位置:首页 > 蛋白库 > NCPP_SULIY
NCPP_SULIY
ID   NCPP_SULIY              Reviewed;         176 AA.
AC   C3N7X4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Probable inosine/xanthosine triphosphatase {ECO:0000255|HAMAP-Rule:MF_00648};
DE            Short=ITPase/XTPase {ECO:0000255|HAMAP-Rule:MF_00648};
DE            EC=3.6.1.73 {ECO:0000255|HAMAP-Rule:MF_00648};
DE   AltName: Full=Non-canonical purine NTP phosphatase {ECO:0000255|HAMAP-Rule:MF_00648};
DE   AltName: Full=Non-standard purine NTP phosphatase {ECO:0000255|HAMAP-Rule:MF_00648};
DE   AltName: Full=Nucleoside-triphosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_00648};
DE            Short=NTPase {ECO:0000255|HAMAP-Rule:MF_00648};
GN   OrderedLocusNames=YG5714_0048;
OS   Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=439386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.G.57.14 / Yellowstone #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Phosphatase that hydrolyzes non-canonical purine nucleotides
CC       such as XTP and ITP to their respective diphosphate derivatives.
CC       Probably excludes non-canonical purines from DNA/RNA precursor pool,
CC       thus preventing their incorporation into DNA/RNA and avoiding
CC       chromosomal lesions. {ECO:0000255|HAMAP-Rule:MF_00648}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + XTP = H(+) + phosphate + XDP; Xref=Rhea:RHEA:28406,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:59884, ChEBI:CHEBI:61314; EC=3.6.1.73;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + ITP = H(+) + IDP + phosphate; Xref=Rhea:RHEA:28330,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58280, ChEBI:CHEBI:61402; EC=3.6.1.73;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00648};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00648};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00648};
CC       Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+)
CC       or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_00648};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00648}.
CC   -!- SIMILARITY: Belongs to the YjjX NTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00648}.
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; CP001403; ACP44342.1; -; Genomic_DNA.
DR   RefSeq; WP_012712728.1; NC_012622.1.
DR   AlphaFoldDB; C3N7X4; -.
DR   SMR; C3N7X4; -.
DR   EnsemblBacteria; ACP44342; ACP44342; YG5714_0048.
DR   GeneID; 7811421; -.
DR   GeneID; 8759887; -.
DR   KEGG; siy:YG5714_0048; -.
DR   HOGENOM; CLU_087417_0_0_2; -.
DR   OMA; ADYWVGI; -.
DR   Proteomes; UP000002308; Chromosome.
DR   GO; GO:0103023; F:ITPase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_00648; Non_canon_purine_NTPase_YjjX; 1.
DR   InterPro; IPR029001; ITPase-like_fam.
DR   InterPro; IPR002786; Non_canon_purine_NTPase.
DR   InterPro; IPR026533; NTPase/PRRC1.
DR   Pfam; PF01931; NTPase_I-T; 1.
DR   SUPFAM; SSF52972; SSF52972; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism;
KW   Nucleotide-binding.
FT   CHAIN           1..176
FT                   /note="Probable inosine/xanthosine triphosphatase"
FT                   /id="PRO_1000212396"
FT   BINDING         36
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00648"
SQ   SEQUENCE   176 AA;  19114 MW;  4E93D10E0DB5682B CRC64;
     MVTIALGSKN PVKINATKEA LDVLKLNWDL IGIEVDSGVD KQPFCDQTYV GARNRALNVI
     RVTNADIGLG IEGGVCNVYG KFIANAVVYV ITKEGLENFA ISSSFTLPSS MVSLILQGKE
     LGEASDIIFK TNNSKTKEGA IGLLTNNVIN RKMLYVQPIV LALYPIYNTM INNTPF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024