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Protein

Cysteine desulfurase IscS

Gene

iscS

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei155Pyridoxal phosphateUniRule annotation1
Binding sitei183Pyridoxal phosphateUniRule annotation1 Publication1
Binding sitei243Pyridoxal phosphateUniRule annotation1 Publication1
Active sitei328Cysteine persulfide intermediateUniRule annotation1
Metal bindingi328Iron-sulfur (2Fe-2S); via persulfide group; shared with IscUUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processtRNA processing
Ligand2Fe-2S, Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotationCurated

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39R → E: Decreased binding to CyaY. 1 Publication1
Mutagenesisi45W → R: No binding to TusA, decreased binding to ThiI. 3% 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U), 7% 4-thiouridine produced. 1 Publication1
Mutagenesisi49E → A: No binding to TusA. 24% mnm(5)s(2)U tRNA produced. 1 Publication1
Mutagenesisi52D → A, M, R or Y: No binding to TusA. 0-20% mnm(5)s(2)U tRNA produced. 1 Publication1
Mutagenesisi65D → F: Decreased binding to TusA. 22% mnm(5)s(2)U tRNA produced. 1 Publication1
Mutagenesisi89F → E: Decreased binding to ThiI. 1 Publication1
Mutagenesisi112R → E: Decreased binding to IscX. 1 Publication1
Mutagenesisi116R → E: Decreased binding to CyaY, IscX, ThiI. 1 Publication1
Mutagenesisi220R → E: No binding to CyaY, IscX, ThiI. 1 Publication1
Mutagenesisi223 – 225RVR → EVE: No binding to IscX. 1 Publication3
Mutagenesisi223R → E: No binding CyaY, IscX, decreased binding to ThiI. 1 Publication1
Mutagenesisi225 – 227RIE → EIR: No binding to CyaY, IscX. 1 Publication3
Mutagenesisi234G → L: Decreased binding to CyaY, IscX. 1 Publication1
Mutagenesisi237 – 239RGM → EGE: No binding to CyaY, IscX, ThiI. 1 Publication3
Mutagenesisi311E → R: Decreased binding to ThiI. 1 Publication1
Mutagenesisi327A → V: No binding to IscX, decreased binding to CyaY, IscU, ThiI. 1 Publication1
Mutagenesisi328C → S: Retains binding to IscU, ThiI. 1 Publication1
Mutagenesisi340R → E: No binding to CyaY, ThiI, decreased binding to IscX, TusA. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001502651 – 404Cysteine desulfurase IscSAdd BLAST404

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei206N6-(pyridoxal phosphate)lysineUniRule annotation1 Publication1

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

Binary interactionsi

Show more details

Protein-protein interaction databases

DIPiDIP-58573N
IntActiP0A6B9, 5 interactors
STRINGi155864.Z3797

Structurei

Secondary structure

1404
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Turni9 – 11Combined sources3
Helixi17 – 23Combined sources7
Beta strandi26 – 28Combined sources3
Helixi42 – 62Combined sources21
Helixi66 – 68Combined sources3
Beta strandi69 – 74Combined sources6
Helixi75 – 90Combined sources16
Turni91 – 93Combined sources3
Beta strandi96 – 100Combined sources5
Helixi105 – 116Combined sources12
Beta strandi120 – 124Combined sources5
Helixi134 – 140Combined sources7
Beta strandi145 – 149Combined sources5
Turni155 – 157Combined sources3
Helixi163 – 173Combined sources11
Beta strandi176 – 180Combined sources5
Turni182 – 187Combined sources6
Turni192 – 194Combined sources3
Beta strandi198 – 204Combined sources7
Turni205 – 208Combined sources4
Beta strandi214 – 218Combined sources5
Turni220 – 223Combined sources4
Turni235 – 239Combined sources5
Helixi246 – 281Combined sources36
Beta strandi287 – 291Combined sources5
Beta strandi293 – 296Combined sources4
Beta strandi300 – 305Combined sources6
Helixi310 – 316Combined sources7
Turni317 – 319Combined sources3
Beta strandi323 – 325Combined sources3
Helixi337 – 342Combined sources6
Helixi346 – 350Combined sources5
Beta strandi352 – 356Combined sources5
Helixi363 – 381Combined sources19
Helixi385 – 389Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0A6B9

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni75 – 76Pyridoxal phosphate bindingUniRule annotation1 Publication2
Regioni203 – 205Pyridoxal phosphate bindingUniRule annotation1 Publication3

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

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_00331 Cys_desulf_IscS, 1 hit
InterProiView protein in InterPro
IPR000192 Aminotrans_V_dom
IPR020578 Aminotrans_V_PyrdxlP_BS
IPR010240 Cys_deSase_IscS
IPR016454 Cysteine_dSase
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PANTHERiPTHR11601:SF34 PTHR11601:SF34, 1 hit
PfamiView protein in Pfam
PF00266 Aminotran_5, 1 hit
PIRSFiPIRSF005572 NifS, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR02006 IscS, 1 hit
PROSITEiView protein in PROSITE
PS00595 AA_TRANSFER_CLASS_5, 1 hit

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB36819 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_NOKN01000002.1

Genome annotation databases

EnsemblBacteriaiAAG57644; AAG57644; Z3797
BAB36819; BAB36819; BAB36819
GeneIDi915161
KEGGiece:Z3797
ecs:ECs3396
PATRICifig|386585.9.peg.3548

Similar proteinsi

Entry informationi

Entry nameiISCS_ECO57
AccessioniPrimary (citable) accession number: P0A6B9
Secondary accession number(s): P39171
, P76581, P76992, Q8XA86
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 25, 2018
This is version 88 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health