ID   3PASE_HAEIN             Reviewed;         352 AA.
AC   P45267;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Inorganic triphosphatase;
DE            Short=PPPase;
DE            EC=3.6.1.25;
GN   OrderedLocusNames=HI_1598;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Involved in the hydrolysis of the beta-gamma-phosphoanhydride
CC       linkage of triphosphate-containing substrates (inorganic or nucleoside-
CC       linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi),
CC       which could be cytotoxic because of its high affinity for calcium ion,
CC       thereby interfering with calcium signaling (By similarity).
CC       {ECO:0000250}.
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;
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DR   EMBL; L42023; AAC23243.1; -; Genomic_DNA.
DR   PIR; H64172; H64172.
DR   RefSeq; NP_439740.1; NC_000907.1.
DR   AlphaFoldDB; P45267; -.
DR   SMR; P45267; -.
DR   STRING; 71421.HI_1598; -.
DR   DNASU; 950454; -.
DR   EnsemblBacteria; AAC23243; AAC23243; HI_1598.
DR   KEGG; hin:HI_1598; -.
DR   PATRIC; fig|71421.8.peg.1671; -.
DR   eggNOG; COG3025; Bacteria.
DR   HOGENOM; CLU_040400_0_0_6; -.
DR   OMA; ERDIYFS; -.
DR   PhylomeDB; P45267; -.
DR   BioCyc; HINF71421:G1GJ1-1611-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0050355; F:triphosphatase activity; ISS:UniProtKB.
DR   InterPro; IPR033469; CYTH-like_dom_sf.
DR   InterPro; IPR023577; CYTH_domain.
DR   InterPro; IPR039013; YgiF.
DR   PANTHER; PTHR39569; PTHR39569; 2.
DR   Pfam; PF01928; CYTH; 1.
DR   SMART; SM01118; CYTH; 1.
DR   SUPFAM; SSF55154; SSF55154; 1.
DR   PROSITE; PS51707; CYTH; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..352
FT                   /note="Inorganic triphosphatase"
FT                   /id="PRO_0000169407"
FT   DOMAIN          6..203
FT                   /note="CYTH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01044"
SQ   SEQUENCE   352 AA;  41315 MW;  E23487A3B0702316 CRC64;
     MENIMLQEIE LKLAISPQIG IELPQYLAKF TILEHQNLFL GNTYYDYPDH FLAKQKMGLR
     IRQEDQELTL TLKTNGKVVS GLHSRPEYNL PLIEKETPTN AQLRGLYPFE QLPSSTLQPI
     FSTDFNRTFW LVEFQQSKIE VAFDQGKIIA GEYEQPISEI EFELKSGNVQ DLFDFVETLP
     FERDIYFSSA SKAKRGYLLG SKQFLTDWLN KWRDFLKEER EESAVDFCAK FNAVLKMEQK
     LLEETLSFSP TLFSQDFMKT VERVGAFFNL YHYYDENGKI LEAMATEKQK ETRLPALLES
     NQKIFVEIRD LIRFHSETKD NEKTIEKLTA LLKSRVYFER MIKLMELSYD LG