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O29689

- ISCS2_ARCFU

UniProt

O29689 - ISCS2_ARCFU

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
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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 phosphate. 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

    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

    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 – 83
    Helixi14 – 2512
    Helixi36 – 5520
    Beta strandi61 – 688
    Helixi69 – 8416
    Helixi85 – 873
    Beta strandi90 – 945
    Helixi99 – 11012
    Beta strandi114 – 1185
    Helixi128 – 1347
    Beta strandi139 – 1435
    Turni149 – 1513
    Helixi157 – 1648
    Beta strandi165 – 1739
    Turni175 – 1773
    Helixi185 – 1884
    Beta strandi191 – 1977
    Helixi198 – 2003
    Beta strandi207 – 2126
    Helixi227 – 2293
    Helixi237 – 27236
    Beta strandi278 – 2803
    Beta strandi284 – 2874
    Beta strandi291 – 2966
    Helixi301 – 31010
    Helixi320 – 3223
    Beta strandi323 – 3253
    Helixi330 – 3345
    Helixi339 – 3435
    Beta strandi345 – 3495
    Helixi356 – 37520

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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/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]
    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

    MAYFDYTSAK PVDERVLEAM LPYMTESFGN PSSVHSYGFK AREAVQEARE    50
    KVAKLVNGGG GTVVFTSGAT EANNLAIIGY AMRNARKGKH ILVSAVEHMS 100
    VINPAKFLQK QGFEVEYIPV GKYGEVDVSF IDQKLRDDTI LVSVQHANNE 150
    IGTIQPVEEI SEVLAGKAAL HIDATASVGQ IEVDVEKIGA DMLTISSNDI 200
    YGPKGVGALW IRKEAKLQPV ILGGGQENGL RSGSENVPSI VGFGKAAEIT 250
    AMEWREEAER LRRLRDRIID NVLKIEESYL NGHPEKRLPN NVNVRFSYIE 300
    GESIVLSLDM AGIQASTGSA CSSKTLQPSH VLMACGLKHE EAHGTLLLTL 350
    GRYNTDEDVD RLLEVLPGVI ERLRSMSPLY RR 382
    Length:382
    Mass (Da):41,824
    Last modified:January 1, 1998 - v1
    Checksum:i3B2A25229124C02A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000782 Genomic DNA. Translation: AAB90671.1 .
    PIRi D69320.
    RefSeqi NP_069398.1. NC_000917.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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/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 ]
    Pfami PF00266. Aminotran_5. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005572. NifS. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 92 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