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ITPA_DROME
ID   ITPA_DROME              Reviewed;         191 AA.
AC   Q9VMW7;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 130.
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=CG8891;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo, and Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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   -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_03148}.
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DR   EMBL; AE014134; AAF52191.1; -; Genomic_DNA.
DR   EMBL; AY071428; AAL49050.1; -; mRNA.
DR   RefSeq; NP_608890.1; NM_135046.5.
DR   AlphaFoldDB; Q9VMW7; -.
DR   SMR; Q9VMW7; -.
DR   BioGRID; 59902; 9.
DR   STRING; 7227.FBpp0078684; -.
DR   PaxDb; Q9VMW7; -.
DR   PRIDE; Q9VMW7; -.
DR   DNASU; 33718; -.
DR   EnsemblMetazoa; FBtr0079048; FBpp0078684; FBgn0031663.
DR   GeneID; 33718; -.
DR   KEGG; dme:Dmel_CG8891; -.
DR   UCSC; CG8891-RA; d. melanogaster.
DR   FlyBase; FBgn0031663; CG8891.
DR   VEuPathDB; VectorBase:FBgn0031663; -.
DR   eggNOG; KOG3222; Eukaryota.
DR   GeneTree; ENSGT00390000015399; -.
DR   HOGENOM; CLU_082080_1_1_1; -.
DR   InParanoid; Q9VMW7; -.
DR   OMA; DCFADDT; -.
DR   OrthoDB; 1298391at2759; -.
DR   PhylomeDB; Q9VMW7; -.
DR   Reactome; R-DME-74259; Purine catabolism.
DR   BioGRID-ORCS; 33718; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 33718; -.
DR   PRO; PR:Q9VMW7; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0031663; Expressed in eye disc (Drosophila) and 24 other tissues.
DR   Genevisible; Q9VMW7; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central.
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:0009143; P:nucleoside triphosphate catabolic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..191
FT                   /note="Inosine triphosphate pyrophosphatase"
FT                   /id="PRO_0000413109"
FT   BINDING         9..14
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         166
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         171..172
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
SQ   SEQUENCE   191 AA;  21449 MW;  73F7260BD56FAF1E CRC64;
     MSKPITFVTG NAKKLEELVA ILGPSFPRTI VSKKIDLPEL QGDIDEIAIK KCKEAARQVN
     GPVLVEDTSL CFNALEGLPG PYIKWFLEKL QPEGLHRLLH GWENKSAQAI CTFGYCDGVD
     AEPLIFKGIT EGVIVEPRGP RDFGWDPVFQ PSGYDKTYAE LPKSEKNTIS HRYRALALLR
     QHFEKQDKLI N
 
 
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