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Protein

Cysteine desulfurase IscS

Gene

iscS

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis (biotin, thiamine, molybdopterin). Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine, then delivers the sulfur to an acceptor protein such as CyaY, IscU, IscX, MoaD/MoeB, ThiI, or TusA. Transfers sulfur to acceptor proteins via a transpersulfidation reaction; the flexibility of the persulfide sulfur-carrying Cys-328 allows it to reach different partners docked on the homodimer surface. May function as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate.1 Publication

Catalytic activityi

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation1 Publication

Pathwayi: iron-sulfur cluster biosynthesis

This protein is involved in the pathway iron-sulfur cluster biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway iron-sulfur cluster biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551Pyridoxal phosphateUniRule annotation
Binding sitei183 – 1831Pyridoxal phosphateUniRule annotation1 Publication
Binding sitei243 – 2431Pyridoxal phosphateUniRule annotation1 Publication
Active sitei328 – 3281Cysteine persulfide intermediateUniRule annotation
Metal bindingi328 – 3281Iron-sulfur (2Fe-2S); via persulfide group; shared with IscUUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3359-MONOMER.
UniPathwayiUPA00266.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine desulfurase IscS1 PublicationUniRule annotation (EC:2.8.1.7UniRule annotation)
Gene namesi
Name:iscSUniRule annotation
Ordered Locus Names:Z3797, ECs3396
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotationCurated

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391R → E: Decreased binding to CyaY. 1 Publication
Mutagenesisi45 – 451W → R: No binding to TusA, decreased binding to ThiI. 3% 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U), 7% 4-thiouridine produced. 1 Publication
Mutagenesisi49 – 491E → A: No binding to TusA. 24% mnm(5)s(2)U tRNA produced. 1 Publication
Mutagenesisi52 – 521D → A, M, R or Y: No binding to TusA. 0-20% mnm(5)s(2)U tRNA produced. 1 Publication
Mutagenesisi65 – 651D → F: Decreased binding to TusA. 22% mnm(5)s(2)U tRNA produced. 1 Publication
Mutagenesisi89 – 891F → E: Decreased binding to ThiI. 1 Publication
Mutagenesisi112 – 1121R → E: Decreased binding to IscX. 1 Publication
Mutagenesisi116 – 1161R → E: Decreased binding to CyaY, IscX, ThiI. 1 Publication
Mutagenesisi220 – 2201R → E: No binding to CyaY, IscX, ThiI. 1 Publication
Mutagenesisi223 – 2253RVR → EVE: No binding to IscX. 1 Publication
Mutagenesisi223 – 2231R → E: No binding CyaY, IscX, decreased binding to ThiI. 1 Publication
Mutagenesisi225 – 2273RIE → EIR: No binding to CyaY, IscX. 1 Publication
Mutagenesisi234 – 2341G → L: Decreased binding to CyaY, IscX. 1 Publication
Mutagenesisi237 – 2393RGM → EGE: No binding to CyaY, IscX, ThiI. 1 Publication
Mutagenesisi311 – 3111E → R: Decreased binding to ThiI. 1 Publication
Mutagenesisi327 – 3271A → V: No binding to IscX, decreased binding to CyaY, IscU, ThiI. 1 Publication
Mutagenesisi328 – 3281C → S: Retains binding to IscU, ThiI. 1 Publication
Mutagenesisi340 – 3401R → E: No binding to CyaY, ThiI, decreased binding to IscX, TusA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 404404Cysteine desulfurase IscSPRO_0000150265Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei206 – 2061N6-(pyridoxal phosphate)lysineUniRule annotation1 Publication

Proteomic databases

PRIDEiP0A6B9.

Interactioni

Subunit structurei

Homodimer. The homodimer interacts with CyaY, IscU, IscX, ThiI and TusA via an extended surface across both subunits centered around Cys-328. The binding sites for different partners do not necessarily overlap. Certain pairs of proteins can bind simultaneously to IscS; IscS-IscU-CyaY and IscS-IscU-IscX complexes can be isolated in vitro, but others (IscS-IscU-TusA, IscS-TusA-CyaY or IscS-IscX-TusA) complexes cannot.1 Publication

Protein-protein interaction databases

DIPiDIP-58573N.
STRINGi155864.Z3797.

Structurei

Secondary structure

1
404
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Turni9 – 113Combined sources
Helixi17 – 237Combined sources
Beta strandi26 – 283Combined sources
Helixi42 – 6221Combined sources
Helixi66 – 683Combined sources
Beta strandi69 – 746Combined sources
Helixi75 – 9016Combined sources
Turni91 – 933Combined sources
Beta strandi96 – 1005Combined sources
Helixi105 – 11612Combined sources
Beta strandi120 – 1245Combined sources
Helixi134 – 1407Combined sources
Beta strandi145 – 1495Combined sources
Turni155 – 1573Combined sources
Helixi163 – 17311Combined sources
Beta strandi176 – 1805Combined sources
Turni182 – 1876Combined sources
Turni192 – 1943Combined sources
Beta strandi198 – 2047Combined sources
Turni205 – 2084Combined sources
Beta strandi214 – 2185Combined sources
Turni220 – 2234Combined sources
Turni235 – 2395Combined sources
Helixi246 – 28136Combined sources
Beta strandi287 – 2915Combined sources
Beta strandi293 – 2964Combined sources
Beta strandi300 – 3056Combined sources
Helixi310 – 3167Combined sources
Turni317 – 3193Combined sources
Beta strandi323 – 3253Combined sources
Helixi337 – 3426Combined sources
Helixi346 – 3505Combined sources
Beta strandi352 – 3565Combined sources
Helixi363 – 38119Combined sources
Helixi385 – 3895Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LVJX-ray2.44A/B1-404[»]
3LVKX-ray2.44A1-404[»]
3LVLX-ray3.00B1-404[»]
3LVMX-ray2.05A/B1-404[»]
ProteinModelPortaliP0A6B9.
SMRiP0A6B9. Positions 1-398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6B9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni75 – 762Pyridoxal phosphate bindingUniRule annotation1 Publication
Regioni203 – 2053Pyridoxal phosphate bindingUniRule annotation1 Publication

