DANRE Reviewed; 322 AA.
AC Q7T291;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase;
DE EC=3.6.1.13;
DE EC=3.6.1.16;
DE EC=3.6.1.53;
DE AltName: Full=ADPRibase-Mn;
DE AltName: Full=CDP-choline phosphohydrolase;
GN Name=adprm; ORFNames=zgc:64213;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH ZINC.
RG Center for eukaryotic structural genomics (CESG);
RT "Crystal structure of a dimetal phosphatase from Danio rerio loc 393393.";
RL Submitted (DEC-2006) to the PDB data bank.
CC -!- FUNCTION: Hydrolyzes ADP-ribose, IDP-ribose, CDP-glycerol, CDP-choline
CC and CDP-ethanolamine, but not other non-reducing ADP-sugars or CDP-
CC glucose. {ECO:0000250}.
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;
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;
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;
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ADPRibase-Mn family. {ECO:0000305}.
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DR EMBL; BC054642; AAH54642.1; -; mRNA.
DR RefSeq; NP_956715.1; NM_200421.1.
DR PDB; 2NXF; X-ray; 1.70 A; A=2-322.
DR PDBsum; 2NXF; -.
DR AlphaFoldDB; Q7T291; -.
DR SMR; Q7T291; -.
DR STRING; 7955.ENSDARP00000096471; -.
DR PaxDb; Q7T291; -.
DR DNASU; 393393; -.
DR GeneID; 393393; -.
DR KEGG; dre:393393; -.
DR CTD; 56985; -.
DR ZFIN; ZDB-GENE-040426-1406; adprm.
DR eggNOG; ENOG502QUQW; Eukaryota.
DR InParanoid; Q7T291; -.
DR OrthoDB; 1263522at2759; -.
DR PhylomeDB; Q7T291; -.
DR BRENDA; 3.6.1.13; 928.
DR BRENDA; 3.6.1.53; 928.
DR Reactome; R-DRE-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR EvolutionaryTrace; Q7T291; -.
DR PRO; PR:Q7T291; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IDA:ZFIN.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IDA:ZFIN.
DR GO; GO:0047734; F:CDP-glycerol diphosphatase activity; IDA:ZFIN.
DR GO; GO:0030145; F:manganese ion binding; IDA:ZFIN.
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 Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..322
FT /note="Manganese-dependent ADP-ribose/CDP-alcohol
FT diphosphatase"
FT /id="PRO_0000286570"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2NXF"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2NXF"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:2NXF"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2NXF"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:2NXF"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:2NXF"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2NXF"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2NXF"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:2NXF"
FT HELIX 203..219
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:2NXF"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2NXF"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:2NXF"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 303..312
FT /evidence="ECO:0007829|PDB:2NXF"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:2NXF"
SQ SEQUENCE 322 AA; 36645 MW; 8C2BB1A16650934F CRC64;
MEDPVFTFGL IADVQYADIE DGENYLRTRR RYYRGSADLL RDAVLQWRRE RVQCVVQLGD
IIDGHNRRRD ASDRALDTVM AELDACSVDV HHVWGNHEFY NFSRPSLLSS RLNSAQRTGT
DTGSDLIGDD IYAYEFSPAP NFRFVLLDAY DLSVIGREEE SEKHTHSWRI LTQHNHNLQD
LNLPPVSVGL EQRFVKFNGG FSEQQLQWLD AVLTLSDHKQ ERVLIFSHLP VHPCAADPIC
LAWNHEAVLS VLRSHQSVLC FIAGHDHDGG RCTDSSGAQH ITLEGVIETP PHSHAFATAY
LYEDRMVMKG RGRVEDLTIT YS
