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Database: UniProt
Entry: ITPA_COLGM
LinkDB: ITPA_COLGM
Original site: ITPA_COLGM 
ID   ITPA_COLGM              Reviewed;         184 AA.
AC   E3QBC5;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   13-SEP-2023, entry version 47.
DE   RecName: Full=Inosine triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
DE            Short=ITPase {ECO:0000255|HAMAP-Rule:MF_03148};
DE            Short=Inosine triphosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
DE            EC=3.6.1.9 {ECO:0000255|HAMAP-Rule:MF_03148};
DE   AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
DE   AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
DE   AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
DE   AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
DE            Short=NTPase {ECO:0000255|HAMAP-Rule:MF_03148};
GN   ORFNames=GLRG_03307;
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212;
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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:0000255|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:0000255|HAMAP-Rule:MF_03148};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23997;
CC         Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_03148};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44645;
CC         Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_03148};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29400;
CC         Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_03148};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28343;
CC         Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_03148};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28611;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
CC       Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+)
CC       or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_03148};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03148}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03148}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03148}.
CC   -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_03148}.
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DR   EMBL; GG697339; EFQ28163.1; -; Genomic_DNA.
DR   RefSeq; XP_008092183.1; XM_008093992.1.
DR   AlphaFoldDB; E3QBC5; -.
DR   SMR; E3QBC5; -.
DR   STRING; 645133.E3QBC5; -.
DR   EnsemblFungi; EFQ28163; EFQ28163; GLRG_03307.
DR   GeneID; 24408672; -.
DR   VEuPathDB; FungiDB:GLRG_03307; -.
DR   eggNOG; KOG3222; Eukaryota.
DR   HOGENOM; CLU_082080_1_1_1; -.
DR   OrthoDB; 479at2759; -.
DR   Proteomes; UP000008782; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035870; F:dITP diphosphatase activity; IEA:RHEA.
DR   GO; GO:0036220; F:ITP diphosphatase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0036222; F:XTP diphosphatase activity; IEA:RHEA.
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; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..184
FT                   /note="Inosine triphosphate pyrophosphatase"
FT                   /id="PRO_0000413134"
FT   BINDING         11..16
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         51
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         67..68
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         84
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         143..146
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         164
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         169..170
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
SQ   SEQUENCE   184 AA;  20341 MW;  2F3AB67061D5DD14 CRC64;
     MSTTPVVNFI TGNANKLREV KAILEPGITV QSKTVNLEEV QGTVEEVTLA KCRKAAEIIQ
     GPVLVEDTCL CFKALNDLPG PYIKWFMESI GHQGLNNLLV AYEDKSADAV CTFAYSPGPG
     HEPILFQGRT RGKIVPPRGP ADFGWDAIFE YDGQTYAEMD KTAKNNISHR GLALRKLQDW
     FAQQ
//
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