ID F8LBA9_9BACT Unreviewed; 200 AA. AC F8LBA9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-DEC-2022, entry version 38. DE RecName: Full=dITP/XTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE EC=3.6.1.66 {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE Short=NTPase {ECO:0000256|HAMAP-Rule:MF_01405}; GN Name=hamA {ECO:0000313|EMBL:CCB90773.1}; GN ORFNames=WCH_BS10310 {ECO:0000313|EMBL:CCB90773.1}; OS Waddlia chondrophila 2032/99. OC Bacteria; Chlamydiae; Parachlamydiales; Waddliaceae; Waddlia. OX NCBI_TaxID=765953 {ECO:0000313|EMBL:CCB90773.1}; RN [1] {ECO:0000313|EMBL:CCB90773.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2032/99 {ECO:0000313|EMBL:CCB90773.1}; RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C., RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T., RA Myers G.S.A., Horn M.; RT "Unity in variety -- the pan-genome of the Chlamydiae."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of nucleoside CC triphosphates to their monophosphate derivatives, with a high CC preference for the non-canonical purine nucleotides XTP (xanthosine CC triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to CC function as a house-cleaning enzyme that removes non-canonical purine CC nucleotides from the nucleotide pool, thus preventing their CC incorporation into DNA/RNA and avoiding chromosomal lesions. CC {ECO:0000256|HAMAP-Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + ITP = diphosphate + H(+) + IMP; Xref=Rhea:RHEA:29399, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; EC=3.6.1.66; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + XTP = diphosphate + H(+) + XMP; Xref=Rhea:RHEA:28610, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57464, ChEBI:CHEBI:61314; EC=3.6.1.66; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dITP + H2O = dIMP + diphosphate + H(+); Xref=Rhea:RHEA:28342, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:61194, ChEBI:CHEBI:61382; EC=3.6.1.66; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. CC {ECO:0000256|ARBA:ARBA00008023, ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|RuleBase:RU003781}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FR872638; CCB90773.1; -; Genomic_DNA. DR AlphaFoldDB; F8LBA9; -. DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0036220; F:ITP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro. DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00515; HAM1; 1. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1. DR InterPro; IPR020922; dITP/XTP_pyrophosphatase. DR InterPro; IPR002637; Ham1p-like. DR InterPro; IPR029001; ITPase-like_fam. DR PANTHER; PTHR11067; INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN; 1. DR Pfam; PF01725; Ham1p_like; 1. DR SUPFAM; SSF52972; ITPase-like; 1. DR TIGRFAMs; TIGR00042; non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01405}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01405}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01405}; Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01405}. FT ACT_SITE 70 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 7..12 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 41 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 70 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 71 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 153..156 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 176 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 181..182 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" SQ SEQUENCE 200 AA; 22620 MW; 30CDEA02925288CA CRC64; MELILATHNL HKIREFRQIL KEVKGLDLIS LRNFPDYQLP EETGKTFQEN ADLKALHAAK MLKAIVLADD SGLVVPALQG APGIYSARYA SSDATDKENR EKLMQEMEKF EDLDRSAYYE CCITIAGPEG ILKTAKATCE GLIGEQEKGR NGFGYDPIFI KHDYDKTFAE LEEQTKNRIS HRRKALDKIL AFLEAQIPSE //