(data stored in SCRATCH zone)

SWISSPROT: Q13E55_RHOPS

ID   Q13E55_RHOPS            Unreviewed;       210 AA.
AC   Q13E55;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 83.
DE   RecName: Full=dITP/XTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE            EC=3.6.1.66 {ECO:0000256|HAMAP-Rule:MF_01405};
DE   AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
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};
DE            Short=NTPase {ECO:0000256|HAMAP-Rule:MF_01405};
GN   OrderedLocusNames=RPD_0396 {ECO:0000313|EMBL:ABE37634.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37634.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37634.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37634.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of
CC       nucleoside triphosphates to their monophosphate derivatives, with
CC       a high preference for the non-canonical purine nucleotides XTP
CC       (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and
CC       ITP. Seems to function as a house-cleaning enzyme that removes
CC       non-canonical purine nucleotides from the nucleotide pool, thus
CC       preventing their incorporation into DNA/RNA and avoiding
CC       chromosomal lesions. {ECO:0000256|HAMAP-Rule:MF_01405,
CC       ECO:0000256|SAAS:SAAS00805977}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + ITP = diphosphate + H(+) + IMP;
CC         Xref=Rhea:RHEA:29399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58053, ChEBI:CHEBI:61402;
CC         EC=3.6.1.66; Evidence={ECO:0000256|HAMAP-Rule:MF_01405,
CC         ECO:0000256|SAAS:SAAS01118622};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + XTP = diphosphate + H(+) + XMP;
CC         Xref=Rhea:RHEA:28610, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:61314;
CC         EC=3.6.1.66; Evidence={ECO:0000256|HAMAP-Rule:MF_01405,
CC         ECO:0000256|SAAS:SAAS01118649};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dITP + H2O = dIMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:28342, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:61194, ChEBI:CHEBI:61382;
CC         EC=3.6.1.66; Evidence={ECO:0000256|HAMAP-Rule:MF_01405,
CC         ECO:0000256|SAAS:SAAS01118637};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01405};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01405};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405,
CC       ECO:0000256|SAAS:SAAS00730484}.
CC   -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01405, ECO:0000256|RuleBase:RU003781,
CC       ECO:0000256|SAAS:SAAS00730348}.
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; CP000283; ABE37634.1; -; Genomic_DNA.
DR   RefSeq; WP_011500822.1; NC_007958.1.
DR   STRING; 316057.RPD_0396; -.
DR   EnsemblBacteria; ABE37634; ABE37634; RPD_0396.
DR   KEGG; rpd:RPD_0396; -.
DR   eggNOG; ENOG4108V82; Bacteria.
DR   eggNOG; COG0127; LUCA.
DR   HOGENOM; HOG000293319; -.
DR   KO; K02428; -.
DR   OMA; YDPIFQP; -.
DR   OrthoDB; 1824064at2; -.
DR   BioCyc; RPAL316057:RPD_RS02040-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
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-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00515; HAM1; 1.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_01405; Non_canon_purine_NTPase; 1.
DR   InterPro; IPR020922; dITP/XTP_pyrophosphatase.
DR   InterPro; IPR002637; Ham1p-like.
DR   InterPro; IPR029001; ITPase-like_fam.
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;
DR   PRODOM; Q13E55.
DR   SWISS-2DPAGE; Q13E55.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00730407};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00730390};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00730432};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00730340};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00730332}.
FT   REGION       13     18       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION      160    163       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION      195    196       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   ACT_SITE     74     74       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   METAL        45     45       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   METAL        74     74       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING      75     75       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01405}.
FT   BINDING     183    183       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
SQ   SEQUENCE   210 AA;  22291 MW;  777BBF91CA80EB97 CRC64;
     MHRRISGKLV IATHNPGKLA EMRELLAPYG IEAVSAGELG LGEPDETGDS FRANARIKAE
     AAAQAAKLPA FADDSGLSVD ALDGAPGIFS ARWAGEGKDF NAAMAQIERL LRERGATAPA
     QRGAHFVSAL CVAWPDGHIE EVEARADGTL VWPPRGDAGF GYDPMFLPDG HDRTFGEMSS
     IEKHGLPPLG LGLSHRARAF VKLAEICLGR
//

If you have problems or comments...

PBIL Back to PBIL home page