PSUK_ECOLI
ID PSUK_ECOLI Reviewed; 313 AA.
AC P30235; Q2MAR3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Pseudouridine kinase;
DE EC=2.7.1.83;
GN Name=psuK; Synonyms=pscK, yeiC; OrderedLocusNames=b2166, JW2153;
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 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-122.
RC STRAIN=K12;
RX PubMed=3076173; DOI=10.1099/00221287-134-10-2757;
RA Prior T.I., Kornberg H.L.;
RT "Nucleotide sequence of fruA, the gene specifying enzyme IIfru of the
RT phosphoenolpyruvate-dependent sugar phosphotransferase system in
RT Escherichia coli K12.";
RL J. Gen. Microbiol. 134:2757-2768(1988).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12;
RX PubMed=18591240; DOI=10.1074/jbc.m804122200;
RA Preumont A., Snoussi K., Stroobant V., Collet J.-F., Van Schaftingen E.;
RT "Molecular identification of pseudouridine-metabolizing enzymes.";
RL J. Biol. Chem. 283:25238-25246(2008).
CC -!- FUNCTION: Catalyzes the phosphorylation of pseudouridine to
CC pseudouridine 5'-phosphate (PsiMP). {ECO:0000269|PubMed:18591240}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pseudouridine = ADP + H(+) + psi-UMP;
CC Xref=Rhea:RHEA:22448, ChEBI:CHEBI:15378, ChEBI:CHEBI:17802,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58380, ChEBI:CHEBI:456216;
CC EC=2.7.1.83; Evidence={ECO:0000269|PubMed:18591240};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for pseudouridine (in the presence of 0.5 mM ATP)
CC {ECO:0000269|PubMed:18591240};
CC KM=330 uM for ATP (in the presence of 200 uM pseudouridine)
CC {ECO:0000269|PubMed:18591240};
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; U00007; AAA60507.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75227.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76643.1; -; Genomic_DNA.
DR EMBL; M23196; AAA62625.1; -; Genomic_DNA.
DR PIR; E64985; E64985.
DR RefSeq; NP_416671.1; NC_000913.3.
DR RefSeq; WP_001208118.1; NZ_SSZK01000027.1.
DR AlphaFoldDB; P30235; -.
DR SMR; P30235; -.
DR BioGRID; 4260461; 17.
DR BioGRID; 851006; 1.
DR IntAct; P30235; 11.
DR STRING; 511145.b2166; -.
DR PaxDb; P30235; -.
DR PRIDE; P30235; -.
DR EnsemblBacteria; AAC75227; AAC75227; b2166.
DR EnsemblBacteria; BAE76643; BAE76643; BAE76643.
DR GeneID; 946664; -.
DR KEGG; ecj:JW2153; -.
DR KEGG; eco:b2166; -.
DR PATRIC; fig|511145.12.peg.2251; -.
DR EchoBASE; EB1599; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_11_2_6; -.
DR InParanoid; P30235; -.
DR OMA; GHIMNLM; -.
DR PhylomeDB; P30235; -.
DR BioCyc; EcoCyc:EG11646-MON; -.
DR BRENDA; 2.7.1.83; 2026.
DR PRO; PR:P30235; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050225; F:pseudouridine kinase activity; IDA:EcoliWiki.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..313
FT /note="Pseudouridine kinase"
FT /id="PRO_0000080147"
SQ SEQUENCE 313 AA; 33573 MW; 89D0F8439D148103 CRC64;
MREKDYVVII GSANIDVAGY SHESLNYADS NPGKIKFTPG GVGRNIAQNL ALLGNKAWLL
SAVGSDFYGQ SLLTQTNQSG VYVDKCLIVP GENTSSYLSL LDNTGEMLVA INDMNISNAI
TAEYLAQHGE FIQRAKVIVA DCNISEEALA WILDNAANVP VFVDPVSAWK CVKVRDRLNQ
IHTLKPNRLE AETLSGIALS GREDVAKVAA WFHQHGLNRL VLSMGGDGVY YSDISGESGW
SAPIKTNVIN VTGAGDAMMA GLASCWVDGM PFAESVRFAQ GCSSMALSCE YTNNPDLSIA
NVISLVENAE CLN
