(data stored in ACNUC7421 zone)

SWISSPROT: D4YWV4_SPHJU

ID   D4YWV4_SPHJU            Unreviewed;       197 AA.
AC   D4YWV4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   08-MAY-2019, entry version 43.
DE   RecName: Full=Nucleoside triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00528};
DE            EC=3.6.1.9 {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=SJA_C1-00020 {ECO:0000313|EMBL:BAI94836.1};
OS   Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26
OS   / NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI94836.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI94836.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S
RC   {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: Nucleoside triphosphate pyrophosphatase. May have a dual
CC       role in cell division arrest and in preventing the incorporation
CC       of modified nucleotides into cellular nucleic acids.
CC       {ECO:0000256|HAMAP-Rule:MF_00528}.
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;
CC         EC=3.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00528};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside
CC         5'-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: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. {ECO:0000256|HAMAP-
CC       Rule:MF_00528, ECO:0000256|SAAS:SAAS01154117}.
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; AP010803; BAI94836.1; -; Genomic_DNA.
DR   RefSeq; WP_013038685.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-00020; -.
DR   EnsemblBacteria; BAI94836; BAI94836; SJA_C1-00020.
DR   GeneID; 29271712; -.
DR   KEGG; sjp:SJA_C1-00020; -.
DR   eggNOG; ENOG4108UHJ; Bacteria.
DR   eggNOG; COG0424; LUCA.
DR   HOGENOM; HOG000241744; -.
DR   KO; K06287; -.
DR   OMA; CAGSFKA; -.
DR   BioCyc; SJAP452662:GHEL-2-MONOMER; -.
DR   Proteomes; UP000007753; Chromosome 1.
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.
PE   3: Inferred from homology;
DR   PRODOM; D4YWV4.
DR   SWISS-2DPAGE; D4YWV4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   ACT_SITE     73     73       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00528}.
SQ   SEQUENCE   197 AA;  21599 MW;  AC525DF54578B215 CRC64;
     MIVLASQSAS RRALLEAAQV PFEALSPGVD EEAAKEALRA DGLDARQLAD ALAELKALRV
     SRRVPGALVL GCDQTLSLDD GAMIDKAVDR SDAERILKLL SGRVHHLHSA AVIALNGEPI
     WRHIERVRMT VRPLSDAFIA HYLDGDWEQC RWCVGCYRIE GPGAQLFSRV EGSQFAIQGL
     PLLPLLDFLR IRGVLES
//

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