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O29689 (ISCS2_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cysteine desulfurase IscS 2

EC=2.8.1.7
Gene names
Name:iscS2
Ordered Locus Names:AF_0564
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the removal of elemental sulfur from cysteine to produce alanine Probable. Binds 1 2Fe-2S cluster per subunit in a crystal formed under reducing conditions; this subunit provides 1 ligand while IscU provides the other 3 ligands. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. Ref.2 Ref.3

Catalytic activity

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. HAMAP-Rule MF_00331

Cofactor

Pyridoxal phosphate. Cofactor affinity is increased in an IscS-IscU complex. Ref.2 Ref.3

Subunit structure

Homodimer. Forms a heterotetramer with IscU. Ref.2

Sequence similarities

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Cysteine desulfurase IscS 2 HAMAP-Rule MF_00331
PRO_0000150288

Sites

Active site3211Cysteine persulfide intermediate Probable
Metal binding3211Iron-sulfur (2Fe-2S)
Binding site701Pyridoxal phosphate
Binding site1491Pyridoxal phosphate
Binding site2341Pyridoxal phosphate

Experimental info

Mutagenesis3211C → S: No Fe-S cluster assembly. Ref.3

Secondary structure

.......................................................... 382
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O29689 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 3B2A25229124C02A

FASTA38241,824
        10         20         30         40         50         60 
MAYFDYTSAK PVDERVLEAM LPYMTESFGN PSSVHSYGFK AREAVQEARE KVAKLVNGGG 

        70         80         90        100        110        120 
GTVVFTSGAT EANNLAIIGY AMRNARKGKH ILVSAVEHMS VINPAKFLQK QGFEVEYIPV 

       130        140        150        160        170        180 
GKYGEVDVSF IDQKLRDDTI LVSVQHANNE IGTIQPVEEI SEVLAGKAAL HIDATASVGQ 

       190        200        210        220        230        240 
IEVDVEKIGA DMLTISSNDI YGPKGVGALW IRKEAKLQPV ILGGGQENGL RSGSENVPSI 

       250        260        270        280        290        300 
VGFGKAAEIT AMEWREEAER LRRLRDRIID NVLKIEESYL NGHPEKRLPN NVNVRFSYIE 

       310        320        330        340        350        360 
GESIVLSLDM AGIQASTGSA CSSKTLQPSH VLMACGLKHE EAHGTLLLTL GRYNTDEDVD 

       370        380 
RLLEVLPGVI ERLRSMSPLY RR 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. expand/collapse author list , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]"(IscS-IscU)2 complex structures provide insights into Fe2S2 biogenesis and transfer."
Marinoni E.N., de Oliveira J.S., Nicolet Y., Raulfs E.C., Amara P., Dean D.R., Fontecilla-Camps J.C.
Angew. Chem. Int. Ed. 51:5439-5442(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S) UNDER REDUCING AND OXIDIZING CONDITIONS, FUNCTION, COFACTOR, SUBUNIT.
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[3]"Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus."
Yamanaka Y., Zeppieri L., Nicolet Y., Marinoni E.N., de Oliveira J.S., Odaka M., Dean D.R., Fontecilla-Camps J.C.
Dalton Trans. 42:3092-3099(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS), FUNCTION, COFACTOR, PROBABLE ACTIVE SITE, MUTAGENESIS OF CYS-321.
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000782 Genomic DNA. Translation: AAB90671.1.
PIRD69320.
RefSeqNP_069398.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4EB5X-ray2.53A/B1-382[»]
4EB7X-ray2.75A/B1-382[»]
4HVKX-ray1.43A1-382[»]
ProteinModelPortalO29689.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224325.AF0564.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB90671; AAB90671; AF_0564.
GeneID1483780.
KEGGafu:AF0564.

Phylogenomic databases

eggNOGCOG1104.
KOK04487.
OMASAMFANN.
ProtClustDBCLSK541355.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-577-MONOMER.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00331. Cys_desulf_aminotr_5.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010240. Cys_deSase.
IPR016454. Cysteine_dSase_NifS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF005572. NifS. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameISCS2_ARCFU
AccessionPrimary (citable) accession number: O29689
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references