3PASE_ECOLI
ID 3PASE_ECOLI Reviewed; 433 AA.
AC P30871; Q2M9F1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Inorganic triphosphatase;
DE Short=PPPase;
DE EC=3.6.1.25;
DE AltName: Full=ORFXE;
GN Name=ygiF; OrderedLocusNames=b3054, JW3026;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / CS520;
RX PubMed=8412694; DOI=10.1111/j.1365-2958.1993.tb01706.x;
RA van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.;
RT "The genes of the glutamine synthetase adenylylation cascade are not
RT regulated by nitrogen in Escherichia coli.";
RL Mol. Microbiol. 9:443-458(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, ACTIVITY REGULATION, AND SUBSTRATE SPECIFICITY.
RX PubMed=22984449; DOI=10.1371/journal.pone.0043879;
RA Kohn G., Delvaux D., Lakaye B., Servais A.C., Scholer G., Fillet M.,
RA Elias B., Derochette J.M., Crommen J., Wins P., Bettendorff L.;
RT "High inorganic triphosphatase activities in bacteria and mammalian cells:
RT identification of the enzymes involved.";
RL PLoS ONE 7:E43879-E43879(2012).
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. It also hydrolyzes slowly
CC thiamine triphosphate (ThTP). YgiF is a specific PPPase, but it
CC contributes only marginally to the total PPPase activity in E.coli,
CC where the main enzyme responsible for hydrolysis of PPPi is inorganic
CC pyrophosphatase (PPase). {ECO:0000269|PubMed:22984449}.
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:22984449};
CC -!- ACTIVITY REGULATION: Inhibited by calcium ion and activated by
CC magnesium ion. {ECO:0000269|PubMed:22984449}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=270 uM for inorganic triphosphate {ECO:0000269|PubMed:22984449};
CC Vmax=27 umol/min/mg enzyme {ECO:0000269|PubMed:22984449};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:22984449};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not show decrease of
CC specific PPPase activity. {ECO:0000269|PubMed:22984449}.
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DR EMBL; Z21844; CAA79891.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76090.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77105.1; -; Genomic_DNA.
DR PIR; S37754; S37754.
DR RefSeq; NP_417526.1; NC_000913.3.
DR RefSeq; WP_000046281.1; NZ_LN832404.1.
DR PDB; 5A60; X-ray; 1.82 A; A=1-433.
DR PDB; 5A61; X-ray; 1.50 A; A=1-433.
DR PDBsum; 5A60; -.
DR PDBsum; 5A61; -.
DR AlphaFoldDB; P30871; -.
DR SMR; P30871; -.
DR BioGRID; 4259253; 8.
DR DIP; DIP-12218N; -.
DR IntAct; P30871; 24.
DR STRING; 511145.b3054; -.
DR jPOST; P30871; -.
DR PaxDb; P30871; -.
DR PRIDE; P30871; -.
DR EnsemblBacteria; AAC76090; AAC76090; b3054.
DR EnsemblBacteria; BAE77105; BAE77105; BAE77105.
DR GeneID; 947554; -.
DR KEGG; ecj:JW3026; -.
DR KEGG; eco:b3054; -.
DR PATRIC; fig|1411691.4.peg.3677; -.
DR EchoBASE; EB1560; -.
DR eggNOG; COG3025; Bacteria.
DR HOGENOM; CLU_040400_0_1_6; -.
DR InParanoid; P30871; -.
DR OMA; MPCDISK; -.
DR PhylomeDB; P30871; -.
DR BioCyc; EcoCyc:EG11603-MON; -.
DR BioCyc; MetaCyc:EG11603-MON; -.
DR PRO; PR:P30871; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0050355; F:triphosphatase activity; IDA:EcoCyc.
DR InterPro; IPR007899; CHAD_dom.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR023577; CYTH_domain.
DR InterPro; IPR039013; YgiF.
DR PANTHER; PTHR39569; PTHR39569; 1.
DR Pfam; PF01928; CYTH; 1.
DR SMART; SM01118; CYTH; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
DR PROSITE; PS51708; CHAD; 1.
DR PROSITE; PS51707; CYTH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..433
FT /note="Inorganic triphosphatase"
FT /id="PRO_0000169406"
FT DOMAIN 2..202
FT /note="CYTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01044"
FT DOMAIN 218..433
FT /note="CHAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01045"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:5A61"
FT STRAND 29..42
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:5A61"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:5A61"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:5A61"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5A61"
FT STRAND 78..92
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5A61"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:5A61"
FT STRAND 117..133
FT /evidence="ECO:0007829|PDB:5A61"
FT STRAND 136..149
FT /evidence="ECO:0007829|PDB:5A61"
FT STRAND 152..166
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:5A61"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 221..244
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 250..267
FT /evidence="ECO:0007829|PDB:5A61"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 278..293
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 297..302
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 304..318
FT /evidence="ECO:0007829|PDB:5A61"
FT TURN 319..322
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 328..334
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 338..357
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 369..382
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 388..407
FT /evidence="ECO:0007829|PDB:5A61"
FT HELIX 410..422
FT /evidence="ECO:0007829|PDB:5A61"
SQ SEQUENCE 433 AA; 48389 MW; F2CB1519123C0277 CRC64;
MAQEIELKFI VNHSAVEALR DHLNTLGGEH HDPVQLLNIY YETPDNWLRG HDMGLRIRGE
NGRYEMTMKV AGRVTGGLHQ RPEYNVALSE PTLDLAQLPT EVWPNGELPA DLASRVQPLF
STDFYREKWL VAVDGSQIEI ALDQGEVKAG EFAEPICELE LELLSGDTRA VLKLANQLVS
QTGLRQGSLS KAARGYHLAQ GNPAREIKPT TILHVAAKAD VEQGLEAALE LALAQWQYHE
ELWVRGNDAA KEQVLAAISL VRHTLMLFGG IVPRKASTHL RDLLTQCEAT IASAVSAVTA
VYSTETAMAK LALTEWLVSK AWQPFLDAKA QGKISDSFKR FADIHLSRHA AELKSVFCQP
LGDRYRDQLP RLTRDIDSIL LLAGYYDPVV AQAWLENWQG LHHAIATGQR IEIEHFRNEA
NNQEPFWLHS GKR
