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Protein

Cysteine desulfurase

Gene

sufS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.5 Publications

Catalytic activityi

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor.

Cofactori

Enzyme regulationi

Displays a strong preference for selenocysteine as a substrate in vitro and is only very sightly active using cysteine. The interactions with SufE and the SufBCD complex act synergistically to enhance, up to 50-fold, its cysteine desulfurase activity.3 Publications

Pathwayi: iron-sulfur cluster biosynthesis

This protein is involved in the pathway iron-sulfur cluster biosynthesis, which is part of Cofactor biosynthesis.
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
Active sitei364 – 3641Cysteine persulfide intermediate

GO - Molecular functioni

  • cysteine desulfurase activity Source: EcoCyc
  • pyridoxal phosphate binding Source: EcoCyc
  • selenocysteine lyase activity Source: EcoCyc

GO - Biological processi

  • cysteine metabolic process Source: InterPro
  • iron-sulfur cluster assembly Source: EcoCyc
  • selenium compound metabolic process Source: EcoCyc
  • sulfur compound metabolic process Source: EcoCyc
  • sulfur incorporation into metallo-sulfur cluster Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:G6906-MONOMER.
ECOL316407:JW1670-MONOMER.
MetaCyc:G6906-MONOMER.
BRENDAi2.8.1.7. 2026.
4.4.1.16. 2026.
UniPathwayiUPA00266.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine desulfurase (EC:2.8.1.7)
Alternative name(s):
Selenocysteine beta-lyase
Short name:
SCL
Selenocysteine lyase (EC:4.4.1.16)
Selenocysteine reductase
Gene namesi
Name:sufS
Synonyms:csdB, ynhB
Ordered Locus Names:b1680, JW1670
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13962. sufS.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi55 – 551H → A: No effect. 1 Publication
Mutagenesisi123 – 1231H → A: Loss of function; possibly due to destabilization of PLP in the active site. 1 Publication
Mutagenesisi364 – 3641C → A: Abolishes activity towards L-cysteine but not towards selenocysteine. 1 Publication
Mutagenesisi379 – 3791R → A: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Cysteine desulfurasePRO_0000150329Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei226 – 2261N6-(pyridoxal phosphate)lysine

Proteomic databases

EPDiP77444.
PaxDbiP77444.
PRIDEiP77444.

Expressioni

Inductioni

Suf operon is under both the Fe-dependent Fur repressor and the oxidative stress dependent OxyR activator.

Interactioni

Subunit structurei

Homodimer. Interacts with SufE and the SufBCD complex composed of SufB, SufC and SufD. The interaction with SufE is required to mediate the direct transfer of the sulfur atom from the S-sulfanylcysteine.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
sufEP761943EBI-1124981,EBI-1124973

