(data stored in ACNUC7421 zone)

SWISSPROT: C6B0G3_RHILS

ID   C6B0G3_RHILS            Unreviewed;       206 AA.
AC   C6B0G3;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   RecName: Full=dTTP/UTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00528};
DE            Short=dTTPase/UTPase {ECO:0000256|HAMAP-Rule:MF_00528};
DE            EC=3.6.1.9 {ECO:0000256|HAMAP-Rule:MF_00528};
DE   AltName: Full=Nucleoside triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00528};
DE   AltName: Full=Nucleotide pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00528};
DE            Short=Nucleotide PPase {ECO:0000256|HAMAP-Rule:MF_00528};
GN   OrderedLocusNames=Rleg_0271 {ECO:0000313|EMBL:ACS54582.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54582.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54582.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54582.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes
CC       dTTP and UTP. May have a dual role in cell division arrest and in
CC       preventing the incorporation of modified nucleotides into cellular
CC       nucleic acids. {ECO:0000256|HAMAP-Rule:MF_00528}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UTP = diphosphate + H(+) + UMP;
CC         Xref=Rhea:RHEA:29395, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865;
CC         EC=3.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00528};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTTP + H2O = diphosphate + dTMP + H(+);
CC         Xref=Rhea:RHEA:28534, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:63528;
CC         EC=3.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00528};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00528,
CC         ECO:0000256|SAAS:SAAS01154128};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00528,
CC       ECO:0000256|SAAS:SAAS00965376}.
CC   -!- SIMILARITY: Belongs to the Maf family. YhdE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00528}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00528}.
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DR   EMBL; CP001622; ACS54582.1; -; Genomic_DNA.
DR   RefSeq; WP_012755992.1; NC_012850.1.
DR   EnsemblBacteria; ACS54582; ACS54582; Rleg_0271.
DR   KEGG; rlg:Rleg_0271; -.
DR   HOGENOM; HOG000241745; -.
DR   KO; K06287; -.
DR   OMA; RIDGDFY; -.
DR   OrthoDB; 1469203at2; -.
DR   BioCyc; RLEG395491:GHX2-275-MONOMER; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:InterPro.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00555; Maf; 1.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_00528; Maf; 1.
DR   InterPro; IPR029001; ITPase-like_fam.
DR   InterPro; IPR003697; Maf-like.
DR   PANTHER; PTHR43213; PTHR43213; 1.
DR   Pfam; PF02545; Maf; 1.
DR   PIRSF; PIRSF006305; Maf; 1.
DR   SUPFAM; SSF52972; SSF52972; 1.
DR   TIGRFAMs; TIGR00172; maf; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B0G3.
DR   SWISS-2DPAGE; C6B0G3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00528,
KW   ECO:0000256|SAAS:SAAS00965379};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00528,
KW   ECO:0000256|SAAS:SAAS01154120};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00528,
KW   ECO:0000256|SAAS:SAAS01154126}.
FT   ACT_SITE     79     79       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00528}.
FT   SITE         15     15       Important for substrate specificity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00528}.
FT   SITE         80     80       Important for substrate specificity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00528}.
FT   SITE        163    163       Important for substrate specificity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00528}.
SQ   SEQUENCE   206 AA;  22613 MW;  173BFCE63C39659A CRC64;
     MALKYKLILA SGSPRRVDLL NQAGIEPSRL MPMDIDEAPK KSEHPRSLAR RLSAEKAEAA
     LAAIKGDITW KGSYILSADT VVAVGRRILG KAEFADEALS SLHLLSGRNH MVYTGVCLVT
     PDRKIRQKIV ETKVRFKRLS GFEIENYLAS GQWRGKAGAY GIQGLAGTFV QKMVGSYTNV
     VGLPLYETIL LLTGEGFDVH SRWPEG
//

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