ID A0A316GBB0_9RHOB Unreviewed; 371 AA.
AC A0A316GBB0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=ADP-ribose pyrophosphatase {ECO:0000256|ARBA:ARBA00013297};
DE EC=3.6.1.13 {ECO:0000256|ARBA:ARBA00012453};
DE AltName: Full=ADP-ribose diphosphatase {ECO:0000256|ARBA:ARBA00030162};
DE AltName: Full=ADP-ribose phosphohydrolase {ECO:0000256|ARBA:ARBA00033056};
DE AltName: Full=Adenosine diphosphoribose pyrophosphatase {ECO:0000256|ARBA:ARBA00030308};
GN ORFNames=C8D95_10164 {ECO:0000313|EMBL:PWK58259.1};
OS Silicimonas algicola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1826607 {ECO:0000313|EMBL:PWK58259.1, ECO:0000313|Proteomes:UP000245390};
RN [1] {ECO:0000313|EMBL:PWK58259.1, ECO:0000313|Proteomes:UP000245390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103371 {ECO:0000313|EMBL:PWK58259.1,
RC ECO:0000313|Proteomes:UP000245390};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts on ADP-mannose and ADP-glucose as well as ADP-ribose.
CC Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme
CC is a limiting step of the gluconeogenic process.
CC {ECO:0000256|ARBA:ARBA00025164}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR604385-2};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudF subfamily.
CC {ECO:0000256|ARBA:ARBA00007482}.
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:PWK58259.1}.
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DR EMBL; QGGV01000001; PWK58259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316GBB0; -.
DR Proteomes; UP000245390; Unassembled WGS sequence.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03424; ADPRase_NUDT5; 1.
DR CDD; cd06661; GGCT_like; 1.
DR Gene3D; 3.10.490.10; Gamma-glutamyl cyclotransferase-like; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR009288; AIG2-like_dom.
DR InterPro; IPR013024; GGCT-like.
DR InterPro; IPR036568; GGCT-like_sf.
DR InterPro; IPR004385; NDP_pyrophosphatase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR NCBIfam; TIGR00052; nudix-type nucleoside diphosphatase, YffH/AdpP family; 1.
DR PANTHER; PTHR11839:SF5; ADP-RIBOSE PYROPHOSPHATASE; 1.
DR PANTHER; PTHR11839; UDP/ADP-SUGAR PYROPHOSPHATASE; 1.
DR Pfam; PF06094; GGACT; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF110857; Gamma-glutamyl cyclotransferase-like; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|PIRSR:PIRSR604385-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604385-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000245390}.
FT DOMAIN 218..358
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 249..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 261..283
FT /note="Nudix box"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-3"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
SQ SEQUENCE 371 AA; 40162 MW; BE04EA2ECE742DB0 CRC64;
MSQSVFFYGT LRDPALLALV AGREVSARPA SLPGFRTAQV EGHDFPTLVA DDDATAEGLL
AEVDARAQAR LDFYELGFGY DLRPVSVRTD KGAAVALVYF PEPGLWKPDG AWSLDGWQAD
GAPLARAAAE EYMRLHGVMD PASAARAFDQ IQMRAGARLR AAEAPTPAPL PPAMSAKDVR
IAETRQPYTA YFAVREDVLT FPRFSGGHSA PVLRSSFQGG DAVTVVPYDP ATDRLLVVRQ
FRHGPFTRGD ANPWTLEPAA GRIDAGETPE QTARRELLEE TGIEAGALHL ISRYYPSPGA
FNEYLWSYVA IADLSAQDGR IAGLEGENED ILSHVLGFDE AMAMVETGAA NTAPLVLTLF
WLAANRDRLR G
//
