ISCU_AQUAE
ID ISCU_AQUAE Reviewed; 157 AA.
AC O67045;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU;
DE AltName: Full=Sulfur acceptor protein IscU;
GN Name=iscU; Synonyms=nifU; OrderedLocusNames=aq_896;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP SUBUNIT, BINDING OF 2FE-2S CLUSTER, AND MUTAGENESIS OF ASP-38;
RP 140-GLU--THR-157 AND 130-GLU--THR-157.
RC STRAIN=VF5;
RX PubMed=17846064; DOI=10.1093/jb/mvm163;
RA Shimomura Y., Kamikubo H., Nishi Y., Masako T., Kataoka M., Kobayashi Y.,
RA Fukuyama K., Takahashi Y.;
RT "Characterization and crystallization of an IscU-type scaffold protein with
RT bound [2Fe-2S] cluster from the hyperthermophile, aquifex aeolicus.";
RL J. Biochem. 142:577-586(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S),
RP SUBUNIT, AND MUTAGENESIS OF ASP-38.
RC STRAIN=VF5;
RX PubMed=18723024; DOI=10.1016/j.jmb.2008.08.015;
RA Shimomura Y., Wada K., Fukuyama K., Takahashi Y.;
RT "The asymmetric trimeric architecture of [2Fe-2S] IscU: implications for
RT its scaffolding during iron-sulfur cluster biosynthesis.";
RL J. Mol. Biol. 383:133-143(2008).
CC -!- FUNCTION: A scaffold on which IscS assembles Fe-S clusters.
CC Subsequently gives the nascent cluster to other proteins. It is likely
CC that Fe-S cluster coordination is flexible as the role of this complex
CC is to build and then hand off Fe-S clusters (Probable). {ECO:0000305}.
CC -!- SUBUNIT: Homotrimer upon overexpression in E.coli and in crystal
CC structure. The trimer binds Fe-S clusters, upon exposure to air it
CC loses the clusters and concomitantly dissociates into monomers and
CC dimers. {ECO:0000269|PubMed:17846064, ECO:0000269|PubMed:18723024}.
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; AE000657; AAC07015.1; -; Genomic_DNA.
DR PIR; B70377; B70377.
DR RefSeq; NP_213607.1; NC_000918.1.
DR RefSeq; WP_010880545.1; NC_000918.1.
DR PDB; 2Z7E; X-ray; 2.30 A; A/B/C=1-157.
DR PDBsum; 2Z7E; -.
DR AlphaFoldDB; O67045; -.
DR SMR; O67045; -.
DR STRING; 224324.aq_896; -.
DR PRIDE; O67045; -.
DR EnsemblBacteria; AAC07015; AAC07015; aq_896.
DR KEGG; aae:aq_896; -.
DR PATRIC; fig|224324.8.peg.697; -.
DR eggNOG; COG0822; Bacteria.
DR HOGENOM; CLU_079283_5_1_0; -.
DR InParanoid; O67045; -.
DR OMA; YKNPRNY; -.
DR OrthoDB; 1793654at2; -.
DR EvolutionaryTrace; O67045; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR CDD; cd06664; IscU_like; 1.
DR InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N.
DR PANTHER; PTHR10093; PTHR10093; 1.
DR Pfam; PF01592; NifU_N; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..157
FT /note="Iron-sulfur cluster assembly scaffold protein IscU"
FT /id="PRO_0000166179"
FT REGION 137..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared with IscS"
FT /evidence="ECO:0000250|UniProtKB:P0DMG2,
FT ECO:0000269|PubMed:18723024"
FT BINDING 63
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared with IscS"
FT /evidence="ECO:0000250|UniProtKB:P0DMG2,
FT ECO:0000269|PubMed:18723024"
FT BINDING 106
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared with IscS"
FT /evidence="ECO:0000250|UniProtKB:P0DMG2,
FT ECO:0000269|PubMed:18723024"
FT BINDING 107
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared with IscS"
FT /evidence="ECO:0000250|UniProtKB:P0DMG2,
FT ECO:0000269|PubMed:18723024"
FT MUTAGEN 38
FT /note="D->A: Stabilizes 2Fe-2S cluster binding, prolongs
FT its half-life in air."
FT /evidence="ECO:0000269|PubMed:17846064,
FT ECO:0000269|PubMed:18723024"
FT MUTAGEN 130..157
FT /note="Missing: No effect on 2Fe-2S cluster."
FT /evidence="ECO:0000269|PubMed:17846064"
FT MUTAGEN 140..157
FT /note="Missing: No effect on 2Fe-2S cluster."
FT /evidence="ECO:0000269|PubMed:17846064"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:2Z7E"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:2Z7E"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:2Z7E"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:2Z7E"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:2Z7E"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2Z7E"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:2Z7E"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:2Z7E"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:2Z7E"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:2Z7E"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:2Z7E"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2Z7E"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:2Z7E"
SQ SEQUENCE 157 AA; 17531 MW; D684A725D4E03217 CRC64;
MSFEYNEKVL DHFLNPRNVG VLEDANGVGQ CGNPACGDAM LFTIKVNPEN DVIEDVRFKT
FGCGSAIAVS SMLTEMVKGK PIQYALNLTY KDIFEELGGL PPQKIHCTNL GLETLHVAIK
DYLMKQGRVE EASKIPDCYE EEEEQEESKE FEFLSGT
