NTPTH_METBF
ID NTPTH_METBF Reviewed; 174 AA.
AC Q467J7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Nucleoside-triphosphatase THEP1 {ECO:0000255|HAMAP-Rule:MF_00796};
DE Short=NTPase THEP1 {ECO:0000255|HAMAP-Rule:MF_00796};
DE EC=3.6.1.15 {ECO:0000255|HAMAP-Rule:MF_00796};
DE AltName: Full=Nucleoside triphosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00796};
GN OrderedLocusNames=Mbar_A3054;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
CC -!- FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP,
CC TTP and UTP. May hydrolyze nucleoside diphosphates with lower
CC efficiency. {ECO:0000255|HAMAP-Rule:MF_00796}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00796};
CC -!- SIMILARITY: Belongs to the THEP1 NTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00796}.
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DR EMBL; CP000099; AAZ71945.1; -; Genomic_DNA.
DR RefSeq; WP_011307985.1; NC_007355.1.
DR AlphaFoldDB; Q467J7; -.
DR SMR; Q467J7; -.
DR STRING; 269797.Mbar_A3054; -.
DR EnsemblBacteria; AAZ71945; AAZ71945; Mbar_A3054.
DR GeneID; 3625065; -.
DR KEGG; mba:Mbar_A3054; -.
DR eggNOG; arCOG01034; Archaea.
DR HOGENOM; CLU_103145_1_1_2; -.
DR OMA; GAMEFKC; -.
DR OrthoDB; 90019at2157; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00796; NTPase_1; 1.
DR InterPro; IPR004948; Nuc-triphosphatase_THEP1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43146; PTHR43146; 1.
DR Pfam; PF03266; NTPase_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Nucleotide-binding.
FT CHAIN 1..174
FT /note="Nucleoside-triphosphatase THEP1"
FT /id="PRO_1000046953"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
SQ SEQUENCE 174 AA; 18995 MW; EF35886284D6AE7E CRC64;
MLRIAVTGIP GIGKSTVVAK AAEKLADQPG FKIGGIQTAE IRKEGQREGF SIMDLATGKT
GVLGSIRESG PRVGKYHVNL EDLEKIGANA LRSAMDCDLI VIDEVGTMEL KSEAFVSAVK
VVLESDKPVL AVLHRSSSHQ LVQRMRREFE VLVVNEKNRD GLPGKIANRF REMR
