Sequence of HCHA_ECOLI
EC Number:3.5.1.124
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O = a [protein]-L-lysine + lactate
Other sequences found for EC No. 3.5.1.124
EC Number:4.2.1.130
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(R)-lactate = 2-oxopropanal + H2O
Other sequences found for EC No. 4.2.1.130
General information:
Sequence
0 MTVQTSKNPQ VDIAEDNAFF PSEYSLSQYT SPVSDLDGVD YPKPYRGKHK ILVIAADERY
60 LPTDNGKLFS TGNHPIETLL PLYHLHAAGF EFEVATISGL MTKFEYWAMP HKDEKVMPFF
120 EQHKSLFRNP KKLADVVASL NADSEYAAIF VPGGHGALIG LPESQDVAAA LQWAIKNDRF
180 VISLCHGPAA FLALRHGDNP LNGYSICAFP DAADKQTPEI GYMPGHLTWY FGEELKKMGM
240 NIINDDITGR VHKDRKLLTG DSPFAANALG KLAAQEMLAA YAG
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
426519
Itoh T.,Aiba H.,Baba T.,Fujita K.,Hayashi K.,Inada T.,Isono K.,Kasai H.,Kimura S.,Kitakawa M.,Kitagawa M.,Makino K.,Miki T.,Mizobuchi K.,Mori H.,Mori T.,Motomura K.,Nakade S.,Nakamura Y.,Nashimoto H.,Nishio Y.,Oshima T.,Saito N.,Sampei G.,Seki Y.,Sivasundaram S.,Tagami H.,Takeda J.,Takemoto K.,Wada C.,Yamamoto Y.,Horiuchi T.
A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map.
DNA Res.
3
379-392
1996
426520
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
426521
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
426522
Yoshida T.,Ueguchi C.,Yamada H.,Mizuno T.
Function of the Escherichia coli nucleoid protein, H-NS: molecular analysis of a subset of proteins whose expression is enhanced in a hns deletion mutant.
Mol. Gen. Genet.
237
113-122
1993
426523
Misra K.,Banerjee A.B.,Ray S.,Ray M.
Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione.
Biochem. J.
305
999-1003
1995
426524
Sastry M.S.R.,Korotkov K.,Brodsky Y.,Baneyx F.
Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures.
J. Biol. Chem.
277
46026-46034
2002
426525
Malki A.,Kern R.,Abdallah J.,Richarme G.
Characterization of the Escherichia coli YedU protein as a molecular chaperone.
Biochem. Biophys. Res. Commun.
301
430-436
2003
426526
Mujacic M.,Bader M.W.,Baneyx F.
Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions.
Mol. Microbiol.
51
849-859
2004
426527
Sastry M.S.R.,Quigley P.M.,Hol W.G.J.,Baneyx F.
The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures.
Proc. Natl. Acad. Sci. U.S.A.
101
8587-8592
2004
426528
Malki A.,Caldas T.,Abdallah J.,Kern R.,Eckey V.,Kim S.J.,Cha S.S.,Mori H.,Richarme G.
Peptidase activity of the Escherichia coli Hsp31 chaperone.
J. Biol. Chem.
280
14420-14426
2005
426529
Mujacic M.,Baneyx F.
Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31.
Mol. Microbiol.
60
1576-1589
2006
426530
Mujacic M.,Baneyx F.
Chaperone Hsp31 contributes to acid resistance in stationary-phase Escherichia coli.
Appl. Environ. Microbiol.
73
1014-1018
2007
426531
Subedi K.P.,Choi D.,Kim I.,Min B.,Park C.
Hsp31 of Escherichia coli K-12 is glyoxalase III.
Mol. Microbiol.
81
926-936
2011
426532
Kim O.-G.,Kim I.-K.,Kim G.-H.,Ko J.,Park C.,Suh P.-G.,Kang S.-O.,Lee H.-S.,Cha S.-S.
Crystallization and preliminary X-ray crystallographic analysis of a yedU gene product from Escherichia coli.
Acta Crystallogr. D
58
1217-1219
2002
426533
Mihoub M.,Abdallah J.,Gontero B.,Dairou J.,Richarme G.
The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal.
Biochem. Biophys. Res. Commun.
463
1305-1310
2015
426534
Abdallah J.,Mihoub M.,Gautier V.,Richarme G.
The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal.
Biochem. Biophys. Res. Commun.
470
282-286
2016
426535
Richarme G.,Liu C.,Mihoub M.,Abdallah J.,Leger T.,Joly N.,Liebart J.C.,Jurkunas U.V.,Nadal M.,Bouloc P.,Dairou J.,Lamouri A.
Guanine glycation repair by DJ-1/Park7 and its bacterial homologs.
Science
357
208-211
2017
426536
Lee S.-J.,Kim S.J.,Kim I.-K.,Ko J.,Jeong C.-S.,Kim G.-H.,Park C.,Kang S.-O.,Suh P.-G.,Lee H.-S.,Cha S.-S.
Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain.
J. Biol. Chem.
278
44552-44559
2003
426537
Quigley P.M.,Korotkov K.,Baneyx F.,Hol W.G.J.
The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad.
Proc. Natl. Acad. Sci. U.S.A.
100
3137-3142
2003
426538
Zhao Y.,Liu D.,Kaluarachchi W.D.,Bellamy H.D.,White M.A.,Fox R.O.
The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites.
Protein Sci.
12
2303-2311
2003
426539
Quigley P.M.,Korotkov K.,Baneyx F.,Hol W.G.J.
A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function.
Protein Sci.
13
269-277
2004
