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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)DescriptionActionsGraphical viewLength
Active sitei364Cysteine persulfide intermediate1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi55H → A: No effect. 1 Publication1
Mutagenesisi123H → A: Loss of function; possibly due to destabilization of PLP in the active site. 1 Publication1
Mutagenesisi364C → A: Abolishes activity towards L-cysteine but not towards selenocysteine. 1 Publication1
Mutagenesisi379R → A: Loss of function. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001503291 – 406Cysteine desulfuraseAdd BLAST406

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei226N6-(pyridoxal phosphate)lysine1

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 interactors.
DIPiDIP-9324N.
IntActiP77444. 14 interactors.
STRINGi511145.b1680.

Structurei

Secondary structure

1406
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 10Combined sources6
Helixi13 – 16Combined sources4
Turni29 – 31Combined sources3
Helixi37 – 49Combined sources13
Helixi60 – 79Combined sources20
Helixi85 – 87Combined sources3
Beta strandi88 – 93Combined sources6
Helixi94 – 109Combined sources16
Beta strandi115 – 119Combined sources5
Helixi124 – 126Combined sources3
Helixi128 – 137Combined sources10
Beta strandi140 – 144Combined sources5
Helixi154 – 156Combined sources3
Helixi157 – 160Combined sources4
Beta strandi165 – 173Combined sources9
Turni175 – 177Combined sources3
Helixi183 – 192Combined sources10
Beta strandi196 – 200Combined sources5
Turni202 – 207Combined sources6
Helixi212 – 215Combined sources4
Beta strandi218 – 223Combined sources6
Helixi224 – 226Combined sources3
Beta strandi234 – 238Combined sources5
Helixi240 – 243Combined sources4
Beta strandi252 – 258Combined sources7
Turni261 – 263Combined sources3
Beta strandi264 – 267Combined sources4
Helixi272 – 274Combined sources3
Helixi281 – 297Combined sources17
Helixi299 – 317Combined sources19
Beta strandi323 – 327Combined sources5
Beta strandi333 – 339Combined sources7
Helixi344 – 353Combined sources10
Beta strandi359 – 361Combined sources3
Helixi366 – 371Combined sources6
Beta strandi377 – 381Combined sources5
Helixi388 – 405Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C0NX-ray2.80A1-406[»]
1I29X-ray2.80A1-406[»]
1JF9X-ray2.00A1-406[»]
1KMJX-ray2.00A1-406[»]
1KMKX-ray2.20A1-406[»]
5DB5X-ray2.75A/B1-406[»]
ProteinModelPortaliP77444.
SMRiP77444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77444.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01831. SufS_aminotrans_5. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C0NX-ray2.80A1-406[»]
1I29X-ray2.80A1-406[»]
1JF9X-ray2.00A1-406[»]
1KMJX-ray2.00A1-406[»]
1KMKX-ray2.20A1-406[»]
5DB5X-ray2.75A/B1-406[»]
ProteinModelPortaliP77444.
SMRiP77444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260281. 57 interactors.
DIPiDIP-9324N.
IntActiP77444. 14 interactors.
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.
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. 1 hit.
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...

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: November 2, 2016
This is version 148 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.