NTPTH_AQUAE
ID NTPTH_AQUAE Reviewed; 178 AA.
AC O67322;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=aq_1292;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14503925; DOI=10.1186/1471-2091-4-12;
RA Klinger C., Rossbach M., Howe R., Kaufmann M.;
RT "Thermophile-specific proteins: the gene product of aq_1292 from Aquifex
RT aeolicus is an NTPase.";
RL BMC Biochem. 4:12-12(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH PHOSPHATE.
RX PubMed=15777481; DOI=10.1186/1472-6807-5-7;
RA Rossbach M., Daumke O., Klinger C., Wittinghofer A., Kaufmann M.;
RT "Crystal structure of THEP1 from the hyperthermophile Aquifex aeolicus: a
RT variation of the RecA fold.";
RL BMC Struct. Biol. 5:7-7(2005).
CC -!- FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP,
CC TTP and UTP. May hydrolyze nucleoside diphosphates with lower
CC efficiency. Does not have kinase activity. {ECO:0000255|HAMAP-
CC Rule:MF_00796, ECO:0000269|PubMed:14503925}.
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 ECO:0000269|PubMed:14503925};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.5 uM for ATP {ECO:0000269|PubMed:14503925};
CC KM=45 uM for GTP {ECO:0000269|PubMed:14503925};
CC Temperature dependence:
CC Optimum temperature is 70-80 degrees Celsius.
CC {ECO:0000269|PubMed:14503925};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14503925,
CC ECO:0000269|PubMed:15777481}.
CC -!- SIMILARITY: Belongs to the THEP1 NTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00796}.
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DR EMBL; AE000657; AAC07294.1; -; Genomic_DNA.
DR PIR; G70411; G70411.
DR RefSeq; NP_213886.1; NC_000918.1.
DR RefSeq; WP_010880824.1; NC_000918.1.
DR PDB; 1YE8; X-ray; 1.40 A; A=1-178.
DR PDBsum; 1YE8; -.
DR AlphaFoldDB; O67322; -.
DR SMR; O67322; -.
DR STRING; 224324.aq_1292; -.
DR EnsemblBacteria; AAC07294; AAC07294; aq_1292.
DR KEGG; aae:aq_1292; -.
DR PATRIC; fig|224324.8.peg.1010; -.
DR eggNOG; COG1618; Bacteria.
DR HOGENOM; CLU_103145_1_0_0; -.
DR InParanoid; O67322; -.
DR OMA; GAMEFKC; -.
DR OrthoDB; 1935037at2; -.
DR BioCyc; MetaCyc:MON-17884; -.
DR EvolutionaryTrace; O67322; -.
DR Proteomes; UP000000798; Chromosome.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR004948; Nuc-triphosphatase_THEP1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43146; PTHR43146; 1.
DR Pfam; PF03266; NTPase_1; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..178
FT /note="Nucleoside-triphosphatase THEP1"
FT /id="PRO_0000146709"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1YE8"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:1YE8"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1YE8"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:1YE8"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1YE8"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1YE8"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1YE8"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1YE8"
FT HELIX 77..97
FT /evidence="ECO:0007829|PDB:1YE8"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:1YE8"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1YE8"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:1YE8"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:1YE8"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:1YE8"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1YE8"
FT TURN 162..167
FT /evidence="ECO:0007829|PDB:1YE8"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:1YE8"
SQ SEQUENCE 178 AA; 20555 MW; 13AE2F602F08150C CRC64;
MKIIITGEPG VGKTTLVKKI VERLGKRAIG FWTEEVRDPE TKKRTGFRII TTEGKKKIFS
SKFFTSKKLV GSYGVNVQYF EELAIPILER AYREAKKDRR KVIIIDEIGK MELFSKKFRD
LVRQIMHDPN VNVVATIPIR DVHPLVKEIR RLPGAVLIEL TPENRDVILE DILSLLER
