ID   ISU1_KLULA              Reviewed;         180 AA.
AC   Q6CRQ9;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Iron sulfur cluster assembly protein 1, mitochondrial;
DE   AltName: Full=Iron sulfur cluster scaffold protein 1;
DE   Flags: Precursor;
GN   Name=ISU1; OrderedLocusNames=KLLA0D07161g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Scaffold protein for the de novo synthesis of iron-sulfur
CC       (Fe-S) clusters within mitochondria, which is required for maturation
CC       of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins.
CC       First, a [2Fe-2S] cluster is transiently assembled on the scaffold
CC       protein ISU1. In a second step, the cluster is released from ISU1,
CC       transferred to a glutaredoxin, followed by the formation of
CC       mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and
CC       their target-specific insertion into the recipient apoproteins. Cluster
CC       assembly on ISU1 depends on the function of the cysteine desulfurase
CC       complex NFS1-ISD11, which serves as the sulfur donor for cluster
CC       synthesis, the iron-binding protein frataxin as the putative iron
CC       donor, and the electron transfer chain comprised of ferredoxin
CC       reductase and ferredoxin, which receive their electrons from NADH.
CC       {ECO:0000250|UniProtKB:Q03020}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:Q9UTC6};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:Q9UTC6};
CC   -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC       {ECO:0000250|UniProtKB:Q03020}.
CC   -!- SUBUNIT: Component of the core Fe-S cluster (ISC) assembly machinery.
CC       {ECO:0000250|UniProtKB:Q03020}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q03020}.
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; CR382124; CAH00476.1; -; Genomic_DNA.
DR   RefSeq; XP_453380.1; XM_453380.1.
DR   AlphaFoldDB; Q6CRQ9; -.
DR   SMR; Q6CRQ9; -.
DR   STRING; 28985.XP_453380.1; -.
DR   EnsemblFungi; CAH00476; CAH00476; KLLA0_D07161g.
DR   GeneID; 2893074; -.
DR   KEGG; kla:KLLA0_D07161g; -.
DR   eggNOG; KOG3361; Eukaryota.
DR   HOGENOM; CLU_079283_1_2_1; -.
DR   InParanoid; Q6CRQ9; -.
DR   OMA; YKNPRNY; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0001671; F:ATPase activator activity; IEA:EnsemblFungi.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:EnsemblFungi.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:EnsemblFungi.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:EnsemblFungi.
DR   CDD; cd06664; IscU_like; 1.
DR   InterPro; IPR011339; ISC_FeS_clus_asmbl_IscU.
DR   InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N.
DR   PANTHER; PTHR10093; PTHR10093; 1.
DR   Pfam; PF01592; NifU_N; 1.
DR   TIGRFAMs; TIGR01999; iscU; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..180
FT                   /note="Iron sulfur cluster assembly protein 1,
FT                   mitochondrial"
FT                   /id="PRO_0000019697"
SQ   SEQUENCE   180 AA;  19093 MW;  9D4174999B875D47 CRC64;
     MFRGQMFAVQ RMGSALMHGG GGGTRIIGVA AARATAPTVG SSPSMASARF YHPKVIDHYT
     NPRNVGSLDK NLPNVGTGLV GAPACGDVMK LQIQVNDETG VIENVKFKTF GCGSAIASSS
     YMTELVRGKT LEDAAKIKNT EIARELSLPP VKLHCSMLAE DAIKAAIKDY QAKRPTTQLK