ISCU2_ARCFU
ID ISCU2_ARCFU Reviewed; 153 AA.
AC P0DMG2; O34393;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU 2;
DE AltName: Full=Sulfur acceptor protein IscU 2;
GN Name=iscU2; OrderedLocusNames=AF_0565;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S)
RP UNDER REDUCING AND OXIDIZING CONDITIONS, FUNCTION, SUBUNIT, AND MUTAGENESIS
RP OF ASP-35.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=22511353; DOI=10.1002/anie.201201708;
RA Marinoni E.N., de Oliveira J.S., Nicolet Y., Raulfs E.C., Amara P.,
RA Dean D.R., Fontecilla-Camps J.C.;
RT "(IscS-IscU)2 complex structures provide insights into Fe2S2 biogenesis and
RT transfer.";
RL Angew. Chem. Int. Ed. 51:5439-5442(2012).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF ASP-35.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=23160436; DOI=10.1039/c2dt32101g;
RA Yamanaka Y., Zeppieri L., Nicolet Y., Marinoni E.N., de Oliveira J.S.,
RA Odaka M., Dean D.R., Fontecilla-Camps J.C.;
RT "Crystal structure and functional studies of an unusual L-cysteine
RT desulfurase from Archaeoglobus fulgidus.";
RL Dalton Trans. 42:3092-3099(2013).
CC -!- FUNCTION: A scaffold on which IscS assembles Fe-S clusters.
CC Subsequently gives the nascent cluster to other proteins. Binds 1 2Fe-
CC 2S cluster per subunit in a crystal formed under reducing conditions;
CC this subunit provides 3 ligands while IscS2 provides the other ligand.
CC It is likely that Fe-S cluster coordination is flexible as the role of
CC this complex is to build and then hand off Fe-S clusters.
CC {ECO:0000269|PubMed:22511353, ECO:0000269|PubMed:23160436}.
CC -!- SUBUNIT: Forms a heterotetramer with IscS2.
CC {ECO:0000269|PubMed:22511353}.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000782; AAB91040.1; -; Genomic_DNA.
DR PIR; A69273; A69273.
DR RefSeq; WP_010877697.1; NC_000917.1.
DR PDB; 4EB5; X-ray; 2.53 A; C/D=1-153.
DR PDB; 4EB7; X-ray; 2.75 A; C=1-153.
DR PDBsum; 4EB5; -.
DR PDBsum; 4EB7; -.
DR AlphaFoldDB; P0DMG2; -.
DR SMR; P0DMG2; -.
DR EnsemblBacteria; AAB91040; AAB91040; AF_0185.
DR GeneID; 24794105; -.
DR KEGG; afu:AF_0185; -.
DR HOGENOM; CLU_079283_5_1_2; -.
DR OMA; HKKVIDH; -.
DR OrthoDB; 89731at2157; -.
DR PhylomeDB; P0DMG2; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR CDD; cd06664; IscU_like; 1.
DR InterPro; IPR017787; NIF_FeS_clus_asmbl_NifU-like.
DR InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N.
DR PANTHER; PTHR10093; PTHR10093; 1.
DR Pfam; PF01592; NifU_N; 1.
DR TIGRFAMs; TIGR03419; NifU_clost; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..153
FT /note="Iron-sulfur cluster assembly scaffold protein IscU
FT 2"
FT /id="PRO_0000428755"
FT BINDING 33
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared with IscS"
FT /evidence="ECO:0007744|PDB:4EB5"
FT BINDING 58
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared with IscS"
FT /evidence="ECO:0007744|PDB:4EB5"
FT BINDING 101
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared with IscS"
FT /evidence="ECO:0007744|PDB:4EB5"
FT BINDING 102
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared with IscS"
FT /evidence="ECO:0007744|PDB:4EB5"
FT MUTAGEN 35
FT /note="D->A: Generates an iron-sulfur cluster containing
FT IscS-IscU complex that does not dissociate."
FT /evidence="ECO:0000269|PubMed:22511353,
FT ECO:0000269|PubMed:23160436"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:4EB5"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:4EB5"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:4EB5"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:4EB5"
FT STRAND 36..57
FT /evidence="ECO:0007829|PDB:4EB5"
FT HELIX 59..72
FT /evidence="ECO:0007829|PDB:4EB5"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:4EB5"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:4EB5"
FT HELIX 100..120
FT /evidence="ECO:0007829|PDB:4EB5"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:4EB5"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:4EB5"
SQ SEQUENCE 153 AA; 16920 MW; ABC2DD8023EE8185 CRC64;
MYSDKVFDHF QNPRNVGKIE DADGVGTVGN PVCGDLMTIY IKVKDNRIED IKFQTFGCAA
AIATSSMATE MAKGKTIEEA LKITRDAVAE ALGGLPKQKM HCSNLAADAL RRAIVDYFRK
NGKIDKIKEL GLEKELEKME KGEMDDHGEY CEA