Protein-protein interaction databases

BioGridi4260281. 57 interactions.
DIPiDIP-9324N.
IntActiP77444. 14 interactions.
STRINGi511145.b1680.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 106Combined sources
Helixi13 – 164Combined sources
Turni29 – 313Combined sources
Helixi37 – 4913Combined sources
Helixi60 – 7920Combined sources
Helixi85 – 873Combined sources
Beta strandi88 – 936Combined sources
Helixi94 – 10916Combined sources
Beta strandi115 – 1195Combined sources
Helixi124 – 1263Combined sources
Helixi128 – 13710Combined sources
Beta strandi140 – 1445Combined sources
Helixi154 – 1563Combined sources
Helixi157 – 1604Combined sources
Beta strandi165 – 1739Combined sources
Turni175 – 1773Combined sources
Helixi183 – 19210Combined sources
Beta strandi196 – 2005Combined sources
Turni202 – 2076Combined sources
Helixi212 – 2154Combined sources
Beta strandi218 – 2236Combined sources
Helixi224 – 2263Combined sources
Beta strandi234 – 2385Combined sources
Helixi240 – 2434Combined sources
Beta strandi252 – 2587Combined sources
Turni261 – 2633Combined sources
Beta strandi264 – 2674Combined sources
Helixi272 – 2743Combined sources
Helixi281 – 29717Combined sources
Helixi299 – 31719Combined sources
Beta strandi323 – 3275Combined sources
Beta strandi333 – 3397Combined sources
Helixi344 – 35310Combined sources
Beta strandi359 – 3613Combined sources
Helixi366 – 3716Combined sources
Beta strandi377 – 3815Combined sources
Helixi388 – 40518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C0NX-ray2.80A1-406[»]
1I29X-ray2.80A1-406[»]
1JF9X-ray2.00A1-406[»]
1KMJX-ray2.00A1-406[»]
1KMKX-ray2.20A1-406[»]
ProteinModelPortaliP77444.
SMRiP77444. Positions 2-406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77444.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C9B. Bacteria.
COG0520. LUCA.
HOGENOMiHOG000017511.
InParanoidiP77444.
KOiK11717.
OMAiAEKVHGK.
OrthoDBiEOG68DD0M.
PhylomeDBiP77444.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01831. SufS_aminotrans_5.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010970. Cys_dSase_SufS.
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]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01979. sufS. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P77444-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIFSVDKVRA DFPVLSREVN GLPLAYLDSA ASAQKPSQVI DAEAEFYRHG
60 70 80 90 100
YAAVHRGIHT LSAQATEKME NVRKRASLFI NARSAEELVF VRGTTEGINL
110 120 130 140 150
VANSWGNSNV RAGDNIIISQ MEHHANIVPW QMLCARVGAE LRVIPLNPDG
160 170 180 190 200
TLQLETLPTL FDEKTRLLAI THVSNVLGTE NPLAEMITLA HQHGAKVLVD
210 220 230 240 250
GAQAVMHHPV DVQALDCDFY VFSGHKLYGP TGIGILYVKE ALLQEMPPWE
260 270 280 290 300
GGGSMIATVS LSEGTTWTKA PWRFEAGTPN TGGIIGLGAA LEYVSALGLN
310 320 330 340 350
NIAEYEQNLM HYALSQLESV PDLTLYGPQN RLGVIAFNLG KHHAYDVGSF
360 370 380 390 400
LDNYGIAVRT GHHCAMPLMA YYNVPAMCRA SLAMYNTHEE VDRLVTGLQR

IHRLLG
Length:406
Mass (Da):44,434
Last modified:February 1, 1997 - v1
Checksum:i9374C43C3AD9D8E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB055108 Genomic DNA. Translation: BAB21542.1.
U00096 Genomic DNA. Translation: AAC74750.1.
AP009048 Genomic DNA. Translation: BAA15457.1.
PIRiH64925.
RefSeqiNP_416195.1. NC_000913.3.
WP_000577988.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74750; AAC74750; b1680.
BAA15457; BAA15457; BAA15457.
GeneIDi946185.
KEGGiecj:JW1670.
eco:b1680.
PATRICi32118666. VBIEscCol129921_1751.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB055108 Genomic DNA. Translation: BAB21542.1.
U00096 Genomic DNA. Translation: AAC74750.1.
AP009048 Genomic DNA. Translation: BAA15457.1.
PIRiH64925.
RefSeqiNP_416195.1. NC_000913.3.
WP_000577988.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C0NX-ray2.80A1-406[»]
1I29X-ray2.80A1-406[»]
1JF9X-ray2.00A1-406[»]
1KMJX-ray2.00A1-406[»]
1KMKX-ray2.20A1-406[»]
ProteinModelPortaliP77444.
SMRiP77444. Positions 2-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260281. 57 interactions.
DIPiDIP-9324N.
IntActiP77444. 14 interactions.
STRINGi511145.b1680.

