ID   ISU1_SCHPO              Reviewed;         192 AA.
AC   Q9UTC6;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
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; ORFNames=SPAC227.13c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   COFACTOR, AND SUBUNIT.
RX   PubMed=11939799; DOI=10.1021/bi016073s;
RA   Wu G., Mansy S.S., Wu S.-P., Surerus K.K., Foster M.W., Cowan J.A.;
RT   "Characterization of an iron-sulfur cluster assembly protein (ISU1) from
RT   Schizosaccharomyces pombe.";
RL   Biochemistry 41:5024-5032(2002).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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:0000269|PubMed:11939799};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000269|PubMed:11939799};
CC   -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC       {ECO:0000250|UniProtKB:Q03020}.
CC   -!- SUBUNIT: Homodimer (PubMed:11939799). Component of the core Fe-S
CC       cluster (ISC) assembly machinery (By similarity).
CC       {ECO:0000250|UniProtKB:Q03020, ECO:0000269|PubMed:11939799}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC       Mitochondrion matrix {ECO:0000250|UniProtKB:Q03020}.
CC   -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB61462.1; -; Genomic_DNA.
DR   PIR; T50169; T50169.
DR   RefSeq; NP_592967.1; NM_001018367.2.
DR   AlphaFoldDB; Q9UTC6; -.
DR   SMR; Q9UTC6; -.
DR   BioGRID; 278014; 14.
DR   IntAct; Q9UTC6; 4.
DR   STRING; 4896.SPAC227.13c.1; -.
DR   MaxQB; Q9UTC6; -.
DR   PaxDb; Q9UTC6; -.
DR   PRIDE; Q9UTC6; -.
DR   EnsemblFungi; SPAC227.13c.1; SPAC227.13c.1:pep; SPAC227.13c.
DR   GeneID; 2541513; -.
DR   KEGG; spo:SPAC227.13c; -.
DR   PomBase; SPAC227.13c; isu1.
DR   VEuPathDB; FungiDB:SPAC227.13c; -.
DR   eggNOG; KOG3361; Eukaryota.
DR   HOGENOM; CLU_079283_1_2_1; -.
DR   InParanoid; Q9UTC6; -.
DR   OMA; YKNPRNY; -.
DR   PhylomeDB; Q9UTC6; -.
DR   Reactome; R-SPO-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR   UniPathway; UPA00266; -.
DR   PRO; PR:Q9UTC6; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:PomBase.
DR   GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IDA:PomBase.
DR   GO; GO:0140132; F:iron-sulfur cluster carrier activity; IDA:PomBase.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; IDA:PomBase.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:PomBase.
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   1: Evidence at protein level;
KW   2Fe-2S; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..53
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           54..192
FT                   /note="Iron sulfur cluster assembly protein 1,
FT                   mitochondrial"
FT                   /id="PRO_0000019698"
SQ   SEQUENCE   192 AA;  20616 MW;  4D956BF1D4CE78D8 CRC64;
     MSVFRRSVQC VGVLPSILAQ RSSLLARPAN LQFLKTNSSK FVPQVTANVS RRMYHKNVLD
     HYNNPRNVGT LPKGDPDVGI GLVGAPACGD VMRLAIRVNK DGVIEDVKFK TFGCGSAIAS
     SSYVTTMVKG MTLEEASKIK NTQIAKELCL PPVKLHCSML AEDAIKSAVK HYRSKQLTPV
     GTTAGAIESA TA