ID A0A0L8HK24_OCTBM Unreviewed; 189 AA. AC A0A0L8HK24; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 05-DEC-2018, entry version 19. DE RecName: Full=Inosine triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148}; DE Short=ITPase {ECO:0000256|HAMAP-Rule:MF_03148}; DE Short=Inosine triphosphatase {ECO:0000256|HAMAP-Rule:MF_03148}; DE EC=3.6.1.9 {ECO:0000256|HAMAP-Rule:MF_03148}; DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_03148}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148}; DE Short=NTPase {ECO:0000256|HAMAP-Rule:MF_03148}; GN ORFNames=OCBIM_22012863mg {ECO:0000313|EMBL:KOF89577.1}; OS Octopus bimaculoides (California two-spotted octopus). OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Cephalopoda; Coleoidea; OC Neocoleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; OC Octopus. OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF89577.1, ECO:0000313|Proteomes:UP000053454}; RN [1] {ECO:0000313|Proteomes:UP000053454} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Albertin C.B., Simakov O., Mitros T., Wang Z.Y., Pungot J.R., RA Edsinger-Gonzalez E., Brenner S., Ragsdale C.W., Rokhsar D.S.; RT "WGS assembly of Octopus bimaculoides."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine CC nucleotides such as inosine triphosphate (ITP), deoxyinosine CC triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their CC respective monophosphate derivatives. The enzyme does not CC distinguish between the deoxy- and ribose forms. Probably excludes CC non-canonical purines from RNA and DNA precursor pools, thus CC preventing their incorporation into RNA and DNA and avoiding CC chromosomal lesions. {ECO:0000256|HAMAP-Rule:MF_03148}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'- CC deoxyribonucleoside 5'-phosphate + diphosphate + H(+); CC Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; CC EC=3.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_03148, CC ECO:0000256|SAAS:SAAS00721545}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03148}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03148}; CC Note=Binds 1 divalent metal cation per subunit; can use either CC Mg(2+) or Mn(2+). {ECO:0000256|HAMAP-Rule:MF_03148}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03148, CC ECO:0000256|SAAS:SAAS00721538}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148, CC ECO:0000256|SAAS:SAAS00721546}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP- CC Rule:MF_03148, ECO:0000256|RuleBase:RU003781, CC ECO:0000256|SAAS:SAAS00721539}. 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; KQ417945; KOF89577.1; -; Genomic_DNA. DR RefSeq; XP_014771708.1; XM_014916222.1. DR EnsemblMetazoa; Ocbimv22012862m; Ocbimv22012862m.p; Ocbimv22012863m.g. DR GeneID; 106870217; -. DR Proteomes; UP000053454; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009204; P:deoxyribonucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. DR CDD; cd00515; HAM1; 1. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_03148; HAM1_NTPase; 1. DR InterPro; IPR002637; Ham1p-like. DR InterPro; IPR027502; ITPase. DR InterPro; IPR029001; ITPase-like_fam. DR PANTHER; PTHR11067; PTHR11067; 1. DR Pfam; PF01725; Ham1p_like; 1. DR SUPFAM; SSF52972; SSF52972; 1. DR TIGRFAMs; TIGR00042; TIGR00042; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053454}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148, KW ECO:0000256|SAAS:SAAS00721512}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03148, KW ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00721541}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03148, KW ECO:0000256|SAAS:SAAS00721547}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_03148}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03148, KW ECO:0000256|SAAS:SAAS00721543}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_03148, KW ECO:0000256|SAAS:SAAS00721522}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03148, KW ECO:0000256|SAAS:SAAS00721527}; KW Reference proteome {ECO:0000313|Proteomes:UP000053454}. FT REGION 8 13 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03148}. FT REGION 66 67 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03148}. FT REGION 143 146 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03148}. FT REGION 171 172 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03148}. FT METAL 38 38 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_03148}. FT METAL 66 66 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_03148}. FT BINDING 50 50 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03148}. FT BINDING 166 166 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03148}. SQ SEQUENCE 189 AA; 21073 MW; F2A738AA39269B1C CRC64; MTTITFVTGN ANKLKEFIQI LGKNFPYKLI NENIDIPEYQ GESDDISRAK CLEAAKIVKG PVVVEDTSLC FNALGGLPGP YIKWFLDKLK PEGLHHLLHG FEDKSAYALC TLAFSTGNLE TPVLLFKGQT DGKIVEPSGP NDFGWDPCFQ PDGFDQTYAE MPKELKNSLS HRGKAVMAFK EHFMNKTLK //