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Protein

Cysteine desulfurase SufS

Gene

sufS

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40-to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity.3 Publications

Catalytic activityi

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.1 Publication

Cofactori

Enzyme regulationi

A Cys to Ala mutation in SufU (Cys-41-Ala) has been described to be a competivie inhibitor of SufS activity and a non-competitive inhibitor (PubMed:21236255, PubMed:24321018).2 Publications

Kineticsi

In the presence of dithiothreitol, which regenerates the second reaction product SufU.S.

  1. KM=86 µM for L-cysteine2 Publications
  2. KM=30 µM for SufU2 Publications
  1. Vmax=1157 nmol/min/mg enzyme in the presence of SufU2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei361Cysteine persulfide intermediateCurated1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciBSUB:BSU32690-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine desulfurase SufS (EC:2.8.1.7)
Gene namesi
Name:sufS
Synonyms:csd, yurW
Ordered Locus Names:BSU32690
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi361C → A: Loss of cysteine desulfurase activity, still binds SufU and Cys. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001502931 – 406Cysteine desulfurase SufSAdd BLAST406

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei224N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

PaxDbiO32164.
PRIDEiO32164.

Interactioni

Subunit structurei

Homodimer. Interacts with SufU; the complex is more stable in the presence of L-cysteine. An N-terminal His-tag destabilizes this interaction.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
sufUO321638EBI-7826704,EBI-8561343

Protein-protein interaction databases

IntActiO32164. 2 interactors.
MINTiMINT-8082716.
STRINGi224308.Bsubs1_010100017736.

Structurei

Secondary structure

1406
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 7Combined sources5
Helixi11 – 13Combined sources3
Turni27 – 29Combined sources3
Helixi35 – 47Combined sources13
Beta strandi54 – 56Combined sources3
Helixi58 – 78Combined sources21
Helixi83 – 85Combined sources3
Beta strandi86 – 90Combined sources5
Helixi92 – 102Combined sources11
Helixi104 – 107Combined sources4
Beta strandi113 – 117Combined sources5
Helixi122 – 124Combined sources3
Helixi126 – 135Combined sources10
Beta strandi138 – 142Combined sources5
Helixi152 – 158Combined sources7
Beta strandi163 – 171Combined sources9
Turni173 – 175Combined sources3
Helixi181 – 190Combined sources10
Beta strandi194 – 198Combined sources5
Turni200 – 205Combined sources6
Helixi210 – 213Combined sources4
Beta strandi216 – 221Combined sources6
Helixi222 – 224Combined sources3
Beta strandi232 – 236Combined sources5
Helixi238 – 243Combined sources6
Beta strandi253 – 257Combined sources5
Beta strandi262 – 264Combined sources3
Helixi269 – 271Combined sources3
Helixi278 – 294Combined sources17
Helixi296 – 315Combined sources20
Beta strandi320 – 322Combined sources3
Beta strandi330 – 336Combined sources7
Helixi341 – 350Combined sources10
Beta strandi356 – 358Combined sources3
Helixi363 – 369Combined sources7
Beta strandi374 – 378Combined sources5
Helixi385 – 406Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5J8QX-ray1.70A1-406[»]
ProteinModelPortaliO32164.
SMRiO32164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C9B. Bacteria.
COG0520. LUCA.
HOGENOMiHOG000017511.
InParanoidiO32164.
KOiK11717.
OMAiMIDFVGL.
PhylomeDBiO32164.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

O32164-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNITDIREQF PILHQQVNGH DLVYLDSAAT SQKPRAVIET LDKYYNQYNS
60 70 80 90 100
NVHRGVHTLG TRATDGYEGA REKVRKFINA KSMAEIIFTK GTTTSLNMVA
110 120 130 140 150
LSYARANLKP GDEVVITYME HHANIIPWQQ AVKATGATLK YIPLQEDGTI
160 170 180 190 200
SLEDVRETVT SNTKIVAVSH VSNVLGTVNP IKEMAKIAHD NGAVIVVDGA
210 220 230 240 250
QSTPHMKIDV QDLDCDFFAL SSHKMCGPTG VGVLYGKKAL LENMEPAEFG
260 270 280 290 300
GEMIDFVGLY ESTWKELPWK FEAGTPIIAG AIGLGAAIDF LEEIGLDEIS
310 320 330 340 350
RHEHKLAAYA LERFRQLDGV TVYGPEERAG LVTFNLDDVH PHDVATVLDA
360 370 380 390 400
EGIAVRAGHH CAQPLMKWLD VTATARASFY LYNTEEEIDK LVEALQKTKE

YFTNVF
Length:406
Mass (Da):44,922
Last modified:January 1, 1998 - v1
Checksum:iE433C0B5965349D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15258.1.
PIRiF70019.
RefSeqiNP_391148.1. NC_000964.3.
WP_003228604.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15258; CAB15258; BSU32690.
GeneIDi937108.
KEGGibsu:BSU32690.
PATRICi18978514. VBIBacSub10457_3420.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15258.1.
PIRiF70019.
RefSeqiNP_391148.1. NC_000964.3.
WP_003228604.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5J8QX-ray1.70A1-406[»]
ProteinModelPortaliO32164.
SMRiO32164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO32164. 2 interactors.
MINTiMINT-8082716.
STRINGi224308.Bsubs1_010100017736.

Proteomic databases

PaxDbiO32164.
PRIDEiO32164.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15258; CAB15258; BSU32690.
GeneIDi937108.
KEGGibsu:BSU32690.
PATRICi18978514. VBIBacSub10457_3420.

Phylogenomic databases

eggNOGiENOG4105C9B. Bacteria.
COG0520. LUCA.
HOGENOMiHOG000017511.
InParanoidiO32164.
KOiK11717.
OMAiMIDFVGL.
PhylomeDBiO32164.

Enzyme and pathway databases

BioCyciBSUB:BSU32690-MONOMER.

Family and domain databases

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

Entry informationi

Entry nameiSUFS_BACSU
AccessioniPrimary (citable) accession number: O32164
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 112 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, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.