ID B8D4V7_DESA1 Unreviewed; 182 AA.
AC B8D4V7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Nucleoside-triphosphatase DKAM_0812 {ECO:0000256|HAMAP-Rule:MF_00796};
DE Short=NTPase {ECO:0000256|HAMAP-Rule:MF_00796};
DE EC=3.6.1.15 {ECO:0000256|HAMAP-Rule:MF_00796};
DE AltName: Full=Nucleoside triphosphate phosphohydrolase {ECO:0000256|HAMAP-Rule:MF_00796};
GN OrderedLocusNames=DKAM_0812 {ECO:0000313|EMBL:ACL11138.1};
OS Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 /
OS 1221n) (Desulfurococcus kamchatkensis).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Desulfurococcus.
OX NCBI_TaxID=490899 {ECO:0000313|EMBL:ACL11138.1, ECO:0000313|Proteomes:UP000006903};
RN [1] {ECO:0000313|EMBL:ACL11138.1, ECO:0000313|Proteomes:UP000006903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n
RC {ECO:0000313|Proteomes:UP000006903};
RX PubMed=19114480; DOI=10.1128/JB.01525-08;
RA Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V.,
RA Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Complete genome sequence of the anaerobic, protein-degrading
RT hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.";
RL J. Bacteriol. 191:2371-2379(2009).
CC -!- FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP,
CC TTP and UTP. May hydrolyze nucleoside diphosphates with lower
CC efficiency. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00796};
CC -!- SIMILARITY: Belongs to the THEP1 NTPase family. {ECO:0000256|HAMAP-
CC Rule:MF_00796}.
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DR EMBL; CP001140; ACL11138.1; -; Genomic_DNA.
DR RefSeq; WP_012608479.1; NC_011766.1.
DR AlphaFoldDB; B8D4V7; -.
DR STRING; 490899.DKAM_0812; -.
DR GeneID; 7170964; -.
DR KEGG; dka:DKAM_0812; -.
DR eggNOG; arCOG01034; Archaea.
DR HOGENOM; CLU_103145_1_1_2; -.
DR Proteomes; UP000006903; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd19482; RecA-like_Thep1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00796; NTPase_1; 1.
DR InterPro; IPR004948; Nuc-triphosphatase_THEP1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43146; CANCER-RELATED NUCLEOSIDE-TRIPHOSPHATASE; 1.
DR PANTHER; PTHR43146:SF1; CANCER-RELATED NUCLEOSIDE-TRIPHOSPHATASE; 1.
DR Pfam; PF03266; NTPase_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00796}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00796};
KW Kinase {ECO:0000313|EMBL:ACL11138.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00796}; Transferase {ECO:0000313|EMBL:ACL11138.1}.
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00796"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00796"
SQ SEQUENCE 182 AA; 19957 MW; 69529CE659682483 CRC64;
MKIIITGRPG VGKSTFFEKL ISELRENNLL VGGIKAPEVR EHGVRVGFKV IDLLSGEKAW
LAKKSIPGSV RIGSYTVLVE EASRIIETAL RRALGEASVI GIDEVGPMEL KIPVFKPLLL
EILDSGKPVI LVVHYRLTDR DVLGRLSDAE KIVLTMENRE HVKSSTKGLI NKVIEALAPS
RS
//
