UTPP_ECOLI
ID UTPP_ECOLI Reviewed; 167 AA.
AC P42597; Q2M9C1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=UTP pyrophosphatase {ECO:0000303|PubMed:27941785};
DE EC=3.6.1.- {ECO:0000269|PubMed:27941785};
GN Name=ygjP {ECO:0000312|EMBL:AAC76120.2};
GN Synonyms=upp {ECO:0000303|PubMed:27941785};
GN OrderedLocusNames=b3085, JW5514;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=27941785; DOI=10.1038/nmeth.4103;
RA Sevin D.C., Fuhrer T., Zamboni N., Sauer U.;
RT "Nontargeted in vitro metabolomics for high-throughput identification of
RT novel enzymes in Escherichia coli.";
RL Nat. Methods 14:187-194(2017).
CC -!- FUNCTION: Specifically catalyzes the hydrolysis of UTP to UMP and
CC diphosphate in vitro, albeit at apparently slow rate. Shows no activity
CC towards ATP, GTP, CTP, dTTP and ITP as substrates.
CC {ECO:0000269|PubMed:27941785}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UTP = diphosphate + H(+) + UMP; Xref=Rhea:RHEA:29395,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:57865;
CC Evidence={ECO:0000269|PubMed:27941785};
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57886.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA57886.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76120.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77135.1; -; Genomic_DNA.
DR PIR; B65097; B65097.
DR RefSeq; NP_417556.2; NC_000913.3.
DR RefSeq; WP_001333820.1; NZ_LN832404.1.
DR AlphaFoldDB; P42597; -.
DR BioGRID; 4260874; 23.
DR STRING; 511145.b3085; -.
DR PaxDb; P42597; -.
DR PRIDE; P42597; -.
DR EnsemblBacteria; AAC76120; AAC76120; b3085.
DR EnsemblBacteria; BAE77135; BAE77135; BAE77135.
DR GeneID; 947650; -.
DR KEGG; ecj:JW5514; -.
DR KEGG; eco:b3085; -.
DR PATRIC; fig|511145.12.peg.3180; -.
DR EchoBASE; EB2586; -.
DR eggNOG; COG1451; Bacteria.
DR HOGENOM; CLU_101303_0_0_6; -.
DR InParanoid; P42597; -.
DR OMA; LCCYMEP; -.
DR PhylomeDB; P42597; -.
DR BioCyc; EcoCyc:G7604-MON; -.
DR PRO; PR:P42597; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0036221; F:UTP diphosphatase activity; IEA:RHEA.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR002725; YgjP-like_metallopeptidase.
DR Pfam; PF01863; DUF45; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Nucleotide metabolism; Nucleotide-binding; Reference proteome.
FT CHAIN 1..167
FT /note="UTP pyrophosphatase"
FT /id="PRO_0000169424"
SQ SEQUENCE 167 AA; 19483 MW; 4E9BB4FE99F385EB CRC64;
MSNLTYLQGY PEQLLSQVRT LINEQRLGDV LAKRYPGTHD YATDKALWQY TQDLKNQFLR
NAPPINKVMY DNKIHVLKNA LGLHTAVSRV QGGKLKAKVE IRVATVFRNA PEPFLRMIVV
HELAHLKEKE HNKAFYQLCC HMEPQYHQLE FDTRLWLTQL SLGQNKI