Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O29689

- ISCS2_ARCFU

UniProt

O29689 - ISCS2_ARCFU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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: 4 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 PublicationsCurated

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate2 PublicationsUniRule annotationNote: Cofactor affinity is increased in an IscS-IscU complex.2 PublicationsUniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 701Pyridoxal phosphate
Binding sitei149 – 1491Pyridoxal phosphate
Binding sitei234 – 2341Pyridoxal phosphate
Active sitei321 – 3211Cysteine persulfide intermediateCurated
Metal bindingi321 – 3211Iron-sulfur (2Fe-2S)

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.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine desulfurase IscS 2UniRule 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: Chromosome

Subcellular locationi

GO - Cellular componenti

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

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

Homodimer. Forms a heterotetramer with IscU.1 Publication

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[»]
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.
OMAiALKGLYW.

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:January 1, 1998 - 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 .
PIRi D69320.
RefSeqi NP_069398.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4EB5 X-ray 2.53 A/B 1-382 [» ]
4EB7 X-ray 2.75 A/B 1-382 [» ]
4HVK X-ray 1.43 A 1-382 [» ]
ProteinModelPortali O29689.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224325.AF0564.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB90671 ; AAB90671 ; AF_0564 .
GeneIDi 1483780.
KEGGi afu:AF0564.

Phylogenomic databases

eggNOGi COG1104.
KOi K04487.
OMAi ALKGLYW.

Enzyme and pathway databases

BioCyci AFUL224325:GJBC-577-MONOMER.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPi MF_00331. Cys_desulf_IscS.
InterProi IPR000192. 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 ]
Pfami PF00266. Aminotran_5. 1 hit.
[Graphical view ]
PIRSFi PIRSF005572. NifS. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
ProtoNeti Search...

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(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.

Entry informationi

Entry nameiISCS2_ARCFU
AccessioniPrimary (citable) accession number: O29689
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 94 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3