ID   ISU1_CANGA              Reviewed;         213 AA.
AC   Q6FJY3;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=CAGL0M02629g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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}.
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DR   EMBL; CR380959; CAG62437.1; -; Genomic_DNA.
DR   RefSeq; XP_449461.1; XM_449461.1.
DR   AlphaFoldDB; Q6FJY3; -.
DR   SMR; Q6FJY3; -.
DR   STRING; 5478.XP_449461.1; -.
DR   EnsemblFungi; CAG62437; CAG62437; CAGL0M02629g.
DR   GeneID; 2891469; -.
DR   KEGG; cgr:CAGL0M02629g; -.
DR   CGD; CAL0136631; CAGL0M02629g.
DR   VEuPathDB; FungiDB:CAGL0M02629g; -.
DR   eggNOG; KOG3361; Eukaryota.
DR   HOGENOM; CLU_079283_1_0_1; -.
DR   InParanoid; Q6FJY3; -.
DR   OMA; NNIGRRM; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000002428; Chromosome M.
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           ?..213
FT                   /note="Iron sulfur cluster assembly protein 1,
FT                   mitochondrial"
FT                   /id="PRO_0000019695"
SQ   SEQUENCE   213 AA;  22901 MW;  CC698703E5A99823 CRC64;
     MGVCVFFPLC LPCPGALTYI REAQFISSWT PADPRHKQLK MFLQRFVTVG GAAIGARSTM
     GAMGAIGAIG AKGTMNNIGR RMYHPKVIEH YTHPRNVGSM DKTLPNVGTG LVGAPACGDV
     MRLQIKVNDK TGVIEDVKFK TFGCGSAIAS SSYMTELVHG MTLDDAAKIK NTTIAKELSL
     PPVKLHCSML AEDAIKAAIK DYKSKRTSTT TLH