Sequence similaritiesi

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C3J. Bacteria.
COG1104. LUCA.
HOGENOMiHOG000017510.
KOiK04487.
OMAiEPIQSGG.
OrthoDBiEOG62RSBK.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00331. Cys_desulf_IscS.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010240. Cys_deSase_IscS.
IPR016454. Cysteine_dSase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF005572. NifS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02006. IscS. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A6B9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLPIYLDYS ATTPVDPRVA EKMMQFMTMD GTFGNPASRS HRFGWQAEEA
60 70 80 90 100
VDIARNQIAD LVGADPREIV FTSGATESDN LAIKGAANFY QKKGKHIITS
110 120 130 140 150
KTEHKAVLDT CRQLEREGFE VTYLAPQRNG IIDLKELEAA MRDDTILVSI
160 170 180 190 200
MHVNNEIGVV QDIAAIGEMC RARGIIYHVD ATQSVGKLPI DLSQLKVDLM
210 220 230 240 250
SFSGHKIYGP KGIGALYVRR KPRVRIEAQM HGGGHERGMR SGTLPVHQIV
260 270 280 290 300
GMGEAYRIAK EEMATEMERL RGLRNRLWNG IKDIEEVYLN GDLEHGAPNI
310 320 330 340 350
LNVSFNYVEG ESLIMALKDL AVSSGSACTS ASLEPSYVLR ALGLNDELAH
360 370 380 390 400
SSIRFSLGRF TTEEEIDYTI ELVRKSIGRL RDLSPLWEMY KQGVDLNSIE

WAHH
Length:404
Mass (Da):45,090
Last modified:June 7, 2005 - v1
Checksum:i1E4F2E6F9CD266B0
GO

Sequence cautioni

The sequence AAG57644.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB36819.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57644.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB36819.1. Different initiation.
RefSeqiNP_311423.2. NC_002695.1.
WP_001295373.1. NZ_LPWC01000059.1.

Genome annotation databases

EnsemblBacteriaiAAG57644; AAG57644; Z3797.
BAB36819; BAB36819; BAB36819.
GeneIDi915161.
KEGGiece:Z3797.
ecs:ECs3396.
PATRICi18356224. VBIEscCol44059_3307.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57644.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB36819.1. Different initiation.
RefSeqiNP_311423.2. NC_002695.1.
WP_001295373.1. NZ_LPWC01000059.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LVJX-ray2.44A/B1-404[»]
3LVKX-ray2.44A1-404[»]
3LVLX-ray3.00B1-404[»]
3LVMX-ray2.05A/B1-404[»]
ProteinModelPortaliP0A6B9.
SMRiP0A6B9. Positions 1-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58573N.
STRINGi155864.Z3797.

Proteomic databases

PRIDEiP0A6B9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG57644; AAG57644; Z3797.
BAB36819; BAB36819; BAB36819.
GeneIDi915161.
KEGGiece:Z3797.
ecs:ECs3396.
PATRICi18356224. VBIEscCol44059_3307.

Phylogenomic databases

eggNOGiENOG4105C3J. Bacteria.
COG1104. LUCA.
HOGENOMiHOG000017510.
KOiK04487.
OMAiEPIQSGG.
OrthoDBiEOG62RSBK.

Enzyme and pathway databases

UniPathwayiUPA00266.
BioCyciECOL386585:GJFA-3359-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A6B9.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00331. Cys_desulf_IscS.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010240. Cys_deSase_IscS.
IPR016454. Cysteine_dSase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF005572. NifS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02006. IscS. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
  3. "Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions."
    Shi R., Proteau A., Villarroya M., Moukadiri I., Zhang L., Trempe J.F., Matte A., Armengod M.E., Cygler M.
    PLoS Biol. 8:E1000354-E1000354(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH TUSA OR APO-ISCU AND PYRIDOXAL PHOSPHATE, FUNCTION, INTERACTION WITH CYAY; ISCU; ISCX; THII AND TUSA, SUBUNIT, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-206, PATHWAY, MUTAGENESIS OF ARG-39; TRP-45; GLU-49; ASP-52; ASP-65; PHE-89; ARG-112; ARG-116; ARG-220; ARG-223; 223-ARG--ARG-225; 225-ARG--GLU-227; GLY-234; 237-ARG--MET-239; GLU-311; ALA-327; CYS-328 AND ARG-340.
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

Entry informationi

Entry nameiISCS_ECO57
AccessioniPrimary (citable) accession number: P0A6B9
Secondary accession number(s): P39171
, P76581, P76992, Q8XA86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 11, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.