(data stored in ACNUC7421 zone)

SWISSPROT: C5B776_EDWI9

ID   C5B776_EDWI9            Unreviewed;       178 AA.
AC   C5B776;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 42.
DE   RecName: Full=Non-canonical purine NTP phosphatase {ECO:0000256|HAMAP-Rule:MF_00648};
DE            EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_00648};
DE   AltName: Full=Non-standard purine NTP phosphatase {ECO:0000256|HAMAP-Rule:MF_00648};
DE   AltName: Full=Nucleoside-triphosphate phosphatase {ECO:0000256|HAMAP-Rule:MF_00648};
DE            Short=NTPase {ECO:0000256|HAMAP-Rule:MF_00648};
GN   OrderedLocusNames=NT01EI_0622 {ECO:0000313|EMBL:ACR67849.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67849.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphatase that hydrolyzes non-canonical purine
CC       nucleotides such as XTP and ITP to their respective diphosphate
CC       derivatives. Probably excludes non-canonical purines from DNA
CC       precursor pool, thus preventing their incorporation into DNA and
CC       avoiding chromosomal lesions. {ECO:0000256|HAMAP-Rule:MF_00648}.
CC   -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
CC       nucleoside diphosphate + monophosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_00648}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00648};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00648};
CC       Note=Binds 1 divalent metal cation per subunit; can use either
CC       Mg(2+) or Mn(2+). {ECO:0000256|HAMAP-Rule:MF_00648};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00648}.
CC   -!- SIMILARITY: Belongs to the YjjX NTPase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00648}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00648}.
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DR   EMBL; CP001600; ACR67849.1; -; Genomic_DNA.
DR   RefSeq; WP_015870047.1; NC_012779.2.
DR   ProteinModelPortal; C5B776; -.
DR   STRING; 634503.NT01EI_0622; -.
DR   EnsemblBacteria; ACR67849; ACR67849; NT01EI_0622.
DR   GeneID; 7960390; -.
DR   KEGG; eic:NT01EI_0622; -.
DR   PATRIC; fig|634503.3.peg.565; -.
DR   eggNOG; ENOG4108K16; Bacteria.
DR   eggNOG; COG1986; LUCA.
DR   HOGENOM; HOG000098033; -.
DR   OMA; MALIPRM; -.
DR   OrthoDB; POG091H04D1; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:UniProtKB-HAMAP.
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.
DR   TIGRFAMs; TIGR00258; TIGR00258; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B776.
DR   SWISS-2DPAGE; C5B776.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00648};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00648};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00648};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00648};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00648};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00648};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN        7    164       NTPase_I-T. {ECO:0000259|Pfam:PF01931}.
FT   REGION       68     69       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00648}.
FT   METAL        38     38       Manganese or magnesium.
FT                                {ECO:0000256|HAMAP-Rule:MF_00648}.
FT   METAL        68     68       Manganese or magnesium.
FT                                {ECO:0000256|HAMAP-Rule:MF_00648}.
SQ   SEQUENCE   178 AA;  19712 MW;  4080C1CB6893347E CRC64;
     MYHVVAATTN PAKIQAITLA FDATFGAGQY RIEGIDVDSG VPEQPLGSIQ TRSGARHRVI
     CARQLRPEAD FWVGIEAGIE DNMTFAWMSV ENRCHRGESR SASLTLPDRV MDGIRQGQTL
     GYEMRRLSGI DDINRREGAI GIFTQGRLSR TSVYYQALLL ALAALEPGYH HKPPPHYA
//

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