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Database: UniProt/TrEMBL
Entry: B6J602_COXB1
LinkDB: B6J602_COXB1
Original site: B6J602_COXB1 
ID   B6J602_COXB1            Unreviewed;       200 AA.
AC   B6J602;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   26-NOV-2014, entry version 42.
DE   RecName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00101763};
DE            EC=3.6.1.19 {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00101728};
DE   AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE   AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE   AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
GN   OrderedLocusNames=CbuK_1988 {ECO:0000313|EMBL:ACJ21093.1};
OS   Coxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain
OS   Q154)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Coxiellaceae; Coxiella.
OX   NCBI_TaxID=434924 {ECO:0000313|EMBL:ACJ21093.1, ECO:0000313|Proteomes:UP000002504};
RN   [1] {ECO:0000313|EMBL:ACJ21093.1, ECO:0000313|Proteomes:UP000002504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CbuK_Q154 {ECO:0000313|EMBL:ACJ21093.1,
RC   ECO:0000313|Proteomes:UP000002504};
RX   PubMed=19047403; DOI=10.1128/IAI.01141-08;
RA   Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA   Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F.,
RA   Samuel J.E., Heinzen R.A.;
RT   "Comparative genomics reveal extensive transposon-mediated genomic
RT   plasticity and diversity among potential effector proteins within the
RT   genus Coxiella.";
RL   Infect. Immun. 77:642-656(2009).
CC   -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine
CC       nucleotides such as XTP and ITP/dITP to their respective
CC       monophosphate derivatives. Might exclude non-canonical purines
CC       from DNA precursor pool, thus preventing their incorporation into
CC       DNA and avoiding chromosomal lesions. {ECO:0000256|HAMAP-
CC       Rule:MF_01405}.
CC   -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
CC       nucleotide + diphosphate. {ECO:0000256|HAMAP-Rule:MF_01405,
CC       ECO:0000256|SAAS:SAAS00101772}.
CC   -!- COFACTOR:
CC       Note=Binds 1 divalent metal cation ion per subunit; can use either
CC       magnesium or manganese. {ECO:0000256|HAMAP-Rule:MF_01405,
CC       ECO:0000256|SAAS:SAAS00101777};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405,
CC       ECO:0000256|SAAS:SAAS00101722}.
CC   -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01405, ECO:0000256|RuleBase:RU003781}.
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DR   EMBL; CP001020; ACJ21093.1; -; Genomic_DNA.
DR   RefSeq; WP_005769347.1; NC_011528.1.
DR   RefSeq; YP_002306238.1; NC_011528.1.
DR   ProteinModelPortal; B6J602; -.
DR   SMR; B6J602; 1-195.
DR   STRING; 434924.CbuK_1988; -.
DR   EnsemblBacteria; ACJ21093; ACJ21093; CbuK_1988.
DR   GeneID; 7016501; -.
DR   KEGG; cbc:CbuK_1988; -.
DR   PATRIC; 17919423; VBICoxBur77120_1988.
DR   eggNOG; COG0127; -.
DR   HOGENOM; HOG000293319; -.
DR   KO; K02428; -.
DR   OrthoDB; EOG6CZQQP; -.
DR   BioCyc; CBUR434924:GHWU-1983-MONOMER; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_01405; Non_canon_purine_NTPase; 1.
DR   InterPro; IPR002637; Ham1p-like.
DR   InterPro; IPR029001; ITPase-like_fam.
DR   InterPro; IPR020922; NTPase.
DR   PANTHER; PTHR11067; PTHR11067; 1.
DR   Pfam; PF01725; Ham1p_like; 1.
DR   SUPFAM; SSF52972; SSF52972; 1.
DR   TIGRFAMs; TIGR00042; TIGR00042; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002504};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|RuleBase:RU003781};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00101735};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00101759};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00101767};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00101755};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00101739}.
FT   REGION        8     13       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION       69     70       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   METAL        40     40       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01405}.
FT   METAL        69     69       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01405}.
FT   BINDING     157    157       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING     177    177       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING     183    183       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
SQ   SEQUENCE   200 AA;  21777 MW;  A35DF16EE7025113 CRC64;
     MLEIVLASQN SSKLAEMQEL LRDLEIKFIP QTEFSVPDIE ETGSTFVENA IIKARHAAKQ
     TGLPALADDS GLTIAALNSA PGVFSSRYAG KNATDAERIQ KVLEALEAAD DSDRSASFHC
     VIALMENEND PAPLICHGVW EGEIAREPRG KNGFGYDPIF YVPSHQRTAA ELDPQEKNAI
     SHRGQALEQL STVLTEAFLV
//
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