3PASE_ACET2
ID 3PASE_ACET2 Reviewed; 156 AA.
AC A3DIJ8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Inorganic triphosphatase;
DE Short=PPPase;
DE EC=3.6.1.25;
DE AltName: Full=Adenosinetriphosphatase;
DE Short=ATPase;
DE AltName: Full=Polyphosphatase;
GN OrderedLocusNames=Cthe_2577;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
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., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-4; GLU-6; ARG-39; ARG-41;
RP LYS-52; GLU-62; GLU-64; LYS-87; ARG-89; ASP-102; GLU-115 AND GLU-117,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=17303560; DOI=10.1074/jbc.m611328200;
RA Keppetipola N., Jain R., Shuman S.;
RT "Novel triphosphate phosphohydrolase activity of Clostridium thermocellum
RT TTM, a member of the triphosphate tunnel metalloenzyme superfamily.";
RL J. Biol. Chem. 282:11941-11949(2007).
CC -!- FUNCTION: Involved in the hydrolysis of the beta-gamma-phosphoanhydride
CC linkage of triphosphate-containing substrates (inorganic or nucleoside-
CC linked). Catalyzes vigorously the hydrolysis of inorganic triphosphate
CC (PPPi), however it can also catalyze the hydrolysis of ATP to ADP and
CC phosphate. It can use ribonucleotides such as GTP, CTP, or UTP and
CC deoxynucleotides such as dATP, dGTP, dCTP, and dTTP.
CC {ECO:0000269|PubMed:17303560}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + triphosphate = diphosphate + phosphate;
CC Xref=Rhea:RHEA:14157, ChEBI:CHEBI:15377, ChEBI:CHEBI:18036,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.25;
CC Evidence={ECO:0000269|PubMed:17303560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:17303560};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26 uM for ATP {ECO:0000269|PubMed:17303560};
CC Note=kcat is 25 min(-1) for ATPase activity.;
CC pH dependence:
CC Optimum pH is between 8 and 8.5 for ATPase activity and between 9 and
CC 9.5 for PPPase activity. Hydrolysis of ATP declines sharply as the pH
CC is increased to 9.5 or decreased to below 7.0.
CC {ECO:0000269|PubMed:17303560};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17303560}.
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DR EMBL; CP000568; ABN53777.1; -; Genomic_DNA.
DR RefSeq; WP_020457870.1; NC_009012.1.
DR AlphaFoldDB; A3DIJ8; -.
DR SMR; A3DIJ8; -.
DR STRING; 203119.Cthe_2577; -.
DR EnsemblBacteria; ABN53777; ABN53777; Cthe_2577.
DR KEGG; cth:Cthe_2577; -.
DR eggNOG; COG2954; Bacteria.
DR HOGENOM; CLU_109545_1_0_9; -.
DR OMA; WEVDEFF; -.
DR OrthoDB; 1469073at2; -.
DR SABIO-RK; A3DIJ8; -.
DR Proteomes; UP000002145; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0050355; F:triphosphatase activity; IDA:UniProtKB.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR023577; CYTH_domain.
DR InterPro; IPR012042; NeuTTM/CthTTM-like.
DR PANTHER; PTHR40114; PTHR40114; 1.
DR Pfam; PF01928; CYTH; 1.
DR PIRSF; PIRSF016487; CYTH_UCP016487; 1.
DR SMART; SM01118; CYTH; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
DR PROSITE; PS51707; CYTH; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..156
FT /note="Inorganic triphosphatase"
FT /id="PRO_0000426736"
FT DOMAIN 2..148
FT /note="CYTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01044"
FT ACT_SITE 29
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT MUTAGEN 4
FT /note="E->A: Partial loss of ATPase activity and strong
FT loss of inorganic triphosphatase activity."
FT /evidence="ECO:0000269|PubMed:17303560"
FT MUTAGEN 6
FT /note="E->A: Strong loss of ATPase and inorganic
FT triphosphatase activities."
FT /evidence="ECO:0000269|PubMed:17303560"
FT MUTAGEN 8
FT /note="K->A: 16-fold increase in ATPase activity and strong
FT loss of inorganic triphosphatase activity."
FT MUTAGEN 39
FT /note="R->A: Strong loss of ATPase and inorganic
FT triphosphatase activities."
FT /evidence="ECO:0000269|PubMed:17303560"
FT MUTAGEN 41
FT /note="R->A: Strong loss of ATPase and inorganic
FT triphosphatase activities."
FT /evidence="ECO:0000269|PubMed:17303560"
FT MUTAGEN 52
FT /note="K->A: Strong loss of ATPase activity and partial
FT loss of inorganic triphosphatase activity."
FT /evidence="ECO:0000269|PubMed:17303560"
FT MUTAGEN 62
FT /note="E->A: Strong loss of ATPase and inorganic
FT triphosphatase activities."
FT /evidence="ECO:0000269|PubMed:17303560"
FT MUTAGEN 64
FT /note="E->A: Partial loss of ATPase activity and strong
FT loss of inorganic triphosphatase activity."
FT /evidence="ECO:0000269|PubMed:17303560"
FT MUTAGEN 87
FT /note="K->A: Strong loss of ATPase and inorganic
FT triphosphatase activities."
FT /evidence="ECO:0000269|PubMed:17303560"
FT MUTAGEN 89
FT /note="R->A: Strong loss of ATPase and inorganic
FT triphosphatase activities."
FT /evidence="ECO:0000269|PubMed:17303560"
FT MUTAGEN 100
FT /note="E->A: Partial loss of ATPase and inorganic
FT triphosphatase activities. However, the inorganic
FT triphosphatase activity is restored when manganese replaces
FT magnesium."
FT MUTAGEN 102
FT /note="D->A: Strong loss of ATPase and inorganic
FT triphosphatase activities. However, the inorganic
FT triphosphatase activity is restored when manganese replaces
FT magnesium."
FT /evidence="ECO:0000269|PubMed:17303560"
FT MUTAGEN 115
FT /note="E->A: Partial loss of ATPase activity and inorganic
FT triphosphatase activities."
FT /evidence="ECO:0000269|PubMed:17303560"
FT MUTAGEN 117
FT /note="E->A: Strong loss of ATPase activity and inorganic
FT triphosphatase activities."
FT /evidence="ECO:0000269|PubMed:17303560"
SQ SEQUENCE 156 AA; 18159 MW; EBAF96A15143A8F0 CRC64;
MGKEIEKKFI VSGDAYKSLA KGVLYRQGYI FFDKDKSVRV RVFNDKGYLT VKGTSTGISR
LEYEYEIPVG EANEILEYLC EKPVIEKLRY KFQFEGFTWE VDEFLGENEG LVIAEIELPD
ENAVFKKPDW IGREVTGDPR YLNSNLVKNP YKNFKE
