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ITPA_ENCCU
ID   ITPA_ENCCU              Reviewed;         192 AA.
AC   Q8SS24;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 90.
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   OrderedLocusNames=ECU04_1180;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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; AL590444; CAD25306.1; -; Genomic_DNA.
DR   RefSeq; NP_584802.1; NM_001041152.1.
DR   AlphaFoldDB; Q8SS24; -.
DR   SMR; Q8SS24; -.
DR   STRING; 284813.Q8SS24; -.
DR   GeneID; 858950; -.
DR   KEGG; ecu:ECU04_1180; -.
DR   VEuPathDB; MicrosporidiaDB:ECU04_1180; -.
DR   HOGENOM; CLU_082080_1_0_1; -.
DR   InParanoid; Q8SS24; -.
DR   OMA; GYCDGRK; -.
DR   OrthoDB; 1298391at2759; -.
DR   Proteomes; UP000000819; Chromosome IV.
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:0036218; F:dTTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036220; F:ITP diphosphatase activity; IEA:RHEA.
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: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; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..192
FT                   /note="Inosine triphosphate pyrophosphatase"
FT                   /id="PRO_0000413139"
FT   BINDING         8..13
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         34
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         46
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         64..65
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         81
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         141..144
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   192 AA;  21149 MW;  F6BA42A8B3B40F82 CRC64;
     MGRIYFATTN LKKLKEIRSL FEADIVHMNI PMVEIQASLE RIVDHKLNQV VPCIGEGDAV
     IVDDTAVAFE GLYGFPGVYI KDFLRIGSRK ISEIVGKIGN SNATAFCCLG IAHYRDGRVV
     KKVFFGELEG SIVESKEDGL EGFDYIFLPS GSSMCLGDMP VDEKNRISHR RIASKKLADY
     MASVGIIKAH GS
 
 
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