UniProtKB - P77444 (SUFS_ECOLI)
Protein
Cysteine desulfurase
Gene
sufS
Organism
Escherichia coli (strain K12)
Status
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
Cofactori
Activity regulationi
Displays a strong preference for selenocysteine as a substrate in vitro and is only very slightly 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
: iron-sulfur cluster biosynthesis Pathwayi
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 364 | Cysteine persulfide intermediate | 1 |
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
Keywordsi
Molecular function | Lyase, Transferase |
Ligand | Pyridoxal phosphate |
Enzyme and pathway databases
BioCyci | EcoCyc:G6906-MONOMER MetaCyc:G6906-MONOMER |
BRENDAi | 2.8.1.7, 2026 4.4.1.16, 2026 |
UniPathwayi | UPA00266 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:sufS Synonyms:csdB, ynhB Ordered Locus Names:b1680, JW1670 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 55 | H → A: No effect. 1 Publication | 1 | |
Mutagenesisi | 123 | H → A: Loss of function; possibly due to destabilization of PLP in the active site. 1 Publication | 1 | |
Mutagenesisi | 364 | C → A: Abolishes activity towards L-cysteine but not towards selenocysteine. 1 Publication | 1 | |
Mutagenesisi | 379 | R → A: Loss of function. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB04217, L-2-amino-3-butynoic acid DB02761, S-Mercaptocysteine DB03049, S-Selanyl Cysteine DB02345, Selenocysteine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000150329 | 1 – 406 | Cysteine desulfuraseAdd BLAST | 406 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 226 | N6-(pyridoxal phosphate)lysine | 1 |
Proteomic databases
jPOSTi | P77444 |
PaxDbi | P77444 |
PRIDEi | P77444 |
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 PublicationsBinary interactionsi
P77444
With | #Exp. | IntAct |
---|---|---|
sufE [P76194] | 3 | EBI-1124981,EBI-1124973 |
Protein-protein interaction databases
BioGRIDi | 4260281, 100 interactors 850545, 4 interactors |
ComplexPortali | CPX-2124, SufS complex |
DIPi | DIP-9324N |
IntActi | P77444, 14 interactors |
STRINGi | 511145.b1680 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P77444 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P77444 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0520, Bacteria |
HOGENOMi | CLU_003433_2_5_6 |
InParanoidi | P77444 |
PhylomeDBi | P77444 |
Family and domain databases
Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 1 hit |
HAMAPi | MF_01831, SufS_aminotrans_5, 1 hit |
InterProi | View protein in InterPro IPR000192, Aminotrans_V_dom IPR020578, Aminotrans_V_PyrdxlP_BS IPR010970, Cys_dSase_SufS IPR015424, PyrdxlP-dep_Trfase IPR015422, PyrdxlP-dep_Trfase_dom1 IPR015421, PyrdxlP-dep_Trfase_major |
Pfami | View protein in Pfam PF00266, Aminotran_5, 1 hit |
SUPFAMi | SSF53383, SSF53383, 1 hit |
TIGRFAMsi | TIGR01979, sufS, 1 hit |
PROSITEi | View protein in PROSITE PS00595, AA_TRANSFER_CLASS_5, 1 hit |
i Sequence
Sequence statusi: Complete.
P77444-1 [UniParc]FASTAAdd to basket
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
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 |
PIRi | H64925 |
RefSeqi | NP_416195.1, NC_000913.3 WP_000577988.1, NZ_SSZK01000001.1 |
Genome annotation databases
EnsemblBacteriai | AAC74750; AAC74750; b1680 BAA15457; BAA15457; BAA15457 |
GeneIDi | 946185 |
KEGGi | ecj:JW1670 eco:b1680 |
PATRICi | fig|1411691.4.peg.578 |
Similar proteinsi
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 |
PIRi | H64925 |
RefSeqi | NP_416195.1, NC_000913.3 WP_000577988.1, NZ_SSZK01000001.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1C0N | X-ray | 2.80 | A | 1-406 | [»] | |
1I29 | X-ray | 2.80 | A | 1-406 | [»] | |
1JF9 | X-ray | 2.00 | A | 1-406 | [»] | |
1KMJ | X-ray | 2.00 | A | 1-406 | [»] | |
1KMK | X-ray | 2.20 | A | 1-406 | [»] | |
5DB5 | X-ray | 2.75 | A/B | 1-406 | [»] | |
6MR2 | X-ray | 2.40 | A | 1-406 | [»] | |
6MR6 | X-ray | 2.02 | A | 1-406 | [»] | |
6MRE | X-ray | 2.50 | A | 1-406 | [»] | |
6MRH | X-ray | 2.02 | A | 1-406 | [»] | |
6MRI | X-ray | 2.62 | A | 1-406 | [»] | |
6O10 | X-ray | 2.00 | A | 1-406 | [»] | |
6O11 | X-ray | 1.84 | A | 1-406 | [»] | |
6O12 | X-ray | 2.05 | A | 1-406 | [»] | |
6O13 | X-ray | 2.20 | A | 1-406 | [»] | |
6UY5 | X-ray | 1.50 | A/B | 1-406 | [»] | |
SMRi | P77444 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260281, 100 interactors 850545, 4 interactors |
ComplexPortali | CPX-2124, SufS complex |
DIPi | DIP-9324N |
IntActi | P77444, 14 interactors |
STRINGi | 511145.b1680 |
Chemistry databases
DrugBanki | DB04217, L-2-amino-3-butynoic acid DB02761, S-Mercaptocysteine DB03049, S-Selanyl Cysteine DB02345, Selenocysteine |
Proteomic databases
jPOSTi | P77444 |
PaxDbi | P77444 |
PRIDEi | P77444 |
Genome annotation databases
EnsemblBacteriai | AAC74750; AAC74750; b1680 BAA15457; BAA15457; BAA15457 |
GeneIDi | 946185 |
KEGGi | ecj:JW1670 eco:b1680 |
PATRICi | fig|1411691.4.peg.578 |
Organism-specific databases
EchoBASEi | EB3720 |
Phylogenomic databases
eggNOGi | COG0520, Bacteria |
HOGENOMi | CLU_003433_2_5_6 |
InParanoidi | P77444 |
PhylomeDBi | P77444 |
Enzyme and pathway databases
UniPathwayi | UPA00266 |
BioCyci | EcoCyc:G6906-MONOMER MetaCyc:G6906-MONOMER |
BRENDAi | 2.8.1.7, 2026 4.4.1.16, 2026 |
Miscellaneous databases
EvolutionaryTracei | P77444 |
PROi | PR:P77444 |
Family and domain databases
Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 1 hit |
HAMAPi | MF_01831, SufS_aminotrans_5, 1 hit |
InterProi | View protein in InterPro IPR000192, Aminotrans_V_dom IPR020578, Aminotrans_V_PyrdxlP_BS IPR010970, Cys_dSase_SufS IPR015424, PyrdxlP-dep_Trfase IPR015422, PyrdxlP-dep_Trfase_dom1 IPR015421, PyrdxlP-dep_Trfase_major |
Pfami | View protein in Pfam PF00266, Aminotran_5, 1 hit |
SUPFAMi | SSF53383, SSF53383, 1 hit |
TIGRFAMsi | TIGR01979, sufS, 1 hit |
PROSITEi | View protein in PROSITE PS00595, AA_TRANSFER_CLASS_5, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SUFS_ECOLI | |
Accessioni | P77444Primary (citable) accession number: P77444 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 27, 2001 |
Last sequence update: | February 1, 1997 | |
Last modified: | April 7, 2021 | |
This is version 177 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families