Sequence of ISCS_ECOLI
EC Number:2.8.1.7
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
Other sequences found for EC No. 2.8.1.7
General information:
Sequence
0 MKLPIYLDYS ATTPVDPRVA EKMMQFMTMD GTFGNPASRS HRFGWQAEEA VDIARNQIAD
60 LVGADPREIV FTSGATESDN LAIKGAANFY QKKGKHIITS KTEHKAVLDT CRQLEREGFE
120 VTYLAPQRNG IIDLKELEAA MRDDTILVSI MHVNNEIGVV QDIAAIGEMC RARGIIYHVD
180 ATQSVGKLPI DLSQLKVDLM SFSGHKIYGP KGIGALYVRR KPRVRIEAQM HGGGHERGMR
240 SGTLPVHQIV GMGEAYRIAK EEMATEMERL RGLRNRLWNG IKDIEEVYLN GDLEHGAPNI
300 LNVSFNYVEG ESLIMALKDL AVSSGSACTS ASLEPSYVLR ALGLNDELAH SSIRFSLGRF
360 TTEEEIDYTI ELVRKSIGRL RDLSPLWEMY KQGVDLNSIE WAHH
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
48657
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
48658
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
48659
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
48660
Flint D.H.
Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase.
J. Biol. Chem.
271
16068-16074
1996
48661
Kambampati R.,Lauhon C.T.
IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA.
Biochemistry
38
16561-16568
1999
48662
Link A.J.,Robison K.,Church G.M.
Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
Electrophoresis
18
1259-1313
1997
48663
Mihara H.,Kurihara T.,Yoshimura T.,Esaki N.
Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions.
J. Biochem.
127
559-567
2000
48664
Takahashi Y.,Nakamura M.
Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli.
J. Biochem.
126
917-926
1999
48665
Kiyasu T.,Asakura A.,Nagahashi Y.,Hoshino T.
Contribution of cysteine desulfurase (NifS protein) to the biotin synthase reaction of Escherichia coli.
J. Bacteriol.
182
2879-2885
2000
48666
Lauhon C.T.,Kambampati R.
The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamine, and NAD.
J. Biol. Chem.
275
20096-20103
2000
48667
Lacourciere G.M.,Mihara H.,Kurihara T.,Esaki N.,Stadtman T.C.
Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate.
J. Biol. Chem.
275
23769-23773
2000
48668
Schwartz C.J.,Djaman O.,Imlay J.A.,Kiley P.J.
The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli.
Proc. Natl. Acad. Sci. U.S.A.
97
9009-9014
2000
48669
Urbina H.D.,Silberg J.J.,Hoff K.G.,Vickery L.E.
Transfer of sulfur from IscS to IscU during Fe/S cluster assembly.
J. Biol. Chem.
276
44521-44526
2001
48670
Ikeuchi Y.,Shigi N.,Kato J.,Nishimura A.,Suzuki T.
Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions.
Mol. Cell
21
97-108
2006
48671
Kim J.H.,Tonelli M.,Markley J.L.
Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase.
Proc. Natl. Acad. Sci. U.S.A.
109
454-459
2012
48672
Cupp-Vickery J.R.,Urbina H.,Vickery L.E.
Crystal structure of IscS, a cysteine desulfurase from Escherichia coli.
J. Mol. Biol.
330
1049-1059
2003