Proteomic databases

EPDiP77444.
PaxDbiP77444.
PRIDEiP77444.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74750; AAC74750; b1680.
BAA15457; BAA15457; BAA15457.
GeneIDi946185.
KEGGiecj:JW1670.
eco:b1680.
PATRICi32118666. VBIEscCol129921_1751.

Organism-specific databases

EchoBASEiEB3720.
EcoGeneiEG13962. sufS.

Phylogenomic databases

eggNOGiENOG4105C9B. Bacteria.
COG0520. LUCA.
HOGENOMiHOG000017511.
InParanoidiP77444.
KOiK11717.
OMAiAEKVHGK.
OrthoDBiEOG68DD0M.
PhylomeDBiP77444.

Enzyme and pathway databases

UniPathwayiUPA00266.
BioCyciEcoCyc:G6906-MONOMER.
ECOL316407:JW1670-MONOMER.
MetaCyc:G6906-MONOMER.
BRENDAi2.8.1.7. 2026.
4.4.1.16. 2026.

Miscellaneous databases

EvolutionaryTraceiP77444.
PROiP77444.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01831. SufS_aminotrans_5.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010970. Cys_dSase_SufS.
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]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01979. sufS. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary X-ray crystallographic studies."
    Mihara H., Maeda M., Fujii T., Kurihara T., Hata Y., Esaki N.
    J. Biol. Chem. 274:14768-14772(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, CHARACTERIZATION, X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "SufS is a NifS-like protein, and SufD is necessary for stability of the 2Fe-2S FhuF protein in Escherichia coli."
    Patzer S.I., Hantke K.
    J. Bacteriol. 181:3307-3309(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE NAME.
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate."
    Lacourciere G.M., Mihara H., Kurihara T., Esaki N., Stadtman T.C.
    J. Biol. Chem. 275:23769-23773(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions."
    Mihara H., Kurihara T., Yoshimura T., Esaki N.
    J. Biochem. 127:559-567(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-364.
  8. "A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids."
    Takahashi Y., Tokumoto U.
    J. Biol. Chem. 277:28380-28383(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FE-S CLUSTER SYSTEM.
  9. "The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H."
    Mihara H., Kato S., Lacourciere G.M., Stadtman T.C., Kennedy R.A.J.D., Kurihara T., Tokumoto U., Takahashi Y., Esaki N.
    Proc. Natl. Acad. Sci. U.S.A. 99:6679-6683(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase."
    Loiseau L., Ollagnier-de-Choudens S., Nachin L., Fontecave M., Barras F.
    J. Biol. Chem. 278:38352-38359(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH SUFE AND SUFBCD COMPLEX.
    Strain: K12 / TG1.
  11. "The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli."
    Outten F.W., Wood M.J., Munoz F.M., Storz G.
    J. Biol. Chem. 278:45713-45719(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH SUFE AND SUFBCD COMPLEX.
    Strain: K12 / MG1655 / ATCC 47076.
  12. "Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for sulfur transfer from SufS to SufE."
    Ollagnier-de-Choudens S., Lascoux D., Loiseau L., Barras F., Forest E., Fontecave M.
    FEBS Lett. 555:263-267(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH SUFE.
  13. "Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase."
    Fujii T., Maeda M., Mihara H., Kurihara T., Esaki N., Hata Y.
    Biochemistry 39:1263-1273(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  14. "Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine."
    Mihara H., Fujii T., Kato S., Kurihara T., Hata Y., Esaki N.
    J. Biochem. 131:679-685(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), MUTAGENESIS OF HIS-55; HIS-123 AND ARG-379.
  15. "Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formation."
    Lima C.D.
    J. Mol. Biol. 315:1199-1208(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH L-CYSTEINE AND L-SELENOCYSTEINE, PYRIDOXAL PHOSPHATE AT LYS-226.

Entry informationi

Entry nameiSUFS_ECOLI
AccessioniPrimary (citable) accession number: P77444
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 1, 1997
Last modified: March 16, 2016
This is version 145 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, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.