ISU1_DEBHA
ID ISU1_DEBHA Reviewed; 179 AA.
AC Q6BGU0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-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=DEHA2G23958g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382139; CAG91094.1; -; Genomic_DNA.
DR RefSeq; XP_462581.1; XM_462581.1.
DR AlphaFoldDB; Q6BGU0; -.
DR SMR; Q6BGU0; -.
DR STRING; 4959.XP_462581.1; -.
DR EnsemblFungi; CAG91094; CAG91094; DEHA2G23958g.
DR GeneID; 2905540; -.
DR KEGG; dha:DEHA2G23958g; -.
DR VEuPathDB; FungiDB:DEHA2G23958g; -.
DR eggNOG; KOG3361; Eukaryota.
DR HOGENOM; CLU_079283_1_2_1; -.
DR InParanoid; Q6BGU0; -.
DR OMA; YKNPRNY; -.
DR OrthoDB; 1406557at2759; -.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000000599; Chromosome G.
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: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; 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 ?..179
FT /note="Iron sulfur cluster assembly protein 1,
FT mitochondrial"
FT /id="PRO_0000019696"
FT REGION 160..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 179 AA; 19439 MW; C4C00DFF70C0B955 CRC64;
MISRSFLRLA NPARRAMPAV KRVNMMPSMA LPTKRLYHEK VLDHYSNPRN VGTLNKLDVD
VGTGLVGAPA CGDVMRLQIQ VDDETGVIKD VKFKTFGCGS AIASSSYLTE LVKGKTIEEA
VKIKNTAIAK ELSLPPVKLH CSMLAEDAIK SAVKDYRSKR SVKQPTLGPE AAQAETIAT
