ID A0A199UIN7_ANACO Unreviewed; 209 AA.
AC A0A199UIN7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 Name=LOC109714245 {ECO:0000313|RefSeq:XP_020094355.1,
GN ECO:0000313|RefSeq:XP_020094356.1};
GN ORFNames=ACMD2_01920 {ECO:0000313|EMBL:OAY64599.1};
OS Ananas comosus (Pineapple) (Ananas ananas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC Bromelioideae; Ananas.
OX NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY64599.1, ECO:0000313|Proteomes:UP000092600};
RN [1] {ECO:0000313|EMBL:OAY64599.1, ECO:0000313|Proteomes:UP000092600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY64599.1};
RX PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA Redwan R.M., Saidin A., Kumar S.V.;
RT "The draft genome of MD-2 pineapple using hybrid error correction of long
RT reads.";
RL DNA Res. 0:0-0(2016).
RN [2] {ECO:0000313|RefSeq:XP_020094355.1, ECO:0000313|RefSeq:XP_020094356.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_020094355.1,
RC ECO:0000313|RefSeq:XP_020094356.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 distinguish
CC between the deoxy- and ribose forms. Probably excludes non-canonical
CC purines from RNA and DNA precursor pools, thus preventing their
CC incorporation into RNA and DNA and avoiding chromosomal lesions.
CC {ECO:0000256|HAMAP-Rule:MF_03148}.
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=3.6.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
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=3.6.1.9;
CC Evidence={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; EC=3.6.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
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=3.6.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
CC Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+)
CC or Mn(2+). {ECO:0000256|HAMAP-Rule:MF_03148};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03148}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148}.
CC -!- SIMILARITY: Belongs to the HAM1 NTPase family.
CC {ECO:0000256|ARBA:ARBA00008023, ECO:0000256|HAMAP-Rule:MF_03148,
CC ECO:0000256|RuleBase:RU003781}.
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DR EMBL; LSRQ01007777; OAY64599.1; -; Genomic_DNA.
DR RefSeq; XP_020094355.1; XM_020238766.1.
DR RefSeq; XP_020094356.1; XM_020238767.1.
DR STRING; 4615.A0A199UIN7; -.
DR EnsemblPlants; Aco014641.1.mrna1; Aco014641.1.mrna1; Aco014641.1.path1.
DR EnsemblPlants; Aco014642.1.mrna1; Aco014642.1.mrna1; Aco014642.1.path1.
DR GeneID; 109714245; -.
DR Gramene; Aco014641.1.mrna1; Aco014641.1.mrna1; Aco014641.1.path1.
DR Gramene; Aco014642.1.mrna1; Aco014642.1.mrna1; Aco014642.1.path1.
DR OrthoDB; 479at2759; -.
DR Proteomes; UP000092600; Unassembled WGS sequence.
DR Proteomes; UP000515123; Linkage group 8.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR027502; ITPase.
DR InterPro; IPR029001; ITPase-like_fam.
DR InterPro; IPR002637; RdgB/HAM1.
DR NCBIfam; TIGR00042; RdgB/HAM1 family non-canonical purine NTP pyrophosphatase; 1.
DR PANTHER; PTHR11067:SF9; INOSINE TRIPHOSPHATE PYROPHOSPHATASE; 1.
DR PANTHER; PTHR11067; INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN; 1.
DR Pfam; PF01725; Ham1p_like; 1.
DR SUPFAM; SSF52972; ITPase-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03148};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03148};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03148};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_03148};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03148};
KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_03148};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03148};
KW Reference proteome {ECO:0000313|Proteomes:UP000092600}.
FT BINDING 19..24
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 59
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 75..76
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 151..154
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 174
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 179..180
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
SQ SEQUENCE 209 AA; 23146 MW; 400128D493A068A3 CRC64;
MSESVRTTLV LPGPVTFVTG NPKKLEEFRA ILGTSIPFRS LKLDLPELQG EPEEISKEKA
RLAATQVNGP VLVEDTCLCF NALKGLPGPY IKWFLQKIGH EGLNNILKAY EDKSAYAMCI
FSLALGPTSE PITFVGKTEG KIVPPRGPAD FGWDPIFEPD GYEQTYAEMP KEEKNKISHR
SKALAMVKTH FATADYAFQI YVSDFSLLS
//
