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Protein

Cysteine desulfurase IscS 2

Gene

iscS2

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation2 PublicationsNote: Cofactor affinity is increased in an IscS-IscU complex.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 701Pyridoxal phosphateUniRule annotation2 Publications
Binding sitei149 – 1491Pyridoxal phosphateUniRule annotation2 Publications
Binding sitei234 – 2341Pyridoxal phosphateUniRule annotation1 Publication
Active sitei321 – 3211Cysteine persulfide intermediateUniRule annotation1 Publication
Metal bindingi321 – 3211Iron-sulfur (2Fe-2S); via persulfide group; shared with IscUUniRule annotation1 Publication

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. cysteine desulfurase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW
  4. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. cysteine metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-577-MONOMER.
BRENDAi2.8.1.7. 414.
UniPathwayiUPA00266.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine desulfurase IscS 21 PublicationUniRule annotation (EC:2.8.1.7UniRule annotation)
Gene namesi
Name:iscS2UniRule annotation
Ordered Locus Names:AF_0564
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
ProteomesiUP000002199 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi321 – 3211C → S: No iron-sulfur cluster assembly. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382Cysteine desulfurase IscS 2PRO_0000150288Add
BLAST

Interactioni

Subunit structurei

Forms a heterotetramer with IscU, interacts with other sulfur acceptors.UniRule annotation2 Publications

Protein-protein interaction databases

STRINGi224325.AF0564.

Structurei

Secondary structure

1
382
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni6 – 83Combined sources
Helixi14 – 2512Combined sources
Helixi36 – 5520Combined sources
Beta strandi61 – 688Combined sources
Helixi69 – 8416Combined sources
Helixi85 – 873Combined sources
Beta strandi90 – 945Combined sources
Helixi99 – 11012Combined sources
Beta strandi114 – 1185Combined sources
Helixi128 – 1347Combined sources
Beta strandi139 – 1435Combined sources
Turni149 – 1513Combined sources
Helixi157 – 1648Combined sources
Beta strandi165 – 1739Combined sources
Turni175 – 1773Combined sources
Helixi185 – 1884Combined sources
Beta strandi191 – 1977Combined sources
Helixi198 – 2003Combined sources
Beta strandi207 – 2126Combined sources
Helixi227 – 2293Combined sources
Helixi237 – 27236Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi284 – 2874Combined sources
Beta strandi291 – 2966Combined sources
Helixi301 – 31010Combined sources
Helixi320 – 3223Combined sources
Beta strandi323 – 3253Combined sources
Helixi330 – 3345Combined sources
Helixi339 – 3435Combined sources
Beta strandi345 – 3495Combined sources
Helixi356 – 37520Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EB5X-ray2.53A/B1-382[»]
4EB7X-ray2.75A/B1-382[»]
4HVKX-ray1.43A1-382[»]
4R5FX-ray1.90A1-382[»]
ProteinModelPortaliO29689.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1104.
KOiK04487.
OMAiHVIRAMK.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00331. Cys_desulf_IscS.
InterProiIPR000192. Aminotrans_V_dom.
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]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF005572. NifS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

O29689-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYFDYTSAK PVDERVLEAM LPYMTESFGN PSSVHSYGFK AREAVQEARE
60 70 80 90 100
KVAKLVNGGG GTVVFTSGAT EANNLAIIGY AMRNARKGKH ILVSAVEHMS
110 120 130 140 150
VINPAKFLQK QGFEVEYIPV GKYGEVDVSF IDQKLRDDTI LVSVQHANNE
160 170 180 190 200
IGTIQPVEEI SEVLAGKAAL HIDATASVGQ IEVDVEKIGA DMLTISSNDI
210 220 230 240 250
YGPKGVGALW IRKEAKLQPV ILGGGQENGL RSGSENVPSI VGFGKAAEIT
260 270 280 290 300
AMEWREEAER LRRLRDRIID NVLKIEESYL NGHPEKRLPN NVNVRFSYIE
310 320 330 340 350
GESIVLSLDM AGIQASTGSA CSSKTLQPSH VLMACGLKHE EAHGTLLLTL
360 370 380
GRYNTDEDVD RLLEVLPGVI ERLRSMSPLY RR
Length:382
Mass (Da):41,824
Last modified:December 31, 1997 - v1
Checksum:i3B2A25229124C02A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90671.1.
PIRiD69320.
RefSeqiNP_069398.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB90671; AAB90671; AF_0564.
GeneIDi1483780.
KEGGiafu:AF0564.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90671.1.
PIRiD69320.
RefSeqiNP_069398.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EB5X-ray2.53A/B1-382[»]
4EB7X-ray2.75A/B1-382[»]
4HVKX-ray1.43A1-382[»]
4R5FX-ray1.90A1-382[»]
ProteinModelPortaliO29689.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF0564.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB90671; AAB90671; AF_0564.
GeneIDi1483780.
KEGGiafu:AF0564.

Phylogenomic databases

eggNOGiCOG1104.
KOiK04487.
OMAiHVIRAMK.

Enzyme and pathway databases

UniPathwayiUPA00266.
BioCyciAFUL224325:GJBC-577-MONOMER.
BRENDAi2.8.1.7. 414.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00331. Cys_desulf_IscS.
InterProiIPR000192. Aminotrans_V_dom.
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]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF005572. NifS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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(1996) [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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S) UNDER REDUCING AND OXIDIZING CONDITIONS AND PYRIDOXAL PHOSPHATE, 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(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE ANALOG, FUNCTION, COFACTOR, PROBABLE ACTIVE SITE, MUTAGENESIS OF CYS-321, SUBUNIT.
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Entry informationi

Entry nameiISCS2_ARCFU
AccessioniPrimary (citable) accession number: O29689
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2001
Last sequence update: December 31, 1997
Last modified: March 31, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In Archaea the pyridoxal phosphate cofactor is not covalently bound to Lys but ligated by other amino acids.UniRule annotation

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.