Sequence of SUHB_ECOLI
EC Number:3.1.3.25
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
myo-inositol phosphate + H2O = myo-inositol + phosphate
Other sequences found for EC No. 3.1.3.25
General information:
Sequence
0 MHPMLNIAVR AARKAGNLIA KNYETPDAVE ASQKGSNDFV TNVDKAAEAV IIDTIRKSYP
60 QHTIITEESG ELEGTDQDVQ WVIDPLDGTT NFIKRLPHFA VSIAVRIKGR TEVAVVYDPM
120 RNELFTATRG QGAQLNGYRL RGSTARDLDG TILATGFPFK AKQYATTYIN IVGKLFNECA
180 DFRRTGSAAL DLAYVAAGRV DGFFEIGLRP WDFAAGELLV REAGGIVSDF TGGHNYMLTG
240 NIVAGNPRVV KAMLANMRDE LSDALKR
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
236220
Yano R.,Nagai H.,Shiba K.,Yura T.
A mutation that enhances synthesis of sigma 32 and suppresses temperature-sensitive growth of the rpoH15 mutant of Escherichia coli.
J. Bacteriol.
172
2124-2130
1990
236221
Yamamoto Y.,Aiba H.,Baba T.,Hayashi K.,Inada T.,Isono K.,Itoh T.,Kimura S.,Kitagawa M.,Makino K.,Miki T.,Mitsuhashi N.,Mizobuchi K.,Mori H.,Nakade S.,Nakamura Y.,Nashimoto H.,Oshima T.,Oyama S.,Saito N.,Sampei G.,Satoh Y.,Sivasundaram S.,Tagami H.,Takahashi H.,Takeda J.,Takemoto K.,Uehara K.,Wada C.,Yamagata S.,Horiuchi T.
Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features.
DNA Res.
4
91-113
1997
236222
Blattner F.R.,Plunkett G. III,Bloch C.A.,Perna N.T.,Burland V.,Riley M.,Collado-Vides J.,Glasner J.D.,Rode C.K.,Mayhew G.F.,Gregor J.,Davis N.W.,Kirkpatrick H.A.,Goeden M.A.,Rose D.J.,Mau B.,Shao Y.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
236223
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
236224
Shiba K.,Ito K.,Yura T.
Mutation that suppresses the protein export defect of the secY mutation and causes cold-sensitive growth of Escherichia coli.
J. Bacteriol.
160
696-701
1984
236225
Kozloff L.M.,Turner M.A.,Arellano F.,Lute M.
Phosphatidylinositol, a phospholipid of ice-nucleating bacteria.
J. Bacteriol.
173
2053-2060
1991
236226
Chang S.F.,Ng D.,Baird L.,Georgopoulos C.
Analysis of an Escherichia coli dnaB temperature-sensitive insertion mutation and its cold-sensitive extragenic suppressor.
J. Biol. Chem.
266
3654-3660
1991
236227
Matsuhisa A.,Suzuki N.,Noda T.,Shiba K.
Inositol monophosphatase activity from the Escherichia coli suhB gene product.
J. Bacteriol.
177
200-205
1995
236228
Inada T.,Nakamura Y.
Lethal double-stranded RNA processing activity of ribonuclease III in the absence of suhB protein of Escherichia coli.
Biochimie
77
294-302
1995
236229
Inada T.,Nakamura Y.
Autogenous control of the suhB gene expression of Escherichia coli.
Biochimie
78
209-212
1996
236230
Chen L.,Roberts M.F.
Overexpression, purification, and analysis of complementation behavior of E. coli SuhB protein: comparison with bacterial and archaeal inositol monophosphatases.
Biochemistry
39
4145-4153
2000
236231
Haimovich A.,Eliav U.,Goldbourt A.
Determination of the lithium binding site in inositol monophosphatase, the putative target for lithium therapy, by magic-angle-spinning solid-state NMR.
J. Am. Chem. Soc.
134
5647-5651
2012
236232
Singh N.,Bubunenko M.,Smith C.,Abbott D.M.,Stringer A.M.,Shi R.,Court D.L.,Wade J.T.
SuhB Associates with Nus Factors To Facilitate 30S Ribosome Biogenesis in Escherichia coli.
MBio
7
0-0
2016
236233
Baniulyte G.,Singh N.,Benoit C.,Johnson R.,Ferguson R.,Paramo M.,Stringer A.M.,Scott A.,Lapierre P.,Wade J.T.
Identification of regulatory targets for the bacterial Nus factor complex.
Nat. Commun.
8
2027-2027
2017
236234
Dudenhoeffer B.R.,Schneider H.,Schweimer K.,Knauer S.H.
SuhB is an integral part of the ribosomal antitermination complex and interacts with NusA.
Nucleic Acids Res.
47
6504-6518
2019
236235
Wang Y.,Stieglitz K.A.,Bubunenko M.,Court D.L.,Stec B.,Roberts M.F.
The structure of the R184A mutant of the inositol monophosphatase encoded by suhB and implications for its functional interactions in Escherichia coli.
J. Biol. Chem.
282
26989-26996
2007
236236
Huang Y.H.,Said N.,Loll B.,Wahl M.C.
Structural basis for the function of SuhB as a transcription factor in ribosomal RNA synthesis.
Nucleic Acids Res.
47
6488-6503
2019
236237
Huang Y.H.,Hilal T.,Loll B.,Buerger J.,Mielke T.,Boettcher C.,Said N.,Wahl M.C.
Structure-Based Mechanisms of a Molecular RNA Polymerase/Chaperone Machine Required for Ribosome Biosynthesis.
Mol. Cell
0
0-0
2020
